ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
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stringlengths 108
11.1k
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Q9JXY2 | MSFKTDAEIAQSSTMRPIGEIAAKLGLNADNIEPYGHYKAKINPAEAFKLPQKQGRLILVTAINPTPAGEGKTTVTIGLADALRHIGKDAVIALREPSLGPVFGVKGGAAGGGYAQVLPMEDINLHFTGDFHAIGAANNLLAAMLDNHIYQGNELNIDPKRVLWRRVVDMNDRQLRNIIDGMGKPVDGVMRPDGFDITVASEVMAVFCLAKDISDLKERLGNILVAYAKDGSPVYAKDLKANGAMAALLKDAIKPNLVQTIEGTPAFVHGGPFANIAHGCNSVTATRLAKHLADYAVTEAGFGADLGAEKFCDIKCRLAGLKPDAAVVVATVRALKYNGGVERANLGEENLDALEKGLPNLLKHISNLKNVFGLPVVVALNRFVSDADAELAMIEKACAEHGVEVSLTEVWGKGGAGGADLARKVVNAIESQTNNFGFAYDVELGIKDKIRAIAQKVYGAEDVDFSAEASAEIASLEKLGLDKMPICMAKTQYSLSDNAKLLGCPEDFRIAVRGITVSAGAGFIVALCGNMMKMPGLPKVPAAEKIDVDAEGVIHGLF | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 59062
Sequence Length: 558
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
|
Q04FS6 | MKSDIEIDHSIKALPITEIGKQIGLSDSQLIPYGHDKAKIDAYSIANMPRQGKLVLVTSINPTPAGEGKTTVTIGLVDAINRLGKSAIGALREPSMGPVFGLKGGATGGGYAQVIPMEDINLHFTGDIHAVSAAHNLLAAVIDNHLHQGNELKIDPENIYWRRVLDMNDRALRQITLGKGRVNGPERNSGFDITASSEIMAVLTLSKNLFDLKKRLSRIVVALDVQGKPVTVADLKVAGALTAILKDAINPNLVQSLEHSPFIIHGGPFANIAQGTNSVVATDAALKLADFAVTEAGFGSDLGGEKFMDVKVPVLGKEPDAVVIVATVKALKFHGGVALDHLSDKNVDAVRNGLDNLNRHLEAMTHYGKPVVVALNKFLDDDMEEIQLIKNFVEGEKKLQFEIVTSFVDGFEGSLDLAKKVIEATDNQRFFMPLYQADDSIENKIQTIVEKIYGGKDFELSDRAKKDLAEVKENGWGKLPVVIAKTPNSLTDDSKIHGAPTGFTIHIRRFIPKIGAGFIVAMAGKVLMMPGLGKNPAAEKIDVDENGKISGLS | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 59483
Sequence Length: 553
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
|
Q5XZD9 | MKTDVQIAQEAKMLPIMEVAKQIGLGEDDIELYGKYKAKISLDVYKRLADKPDGKLVLVTAINPTPAGEGKTTTNVGLSMGLNKIGKKTITALNEPSLGPCFGVKGGAAGGGYAQVVPMDDINLHFTGDIHAITTAHNLLAALMDNHIKQGNALGIDINKITWKRVLDMNDRALRDIVIGLGGTANGIPRQDGFDITVASEIMAIMCLATSLSDLKDRLSRMIVGYTSRRLAVTADSLTLRGALALLLKDALKPNLVQTLENTPAIIHGGPFANIAHGCNSVTTTKTALKIADYVVTEAGFGADLGAEKFFDIKCRFADLKPDVAVIVATVRALKNHGGVAKANLGAENMKALEDGFGNLERHIENVHKFGVPAVVAINAFPTDTEKELKFVEDACRKLGADVVLSEVWAKGGEGGVELAKKVVEVTEKGAAKFKPLYPAEMPLKQKIETIAKEIYRADGVEFSAKASKELDKFEKLGFGNLPICVAKTQYSFSDNPNLKGAPKGFTVSVSNARISAGAGFIVVLTGDIMTMPGLPKVPAANHMDVLESGEIVGLF | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 59161
Sequence Length: 556
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
|
A9BIV8 | MLSDIEIARSAKLKKIDLIANELDIPEEYYNLYGKNIAKVSHKYLNELNFKNDGNLVMVTAITPTPAGEGKTTTSISLSMALNKIHKRSIVTLREPSLGPVMGIKGGAAGGGYSQVLPMEDINLHFTGDIHAVTSAHNLISAILDDYIKYNKYDIDSTQVSWPRTMDMNDRALREIIVALGGKKNGYPRQDGFIITAASEIMAILCLIENLEDLKKKLSNIVVAKNKKGEPVTVKDLEITGALSVLLKDAINPNLVQTIENTPAFVHGGPFANIAHGTNSILATKLALKLSDYVVTETGFGSDLGGEKFYDFVSPTFGLKPSATVLVATIRALKYHGGQNLKDLNTPNLESLEKGLPNLQVHVENLKKYNIPVVVSLNKFYSDTDEEINMVKDYCDKLGVEVSVNEGFEKGSEGAIDLAEKVVKVSEQQSELKSIYDFKDPLEVKIEKLAKNIYRASKVEYSSEALSTIKFLKKYGYENLPVIVAKTQYSISDDPKKLGFPKDYTFTIRDFELSAGAGFIVALAGDILRMPGLSKVPNAVNMDIDNEGNISGLS | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 60679
Sequence Length: 554
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
|
Q6KZM3 | MKNISEIINIPEDYYDLYGRYIAKVSLNVLDYLKNKRYGKLILVTAMTPTPAGEGKTTTAIGLGNALKLLGKNAGIAIREPSLGPCFGVKGGATGGGKSTVEPSNKINLMFTGDFPAVSAAHNLLSAVINNHMYHGNELKLDPKNIVFPRTIDMDDRSLRSIIVGSGDRSTGVMMNDKYVITAASEVMAILALSRNYNELKQRLGNIMIGYNLNKAPIFARDLKVHGAMASLLVDALRPNIAQTSEHVPAIIHTGPFGNIAHGTSSILGDIIGLKMFDYLVTEAGFGSDLGFEKFIDIVLRLSDFKLSAVVLVATVRAMRYHGGGRINEPDVNAVLRGSENLMWHVQNIKKFGFNPVVAINRHSNDTDAEINAISNILTKNGVEFSISDAYSDGGHGALDLAGKVLKSISDYNPRYIYGINDDPEEKISKIAMNVYNANSVEFSHDAVKTMKLIKDDFSDLYVCMAKTQSSISDNAKLINVPEGFTVKINGININSGSGFIIPLLGNIMTMPGLPRRPASENIDIDDYGNITGLQ | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 58003
Sequence Length: 535
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
|
Q8CNP5 | MLSKELLAALNEQMNQEYFAAHAYMAMAAYCDKESYDGFANFYIEQAKEERFHGKKIYDYINDRGEHAIFDTIKAPKVEFSSILETFKDSLAQERDVTQRFYNLSELARNDKDYATISFLNWFLDEQVEEESTFETHIDYLTRIGDDCNTLYLYEKELAARSFNEQ | Function: Iron-storage protein.
Catalytic Activity: 4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide
Sequence Mass (Da): 19612
Sequence Length: 166
Subcellular Location: Cytoplasm
EC: 1.16.3.2
|
Q9C0B1 | MKRTPTAEEREREAKKLRLLEELEDTWLPYLTPKDDEFYQQWQLKYPKLILREASSVSEELHKEVQEAFLTLHKHGCLFRDLVRIQGKDLLTPVSRILIGNPGCTYKYLNTRLFTVPWPVKGSNIKHTEAEIAAACETFLKLNDYLQIETIQALEELAAKEKANEDAVPLCMSADFPRVGMGSSYNGQDEVDIKSRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVDRSAVAVYSYSCEGPEEESEDDSHLEGRDPDIWHVGFKISWDIETPGLAIPLHQGDCYFMLDDLNATHQHCVLAGSQPRFSSTHRVAECSTGTLDYILQRCQLALQNVCDDVDNDDVSLKSFEPAVLKQGEEIHNEVEFEWLRQFWFQGNRYRKCTDWWCQPMAQLEALWKKMEGVTNAVLHEVKREGLPVEQRNEILTAILASLTARQNLRREWHARCQSRIARTLPADQKPECRPYWEKDDASMPLPFDLTDIVSELRGQLLEAKP | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: RNA demethylase that mediates oxidative demethylation of different RNA species, such as mRNAs, tRNAs and snRNAs, and acts as a regulator of fat mass, adipogenesis and energy homeostasis . Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes . M6A demethylation by FTO affects mRNA expression and stability . Also able to demethylate m6A in U6 small nuclear RNA (snRNA) . Mediates demethylation of N(6),2'-O-dimethyladenosine cap (m6A(m)), by demethylating the N(6)-methyladenosine at the second transcribed position of mRNAs and U6 snRNA . Demethylation of m6A(m) in the 5'-cap by FTO affects mRNA stability by promoting susceptibility to decapping . Also acts as a tRNA demethylase by removing N(1)-methyladenine from various tRNAs . Has no activity towards 1-methylguanine . Has no detectable activity towards double-stranded DNA . Also able to repair alkylated DNA and RNA by oxidative demethylation: demethylates single-stranded RNA containing 3-methyluracil, single-stranded DNA containing 3-methylthymine and has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3-methylcytosine . Ability to repair alkylated DNA and RNA is however unsure in vivo . Involved in the regulation of fat mass, adipogenesis and body weight, thereby contributing to the regulation of body size and body fat accumulation . Involved in the regulation of thermogenesis and the control of adipocyte differentiation into brown or white fat cells . Regulates activity of the dopaminergic midbrain circuitry via its ability to demethylate m6A in mRNAs (By similarity). Plays an oncogenic role in a number of acute myeloid leukemias by enhancing leukemic oncogene-mediated cell transformation: acts by mediating m6A demethylation of target transcripts such as MYC, CEBPA, ASB2 and RARA, leading to promote their expression .
Catalytic Activity: 2-oxoglutarate + a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(N(6),2'-O-dimethyladenosine) in mRNA + O2 = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenosine) in mRNA + CO2 + formaldehyde + succinate
Sequence Mass (Da): 58282
Sequence Length: 505
Domain: The 3D-structure of the Fe2OG dioxygenase domain is similar to that of the Fe2OG dioxygenase domain found in the bacterial DNA repair dioxygenase alkB and its mammalian orthologs, but sequence similarity is very low. As a consequence, the domain is not detected by protein signature databases.
Subcellular Location: Nucleus
|
Q8BGW1 | MKRVQTAEEREREAKKLRLLEELEDTWLPYLTPKDDEFYQQWQLKYPKLVFREAGSIPEELHKEVPEAFLTLHKHGCLFRDVVRIQGKDVLTPVSRILIGDPGCTYKYLNTRLFTVPWPVKGCTVKYTEAEIAAACQTFLKLNDYLQVETIQALEELAVREKANEDAVPLCMAEFPRAGVGPSCDDEVDLKSRAAYNVTLLNFMDPQKMPYLKEEPYFGMGKMAVSWHHDENLVDRSAVAVYSYSCEGSEDESEDESSFEGRDPDTWHVGFKISWDIETPGLTIPLHQGDCYFMLDDLNATHQHCVLAGSQPRFSSTHRVAECSTGTLDYILERCQLALQNVLNDSDDGDVSLKSFDPAVLKQGEEIHNEVEFEWLRQFWFQGNRYKLCTDWWCEPMTHLEGLWKKMESMTNAVLREVKREGLPVEQRSEILSAILVPLTVRQNLRKEWHARCQSRVVRTLPVQQKPDCRPYWEKDDPSMPLPFDLTDVVSELRGQLLEARS | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: RNA demethylase that mediates oxidative demethylation of different RNA species, such as mRNAs, tRNAs and snRNAs, and acts as a regulator of fat mass, adipogenesis and energy homeostasis . Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes . M6A demethylation by FTO affects mRNA expression and stability (By similarity). Also able to demethylate m6A in U6 small nuclear RNA (snRNA) (By similarity). Mediates demethylation of N(6),2'-O-dimethyladenosine cap (m6A(m)), by demethylating the N(6)-methyladenosine at the second transcribed position of mRNAs and U6 snRNA . Demethylation of m6A(m) in the 5'-cap by FTO affects mRNA stability by promoting susceptibility to decapping (By similarity). Also acts as a tRNA demethylase by removing N(1)-methyladenine from various tRNAs (By similarity). Has no activity towards 1-methylguanine (By similarity). Has no detectable activity towards double-stranded DNA (By similarity). Also able to repair alkylated DNA and RNA by oxidative demethylation: demethylates single-stranded RNA containing 3-methyluracil, single-stranded DNA containing 3-methylthymine and has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3-methylcytosine . Ability to repair alkylated DNA and RNA is however unsure in vivo . Involved in the regulation of fat mass, adipogenesis and body weight, thereby contributing to the regulation of body size and body fat accumulation . Involved in the regulation of thermogenesis and the control of adipocyte differentiation into brown or white fat cells . Regulates activity of the dopaminergic midbrain circuitry via its ability to demethylate m6A in mRNAs .
Catalytic Activity: 2-oxoglutarate + a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(N(6),2'-O-dimethyladenosine) in mRNA + O2 = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenosine) in mRNA + CO2 + formaldehyde + succinate
Sequence Mass (Da): 58007
Sequence Length: 502
Domain: The 3D-structure of the Fe2OG dioxygenase domain is similar to that of the Fe2OG dioxygenase domain found in the bacterial DNA repair dioxygenase alkB and its mammalian orthologs, but sequence similarity is very low. As a consequence, the domain is not detected by protein signature databases.
Subcellular Location: Nucleus
|
I1BRD6 | MSQDLFNVPIFFILFRETTEAAIIISVLLSFLKRMFNTESPVYKRLRNQVWIGGAAGLFICLCIGAAFIAVYYTVLNDLWGNSEDIWEGVFSLVAVIMITAMGLAMLKTERMQEKWKVKLAKAMQKSNSEKSSFKEKLQKYAFFVLPFITVLREGLEAVVFIGGVSLGIQGKSIPIAAIMGIICGCLVGFLIYRGGSLIQLRWFFVFSTVVLYLVAAGLMAKGVGYLEQNAWNQVIGGEAADVISYRVSTAVWHVSWGDPEANNDTSGGWQIFNAILGWNNTATYGSIISYCLYWLFVCCYLVFSYFKEKRAAIRKAEAGEWDDGDEALENAKQYIGNDGEFIVEDKESDEEANNHPKEKIESDAIKA | Function: High affinity iron permease required for iron uptake in iron-depleted environments . Required for full virulence in mice .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41125
Sequence Length: 368
Subcellular Location: Cell membrane
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A1URA3 | MNSNFRSLMIWGLIALFLIVLFSFFNGNRQRASNGEVSYSEFLQKIDNNELKTVTIQGQKLTGQTADRRMISTYAPRDPGLVQRLNTNKVNIRAVPESSGNSIFLNLLFSLLPVLIIVGAWIFFMRQMQGGSRGALGFGKSKAKLLTEAQGRVTFKDVAGVEEAKQDLQEIVDFLREPQKFQRLGGRIPRGVLLVGPPGTGKTLLARSIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEPNESIILIAATNRPDVLDPALLRPGRFDRQVVVPNPDVAGREKILEVHVRNVPLAPNVNLRVLARGTPGFSGADLMNLVNEAALMAASRNKKVVTMQEFEDAKDKVMMGAERRSTAMTQEEKELTAYHEAGHAIVALNVPVSDPVHKATIVPRGRALGMVMQLPEGDRYSMSYLWMVSRLAIMMGGRVAEELKFGKENITSGAASDIEQATKLARAMITRWGFSDMLGHVAYGDNQDEIFLGHSVARTQNISEETARMIDAEVRRLIDDAYKTATKILKTQNKQWLALAQGLLEYETLTGTEINEVIAGKPPSRTQGSDTAPLRTSSVPKIGAKNSKGASKSGDAEETEPSVGTKATAASSAKKVVKNASAKSAEKKASGTQVKAATPAATSIKATSAKVASAKAETENVASAQAATENVAMVKAATANVAKKSVESAQADDAEKKRLEEHNKSAHNKKGNLTAGAASNTEDEK | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82521
Sequence Length: 764
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
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B7J0N5 | MNGNNNMNNNGKSNNKKKNKNWILGLVVVFLISAIFMSYFIRGGESYKNVPYSTFQSYLDNGLVESVVIIDKNLIQFVVKGSNFAKSYFSTSIPYLDINLLSELKNKKVELSSGKSQASLIGVLLQTLPWILFFIFFFFIFRQTQGGGGKVFTFGKSNAQKYEAGKNKITFKDVAGQEEVKQELREVVEFLKNPKKFEKIGAKIPKGVLLVGSPGTGKTLLAKAVAGEAGVSFFHMSGSDFVEMFVGVGASRVRDLFDNARKNSPCIIFIDELDAVGRSRGAGLGGGHDEREQTLNQLLVEMDGFGTHTNVIVMAATNRPDVLDSALLRPGRFDRQVTVSLPDIKEREAILNIHSLKTKLSKDINLQVIARATPGASGADLANLINEGALIAARNNQDEILMKDMEEARDKILMGVAKKSMTITDRQKLETAYHEAGHALLHYYLEHADPLHKVTIIPRGRALGVAFSLPREDRLSINKHQILDKIKICYGGYASEQINLGVTTAGVQNDLMQATSLAKKMVTEWGMGEEVGPIFLVDDEAPIFLPKEFSKAKAYSENTADKVDREVKRILEECLKEASDILLKHKDQLVKLAKELVLKETLTDKEVRELLGFEANKDEYDLFSSDSTTKEVKGEDVKG | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70802
Sequence Length: 639
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
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C7MC16 | MADSAKTPRGKKRRPFTGLALWIIVALLLGMAMFSLFGRDGYQQIDTQQGLELLAGDTVEQAKIIDGNQQRVDLVLTEDFKDGDEDKGTQVRFSYVDARGDAVVQAVEDAAPAKGYTDEIASSSWWSTLLLSFLPLLIFIGLFWFLIMNAQGGGKAMQFGKSKAKLFNKEAPKVTFADVAGADEAVEELDEIKQFLVDPGRYQAVGAKIPKGVLLYGPPGTGKTLLAKAVAGEANVPFYSISGSDFVEMFVGVGASRVRDLFNTAKENAPAIIFIDEIDAVGRHRGAGMGGGHDEREQTLNQMLVEMDGFEENQNVILIAATNRVDILDPALLRPGRFDRQIGVEAPDLKGRLHILGVHAKGKPLAHDVDLEAVAKRAIGMSGADLANVLNEAALLTARSGNQIIDNRALDEAIDRVSMGPQRYSKVMTERERQMTAYHEGGHALVAAAMNNSAPVTKVTILPRGRAGGYTMVVPTQDRNYQSRNELLDRLAYAMGGYAVEESIFHDVTTGPSSDLQNATKIARTMVMQLGMSGTVGQVALSGEQDEVFVGMQQGQAPRFSAETASLVDQEVRTLLDNALDEAWSVIVENRHVLDRLVEELLEKETLNERELAQIFRDVKKQPPREVWISSTERPSLAAPSVGGTTTATGTESHDAGEPLQPNPPELPHPGGEGPQIPGAPHGGEPGGGGYGYDGSAGTDGTGR | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75758
Sequence Length: 704
Subcellular Location: Cell membrane
EC: 3.4.24.-
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Q89AF2 | MAKNLMLWLVIAVVLMSIFQNFSANNINNRKIDYSTFLSDVNQDQVREVHISGREMNIIRKDNGRYITYIPISDPKLLDNLLVKNVKIIGAAPEEQSFFTAIFISWFPMLLLIGVWVFFMRQMQVGGGKGAMSFGKSKARMLPEDQVKITFSDVAGCDEAKEEVQELVEYLKEPSRFQKLGGKIPKGILMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEHSRKVAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFDGNEGIILIAATNRPDVLDPALLRPGRFDRQIFVALPDIRGREKIIQVHMKKVPLGNNVDPMIIARGTPGFSGADLANLVNEAALFAARNNRDVVMMSDFESAKDKITMGSERRSMVMTEKQKESTAYHEAGHVIVGRLVPEHDPAHKVTIIPRGRALGVTFFLPKDDVLSINKNKLESQISTLYGGRLAEEIIYGVNNVSTGAHNDIKVATNLARNMVTQWGFSKKLGPLLYSEEEGEIFLGRTVTKSKHMSDETARIIDEEVKLLVEKNYNRAKKILEENLDILHAMKDALIKYETINSRQIDDLMKRKSIQSSNICTDDDNN | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68020
Sequence Length: 610
Subcellular Location: Cell membrane
EC: 3.4.24.-
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Q3JMH0 | MKSETGYMGFVVVLVFMVLLALQLATLSAPATQIAYSDFRKLAAAAQLDDLEVSPTRITGVLRSASAAAALPASDAEAIKRAGTPWRFSTKRVTDERLIDTLAATGTRYRGADDDTWIGTLASWIVPIAVFALVWNLMLRRPRGGLQDWSGVGKSKPRVYVEAKTGIDFDDIAGIDEAKAELQQIVAFLRAPARYQRLGGKIPKGVLIVGAPGTGKTLLAKAVAGEAGVPFFSTSGSSFVEMFVGVGAARVRDLFEQAQQKAPCIIFIDELDALGKVRGAGLASGNDEREQTLNQLLVEMDGFQANSGVILMAATNRPEILDPALLRPGRFDRHIAIDRPDLTGRRQILSVHVKHVKLGPDVDLGELASRTPGFVGADLANIVNEAALHAAELDKPAIDMSDFDEAIDRAMTGMERKSRVMSEREKITIAHHEAGHALIAQTRAHSDPVKKVSIIPRGIAALGYTQQVPTEDRYVLRKSELLDRLDVLLGGRVAEEIVFGDVSTGAENDLERATEMARHMVARYGMSERIGLATFGDADTQGLSPLVWQRGGERCSESTATRIDDEIQRLLAEAHDRVSRTLKERRGALERIAGYLLEHEVVDHDKLVRLVNDEPTPEPGARDPGGDAAKRSGIGAAPAKPPAEVGSAELRDPARKADNADHSVPQ | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71914
Sequence Length: 666
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
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B9MPK5 | MRNLFKTATIYILIALVILLLVDIFSGGLSYNQFFSNLSERREVIYSELINDINDGKVTRIVLSYNNVSGQYADGTKFDNVFVPSPDKFLDQIQPAIQAKKIQIVTKEPPQVPWWLSTFLPMLIFAGLMIFVWIFMLQQTQGGGSKIMSFTKSRAKTIQDLKKKVTFADVAGADEEKEELKEVIDFLKNPRKYIELGARIPKGILLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGAARVRDLFDQAKRNAPCVVFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFGTNEGIIVMAATNRPDILDPALLRPGRFDRQIVVNVPDAKAREEILKVHARNKPLGEDVDLSQIAKITAGFTGADLENLLNEAALLAARKGKRQINMEEVQEAVAKVLMGPEKRSRVYTEKEKKLTAYHEAGHAIVRTMIPDSEPVHEVSIIPRGYAGGYTMYLPKEDKFYASKSDMMREIVTLLGGRVAEKLVLEDVSTGAASDIKRATKIARDMVTKYGMSDKLGPMTFGTEQEEVFLGRDLALARNYSEEVAAEIDREIKSIIEEAYKKAEEILKQNIDKLHKVANALLEKEKLTGEEFRKLVFEDAQPQLV | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68457
Sequence Length: 616
Subcellular Location: Cell membrane
EC: 3.4.24.-
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B8H444 | MNFRNLAIWLVIVAVLGGVFVVSQNSRTKSSSEISYSQLLKDVDAGKIKSAEIAGQTVLAKTADNKTLTVNAPMNSEELVNRMVAKNADVKFKSGSISFLAILVQLLPILLVVGVWLFLMRQMQGGAKGAMGFGKSKARLLTENKNRITFEDVAGVDEAKEELQEVVDFLKDPAKFQRLGGKIPKGALLVGPPGTGKTLIARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQVVVPNPDVAGREKIIRVHMKNVPLAADVDVKTLARGTPGFSGADLANLVNEAALMAARKNRRMVTMQDFEQAKDKVMMGAERRSMAMNEEEKKLTAYHEGGHAIVALNVPLADPVHKATIVPRGRALGMVMQLPEGDRYSMKYQQMTSRLAIMMGGRVAEEIIFGKENITSGASSDIKAATDLARNMVTRWGYSDILGTVAYGDNQDEVFLGHSVARTQNVSEETARLIDSEVKRLVQYGLDEARRILTDKIDDLHTLGKALLEYETLSGEEIADILKGIPPKREEEEAATAVIAPSLVPLSPGAGASVTA | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67693
Sequence Length: 626
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
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Q3B6R3 | MAKNSLKPSNPYNSEPETPQPRPKLPMIYYVVVIALLIGLQLAFFWSGSSREIPYSTFRTFITENKVESVRIAPEKIYVTLKPGVDSGLPKQEEGNDTTRKLLPGAKTPENEVTVNPVRDESLTALLETHGVRYEGSPGTTWISELIQWVLPFALLFGLYFFIFRRMGAGGPGAQFMNIGKNKAALYENLDEHTRITFKDVAGLDEAKAEVMEVVDFLKDPKKYTRLGGKLPKGVLLVGPPGTGKTLLAKAVAGEADVPFFSISGSDFVEMFVGVGAARVRDLFRQAKEKAPCIIFIDEIDAVGRSRGKGAMMGGNDERENTLNQLLVEMDGFATDKGVILMAATNRPDVLDPALLRPGRFDRQIMVDKPDLKGRMDTFRVHTKNMSLSPDVNLKALASQTPGFAGAEIANAANEAALLASRRNKESIEMKDFEDAIERVVAGLEKKNKVINPKEKRIVAYHEAGHAIVSWMMPENDPVQKISIVPRGMSALGYTMNIPLEDRYLMTKRELFARICGLLGGRIAEESVFGEISTGAQNDLEKITGIAYNMVMVYGMSDKIGNLSYYESNNPYYGAPGVEKKFGGETARLIDEEVKAIVESAADTVRTMLKEHRSKLEALARELLTKEMLQYCQIEEILGKRPGGQEEDSGEVDCSKKSAENGMVAHEPETTADAESTEKVGLSATELAELEAAAERLRQSRNVSDN | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77720
Sequence Length: 706
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
|
A0PXM8 | MGGINVKKRLSSATIWIVLLIVLFFAAITVLESSKTSGAISYNEFKKYWIENKVSRVEIKQDGRTVAGELNDKAKTQFQVVVPQSLLVQDILVNNPKSSVNVKFEPASSMPMWISWIPTIILILVMVGFWVMFMQQSQGGGGGNRGVMNFGKSRAKLATPDSQKVTFKDVAGADEEKGELEEIVDFLKEPKKYLDMGARIPKGILLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNSPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGVNEGIILVAATNRPDILDKALLRPGRFDRQILVGAPDAKGREEVLKVHVRNKRLSDDVDLKVLAKRTPGFVGADLENLMNEAALLAVRANKKQIGMEELEEAITRVIAGPEKKSRVIHEEDRKITAYHEAGHAIVMKFSPHSDPVHEISIIPRGMAGGYTMHLPERDTSYMSKSKLKDEMVGLLGGRVAEQIIIGDISTGASNDIQRVSNIARKMVMEYGMSEKLGTITFGSDHDEVFIGREIGKSKNYSEEVAFEIDNEVKALVDEAYKKAEKILTEHIDKLHAVAKVLLDKEKVTGEEFNAIVEGRPLEELNKKENAIDLEKHDNVEEVHDDVEGVHDDVEGVNIKDTSEDNIETTDAFANNTDLEEDKKEI | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74487
Sequence Length: 676
Subcellular Location: Cell membrane
EC: 3.4.24.-
|
Q0TTK8 | MFKDKKMLKYIVIYSIIAFGILLTFNMVKDEMLYEKVDYSTFMQMLDKKEVKSVNFSGNQIEITPSDSSNLKGKILYTTNPAVAGITQPELIKDLTVAGVEFNVTKPENYQLLGLLMSWVFPLILIFFVGRMMFSKMNNKMGGGVMSFGKNNAKLYAENETGITFKDVAGQDEAKESLVEIVDFLHDTRKYVEIGAKLPKGALLVGPPGTGKTLLAKAVAGEAKVPFFSMSGSDFVEMFVGMGAARVRDLFKQAEEKAPCIVFIDEIDAIGKSRDGAIQGNDEREQTLNQLLTEMDGFDSSKGVVILAATNRPEVLDKALLRPGRFDRRIIVDRPDLIGREEILKVHSRDVKLSDDVSLEEIAKSTPGAVGADLANIVNEAALRAVKHGRKFVIQEDLDEAVEVIIAGQEKRDRILSPKEKKIVAYHEVGHALVAALLNNTDPVHKITIVPRTMGALGYTMQLPEEEKYLVSKEEMIDQISVMLGGRAAEEVVFNSITTGASNDIERATQSARNMITIYGMSERFDMMALEAMSNRYLDGRPVRNCSETTAAIADEEVLQVIKKAHEKSIKILIENRELLDEITGVLLDKETIMGDEFMEIVYGKYPEKREADEKAKKEIQSLREQALAKRKEKEEAIKKAREEALRLEEEQRKQDELKAMIEAQEEAAKLARANNEANNDALDSSKENEEVKSNVNDGATEEKKDDSSTNNKVDGE | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79891
Sequence Length: 717
Subcellular Location: Cell membrane
EC: 3.4.24.-
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Q6M2F0 | MKNKKYLQFGGIAAVILIVLFLVSLFSSDTRNFQEVDTSVAMAQLDAGNVAEAQIDDREQRVRLTLREPITVDEREGVEEILAQYPARTAPAIFEKVEASNTDSYTTNVTQESFLMSMLSFILPMVIIFGLLMFFLTRMQGGGMFGIGGSKAKQLTKDMPTNTFADVAGAEEAVDELHEIKDFLEDPTRYEALGAKIPRGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFKQAKENSPCIIFVDEIDAVGRARGSGMGGGHDEREQTLNQLLVEMDGFGDRQGVILMAATNRPDVLDPALLRPGRFDRQIPVTNPDLRGREQILEVHAKGKPFAPDADIKALAKRTAGMSGADLANVLNEAALLTARVGGNVITADALEEATDRVVGGPRRSGKVISEKEKKVTAYHEGGHTLSAWALEDIERVYKVTILARGRTGGHAMTAQEDDKGMYNRNELFARLVFAMGGRSAEELVFGEPTTGASADIEMATKIARSMVTEYGMSPAVGMVKYGQEQGDPFSGRGGGGNLDHSQEVAATIDTEVQFLLDKAHEVSYSILAEYRDHLDRLAEKLLEKETLRRPDLEALFDDIVPRKVAEVFPDESTRFPRQENREPVKTPVELALERGEEPPKKFSILEASRATRERRRKELEAQGKLPVQPASSAGVAPAAGAAAGSYGTPPPADWSVPGSAGKHRSRAEEQPAEQGFPAQTPAQAPEQSPDSSGGRPNPYATPTASGEHPGMKAYGFGDSELMDQSTGAEHTPGNVSQESPTEMIGFRLPDHERSDYPEKAQKESVLDASETTEMPVVPDQPIDGDSGKSAEGTQENPENEGDNRG | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 92253
Sequence Length: 853
Subcellular Location: Cell membrane
EC: 3.4.24.-
|
Q1LLA9 | MQCSYPLARQLERSSALNNNLFQKAAIWLVIALVLFTVFKQFDKPRAQDSVTYSQFMDDAKNGKVSRVDVQGRNLVVSPKEGSKYTIISPGDIWMVGDLMKYGVQVTGKADDEPNVLVQALYYLGPTLLIIVFWFYMMRQMQGGGKGGAFSFGKSRARLIDENQNAVTFADVAGCDESKEEVVELVDFLKDPQKFQKLGGRIPRGVLLVGPPGTGKTLLARAIAGEAKVPFFSISGSDFVEMFVGVGAARVRDMFENAKKQAPCIVFIDEIDAVGRHRGAGMGGGNDEREQTLNQMLVEMDGFEANSGVIVIAATNRADVLDKALLRPGRFDRQVYVGLPDIRGREQILKVHMRKVPIGNDVDASIIARGTPGFSGADLANLVNEAALFAARRSKRVVDMQDFEDAKDKIYMGPERKSTVMREEERKATAYHESGHAVVAKLLPKADPVHKVTIMPRGWALGVTWQLPEHDKYSKYKDNMLEEIAILFGGRAAEEVFLNAMSTGASNDFERATKIARDMVTRFGMSDSLGAMVYVDTEQDGMFGKLSSKTVSEATQQKVDAEIRRIIDDQYALAKRLLEENRDKVEAMTNALMEWETIDAEQVNDIMAGRPPRPPRGAQGPNSGGNTPPGGSPVAPTNAPATARADETV | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71260
Sequence Length: 649
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
|
D4HA34 | MKNASRIFKGPLIWILLCIGLIIVFLQFAGSGNGYKDIPTSEAVSIINSSKKLDSVTLTDGDQVIKITENENKKYRSYWVGNQSDQLVDRLNDRVKAKTLKSWQGENPGQSIWKALLINFLPFVIILLFFLWAMNAAQGMGGRGGVMGFGKSKAKVGSKDTPKSTFADVAGCQEAIDELQEIREFLAEPAKFQRVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKEAAPAIIFIDEIDAVGRHRGAGMGGGHDEREQTLNQLLVEMDGFDVHGGVILIAATNRPDVLDPALLRPGRFDRQIAVEAPDLDGRLKILKVHAHGKPMADDVDLASIARRTPGMTGADLANVLNEAALLTARANLPVIGNSELDEAIDRVIAGPQKKTRLMNQHERLVTAYHEGGHALVAAAMPGTDPVQKITILPRGRALGYTMVMPDSDKYSQTRSELLDSMAYMMGGRAAEELIFHDPSTGASNDIEKATKVARALVTQYGLSARVGTVQLGSGDTEPFLGMTAGQQRDYSDETAKIIDDEVRELLENAHQEAFDCLDANREVLDELVRQLFARETLSKAEVADIFKPLKRWPERGAFTGSDKRVPSSIPPVKPPQIAGVDEDAPEVGAPRRGVIAPPTPEPGGDLPGDNPGEWEPPSDWQPPSVGGGKSPEPPSPTHPGEGPQPPSNGNPWGPPRS | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 77231
Sequence Length: 717
Subcellular Location: Cell membrane
EC: 3.4.24.-
|
O22993 | MASIDNVFSLGTRFSIPENPKRSILKHATTSSFSARTQTRWRAPILRRSFTVLCELKTGSSSSGETNNSPAADDFVTRVLKENPSQVEPRYRVGDKLYNLKEREDLSKGTNAATGAFEFIKRKFDSKKKTETDKSEESVYLSDILREYKGKLYVPEQVFGPELSEEEEFEKNVKDLPKMSLEDFRKAMENDKVKLLTSKEVSGVSYTSGYRGFIVDLKEIPGVKSLQRTKWSMKLEVGEAQALLKEYTGPQYEIERHMTSWVGKVADFPNPVASSISSRVMVELGMVTAVIAAAAVVVGGFLASAVFAVTSFAFVTTVYVVWPIAKPFLKLFVGVFLGVLEKSWDYIVDVLADGGIFSRISDFYTFGGVASSLEMLKPILLVVMTMVLLVRFTLSRRPKNFRKWDLWQGIAFSQSKAEARVDGSTGVKFADVAGIDEAVDELQELVKYLKNPDLFDKMGIKPPHGVLLEGPPGCGKTLVAKAIAGEAGVPFYQMAGSEFVEVLVGVGSARIRDLFKRAKVNKPSVIFIDEIDALATRRQGIFKENSDQLYNAATQERETTLNQLLIELDGFDTGKGVIFLGATNRRDLLDPALLRPGRFDRKIRVRPPNAKGRLDILKIHASKVKMSDSVDLSSYASNLPGWSGAKLAQLVQEAALVAVRKTHNSILQSDMDDAVDRLTVGPTRIGLELGHQGQCRRATTEVGVAITSHLLLRYENAKIERCDRVSIIPRGQTLSQVVFHRLDDESYMFGRLPQLLHRLQVLLGGRAAEEVIYGSDTSKASVDYLSDASWLARKILTIWNLENPMVIHGEPPPWRKRPQFVGPRLDFEGSLYDDYDLVEPPVNFNMDDEVAHRSEELISQMYNKTVSLLRQNQTALLKTVKVLLNQKEISGEAIDFILDHYPPQTPLNSLLQEQNPGSLPFVPEHLRRESGDFVLVNHSTDVNAQV | Function: Functions in chloroplast biogenesis and chloroplast division . Required for plastid development during embryogenesis . Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 105543
Sequence Length: 946
Subcellular Location: Plastid
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A8MPR5 | MACRFPLHSSSPSQFLSPENRQRLPRNYPSISCQNNSATNVVHEDGDDNDKAKTNQVNLLAIPITLTIISASLAKPSFAAAKVTERKRTQKKPQEALTLEQLKAWSKDLPVVSNRIPYTDILSLKAEGKLKHVIKPPNLSLRQKAEPVLVVLEDSRVLRTVLPSLEGNKRFWEQWDELGIDVQCVNAYTPPVKRPPVPSPYLGFLWKVPAYMLTWVKPKKESKRAAELKRMREDFKRQRKEEIETMKEERVMMEKTMKAQKKQQERKKRKAVRKKKYEESLREARKNYRDMADMWARLAQDPNVATALGLVFFYIFYRVVVLNYRKQKKDYEDRLKIEKAEADERKKMRELEREMEGIEEEDEEVEEGTGEKNPYLQMAMQFMKSGARVRRASNKRLPEYLERGVDVKFTDVAGLGKIRLELEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQLLVSLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFIPKPGLIGRMEILQVHARKKPMAEDLDYMAVASMTDGMVGAELANIVEIAAINMMRDGRTELTTDDLLQAAQIEERGMLDRKDRSLETWRQVAINEAAMAVVAVNFPDMKNIEFLTINPRAGRELGYVRVKMDHIKFKEGMLSRQSILDHITVQLAPRAADELWYGEDQLSTIWAETSDNARSAARSLVLGGLSDKHHGLNNFWVADRINDIDVEALRILNMCYERAKEILGRNRTLMDEVVEKLVQKKSLTKQEFFTLVELYGSSKPMPPSILELRKIKRLELEEMVLKLDMTTARNSS | Function: Required for plastid development during embryogenesis . Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 99864
Sequence Length: 876
Subcellular Location: Plastid
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Q9I1K1 | MSSQRRNYRFILVVTLFVLASLAVSGRLVYLQVHDHEFLADQGDLRSIRDLPIPVTRGMITDRNGEPLAVSTEVASIWCNPREMAAHLDEVPRLAGALHRPAAALLAQLQANPNKRFLYLERGLSPIEASEVMALGITGVHQIKEYKRFYPSSELTAQLIGLVNIDGRGQEGTELGFNDWLSGKDGVREVAINPRGSLVNSIKVLKTPKASQDVALSIDLRLQFIAYKALEKAVLKFGAHSGSAVLVNPKSGQILAMANFPSYNPNNRASFAPAFMRNRTLTDTFEPGSVIKPFSMSAALASGKFDENSQVSVAPGWMTIDGHTIHDVARRDVLTMTGVLINSSNIGMSKVALQIGPKPILEQLGRVGFGAPLSLGFPGENPGYLPFHEKWSNIATASMSFGYSLAVNTAELAQAYSVFANDGKLVPLSLLRDNPQNQVRQAMDPQIARRIRAMLQTVVEDPKGVVRARVPGYHVAGKSGTARKASGRGYADKSYRSLFVGMAPASDPQLVLAVMIDSPTRIGYFGGLVSAPTFSDIMAGSLRALAIPPDNLQDSPAVADRQHHG | Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin .
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 61101
Sequence Length: 565
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 3.4.16.4
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Q9M895 | MATFNVLCSNRFRFNGGYSPEKFNRKVSSRSSELNVCVSRIRTQSFSCRRLGGFMEIGETRLGVIRVHGDSRNRFSCNSEIKRLVTGDYGDKETRIGENGRNKGKRRRFSLRLRPRLRLVRMRLGRFDFRASMEDFRYFLKKNLKRVILSTGVALIFGLCYLFLRLTAVPSPSIVPYSDFVTNLRGGSVSKVLLEEGSRRIYYNTDENVEVVDDVHKSETLEDPAIQIDGGTVTEAVTKDDTPRKVRALPPVWKYVTRKVDHDEKFLLSLMREKGITYSSAPQSALMSMRTTLITIISLWIPLTPLMWLLYRQLSASNSPAKKRRSKNPTVGFDDVEGVDSAKDELVEIVSCLQGSINYKKLGARLPRGVLLVGPPGTGKTLLARAVAGEAGVPFFSVSASEFVELFVGRGAARIRDLFNAARKNSPSIIFIDELDAVGGKRGRSFNDERDQTLNQLLTEMDGFESDTKVIVIAATNRPEALDSALCRPGRFSRKVLVAEPDQEGRRKILAIHLRDVPLEEDAFLICDLVASLTPGFVGADLANIVNEAALLAARRGGEAVAREDIMEAIERAKFGINDKEARPRTLGNELSKMFPWMPSLARRNGPDQDGLQGPLGYQTLS | Function: Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69410
Sequence Length: 622
Subcellular Location: Plastid
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F4KF14 | MTFYISSSLTPTHFSKPLNPSNTLFPSQFRGSLSSFVRRRKPTEAKLSSKFNLFPSRRNGLITCCSTSSFESTESSVSQEEDAESNRLFEKLRETERERLSNMEELERKANVQLERQLVMASDWSRTLLTMRGKLKGTEWDPETSHRINFSDFMKLLDSNSVQYMEYSNYGQTISVILPYYKDGEPLGEEEDSKKEIIFRRHIVDRMPIDGWNDVWKKLHQQIVNVEVFNVDVVPAEVYTTVATFVVWSMRLALFVSLYVWIDSITRPIYAKLIPCDLGTPTKKIRQPLKRQALGSLGKSRAKFISAEEKTGVTFDDFAGQEYIKRELQEIVRILKNDEEFQNKGIYCPKGVLLHGPPGTGKTLLAKAIAGEAGLPFFAANGTDFVEMFVGVAASRVKDLFASSRSYAPSIIFIDEIDAIGSKRGGPDIGGGGAEREQGLLQILTEMDGFKVTTSQVLVIGATNRLDILDPALLRKGRFDKIIRVGLPSKDGRLAILKVHARNKFFRSEDEKEELLQEVAENTEDFTGAELQNVLNEAGILTARKDLDYIGREELLEALKRQKGTFETGQEDSTEVPEELKLRLAYREAAVAVLACYLPDQYRPISETDINSIRSQPNMRYSETSGRVFARKSDYVNSIIRACAPRVVEEEMFGIENLCWISAKSTLEASQRAEFLILQTGMTAFGKAYYRNQRDLVPNLVPKLEALRDEYMRFAVEKCSSILQEYQSALEEITDVLLEKGEIKADEIWNIYNTAPRIPQKPVRPVDEYGALIYAGRWGIHGVSLPGRVTFSPGNIGFATFGAPRPMETQIISDDTWKLVDEIWDKKVEEIKAEAVIQIEEEKKKPQILMATHFF | Function: Functions in chloroplast biogenesis and chloroplast division. Required for plastid development during embryogenesis . Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 96854
Sequence Length: 855
Subcellular Location: Plastid
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A2CI41 | MKPYEPKSWVTRVFLVWWLTALSCFFISGRLIYLQLLKGKWLKEKALKQQTVTLKTFQPRRNICDRNGIPLAIDTLAYDVFAHPLYFSISIEEVANKLSPILCIDSLSIQKLLKPTSTGICLASQLPENTGKLIASLRLDGIDLIKHPKRYYPYKEIVGNVIGYVDTSHQGQAGIELSCQESLQLNSPTLTSSIDGRGVLISHQIPKELFIQDNLSLQLTLDLELQKIAYKALKQGLENCKGKRGTVLILDPKTGGILTLVALPSYDPNIYYDFPIERFKPWPVTDLYEPGSTFKPLNIAIALETKAISPEDSFYDEGCIRVGDSIITNNDYNSYKPLPCLPNTYNKIVKLLANSSNVGMVHILERIAPEIYHSWLSKLDLGHAASPLETDLPWASESSLKDINEFVCYEIEPAAASFGQGLAMTPIKLAQLYASLANGGILVKPYLVTGLANAAEDTQKAKGIDLPSYNIRKKNLGNHLSWHKAEPSYLFLKRSGIRVTDLLRHIKAEGRFALPFRKNLLQLFTQDAHRTTELQLEPKAHQPQLLRPTRHAVYATNQSKRVFSHETTKLLLDMLEDVIWNGTGSSCFVEGYRIGGKTGTSQKHTQEGGYSKTKIITSFAAIFPTEDPQYVILTVIDEPNIPLSFGSNTAAPIVKSIIESLIDIKKMKPTIPIIKVKKD | Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 75878
Sequence Length: 679
Subcellular Location: Plastid
EC: 3.4.16.4
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Q9TL36 | MIYNYPMKYRRQFRRLPKHLQGIYYAFLSISTMIKIALDPYSKRPMKWMHSGTPFQYENERMVMIKLSLATVGLLFATRLSGLQFNKYTELKSVAERQQIGQVNDPQQRKIILDHHGDIVAIDLPAYDLYVHPRMCSISLERIAELLSPILDLSSQYLYNRLDEGDSGICLMHQIDTNTSAQIRRLGVDGIELVHHPQRVYPKRGSFESILGYVDTEGYGQAGLESSLDDWMKSTYQDVPCWMDGHGNFLGIRFPKQILFHQESALQLTIDCGLQEKVSQLITNAMNRFGAKRIAAIIMEAHSGAIRCLATSPSYDPNCYGWFPMERFRCWPITDLFEPGSTFKPVNLAIALENGIFQPTDRILDTGKIRIGDSWIGNVGGGFIWDRSLDHLTGTQILQRSSNVGMVRVMQSLDPAIYHRNLIRLGLGSHRNDNQTSFKMSSHDHNESGWNLKDLTSDYAISVVKDQDEFVDHEIEAATASFGQGLAMTPLKLLQLIATIANGGMAVTPHLISKIVTLDHFHHLQSMNEFSLQGWVGQSVLSRSQYHAKQPRPYTHDLYLGHVPVPSLELGWFDVKSIPPHTRERRRLFSRQTCNVLLGMLEQVVLDAQATGSRGFLPGYAMAGKTGTAQKASALGGYSTDSVVTSFVGIYPAVKPKFVTLVIIDEPEDPFRFGFNTAVDVTQTLISEMIVQEQDPPSYPTVSLFERNM | Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 79946
Sequence Length: 709
Subcellular Location: Plastid
EC: 3.4.16.4
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P57317 | MYKKEKNRFLKSKQINYINWRFFLLYGFIFLSLFILTLRVIFLQIISSNRLITEGDRRTLRTQSLLSTRGAIKDRRGYPLAVTVLVNAICADPSVILKTKNIKNHKRWQALSEILSIPLKKMFLRINSHKKSKFIYLARQINPEISEYIKKLQLPGIFLLEESKRYYPFKEISAQLVGFTNIDGIGIEGIEKSFDLLLTGKPGKRKIRQDNKGHVIEKISLVHKRASNNLNLSIDTKLQTIVYNELQEGVKKSQSDSGTAILINIKSGEVLAMANSPSYNPNNIRHIIQKNVRNKAITDLFEPGSTVKPIVIIEALKLGIIQENSIIDTKPFLIQKHQIKDVSYHEKLTITGILQKSSNVGVSKIALSMPTLKLLDSYIKFGLGKPTQLGLIGEKHGFFPPKKRWSNLDKATLSFGYGLMVTPLQLARLYSTIASYGIYRPLSIIKTDRPTGGKQIFPPKYVKKVINMMESVSQPGGGGLQAAVRGYRVAVKTGTAKKVGIHGRYIKKYTAYTAGIAPASDPRFSLIIILDNPQGKKYYGGAVSAPVFSNIMKLILKKMNIKPDNLSNQKMILKSNKRN | Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 65205
Sequence Length: 579
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 3.4.16.4
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Q89AQ0 | MKYFFQNKKNIHIKNETFNNRITILLSLIIITIILVLSRITFLQIIVSKKLIYKSNLRSLRTQIEFNQRGNITDRLGYPLAINIPVKNICIDPKLLFSKQTHIYPNLKWKMLSTVLSIPLSEIFYRIKYSKNNHFIYLAHKVNPEISEYISQLHIPGIYILDDFKRFYPFGKLTSQLIGFTNIDNEGIEGVEKSFNKLLMGKPGKKQIITDRYGRIIEQHNLVNKIQSHDIILSIDCSFQKFIYHILNQAVMSNKAKFGVAILVNIPTGEILSMVNTPSYDPNNSSELFKNNPLIRNKAITDIFELGSTVKPMIIMKALEKKIITPETVINTSSLVVNKHIIHDVSYHHALTASDILKKSSNTGVSRLALSIPISELIDIYSKFELGKSTNLGLIGERNGVLNTNKKHWSDLDKVTLSFGYGLMATPLQLARIYTTIGRYGLSKPLSIIVKNDTNLKNDIFSKQVFSKKIIKTVINMLEEVAKPGGAGFKAAIKGYRIAVKTGTAKKINSKGKYDNKYVSYIVGFAPVSNPTFCLMIMINEPKSNKYYGGEIAAPIFKTIMQKILKIKNIKPDAYL | Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 65288
Sequence Length: 576
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 3.4.16.4
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B8H0A0 | MSLSNLGPGGVHSPLWRWVVERVWRLEHAFERSRAAARPEDDTRIRIFLVMGFFGFCFVGVSLGAGWSALFSRAGQGGGYAQGVEGARGDVVDRNGKLLAVDLAHYALYVDPREVWDAKETRAALGRALPQVPAKRLDKAVFGDHRAFVLGGLTPDEKDAIFNLGLPGVTFEEQERRMYPLGPTAAHLIGFVDSGGKGLAGAERALDDPIRKAAGGEGGPAQLSIDVRVQAALEDELRKAAEEFTPKGAVGLVTNVHTGEILGMASWPDYDANKAGGATDDQRLNRAAASVYEMGSTFKAFTVAIGLDTGVATAASTFDAREPYKLGYRTIHDYHATKAVLNLVEVFQHSSNIGTAMLAERVGGQRLSQYFTNLGLTKPAKVELQESARPLTPRKWDQDTVASTSFGHGMNISPLALAQAMNALLNGGEMRPLTIRKLPPGVRPEGRRVLSEHTSAEMLKIMRANVVPGEGGSGGKADVPGLSVGGKTGTGEKYDPAIRRYNHQRQVSSFAATFPTDGPLEADRYFVLILLDEPKGNANSFGFSTGGWVAAPAAGRVIERIAPFLGVKRKTELVTIANSPKNAAPEAGL | Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 62995
Sequence Length: 589
Domain: The active site is important for FtsI localization.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 3.4.16.4
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P0AD69 | MKAAAKTQKPKRQEEHANFISWRFALLCGCILLALAFLLGRVAWLQVISPDMLVKEGDMRSLRVQQVSTSRGMITDRSGRPLAVSVPVKAIWADPKEVHDAGGISVGDRWKALANALNIPLDQLSARINANPKGRFIYLARQVNPDMADYIKKLKLPGIHLREESRRYYPSGEVTAHLIGFTNVDSQGIEGVEKSFDKWLTGQPGERIVRKDRYGRVIEDISSTDSQAAHNLALSIDERLQALVYRELNNAVAFNKAESGSAVLVDVNTGEVLAMANSPSYNPNNLSGTPKEAMRNRTITDVFEPGSTVKPMVVMTALQRGVVRENSVLNTIPYRINGHEIKDVARYSELTLTGVLQKSSNVGVSKLALAMPSSALVDTYSRFGLGKATNLGLVGERSGLYPQKQRWSDIERATFSFGYGLMVTPLQLARVYATIGSYGIYRPLSITKVDPPVPGERVFPESIVRTVVHMMESVALPGGGGVKAAIKGYRIAIKTGTAKKVGPDGRYINKYIAYTAGVAPASQPRFALVVVINDPQAGKYYGGAVSAPVFGAIMGGVLRTMNIEPDALTTGDKNEFVINQGEGTGGRS | Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 63877
Sequence Length: 588
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 3.4.16.4
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P45059 | MVKFNSSRKSGKSKKTIRKLTAPETVKQNKPQKVFEKCFMRGRYMLSTVLILLGLCALVARAAYVQSINADTLSNEADKRSLRKDEVLSVRGSILDRNGQLLSVSVPMSAIVADPKTMLKENSLADKERIAALAEELGMTENDLVKKIEKNSKSGYLYLARQVELSKANYIRRLKIKGIILETEHRRFYPRVEEAAHVVGYTDIDGNGIEGIEKSFNSLLVGKDGSRTVRKDKRGNIVAHISDEKKYDAQDVTLSIDEKLQSMVYREIKKAVSENNAESGTAVLVDVRTGEVLAMATAPSYNPNNRVGVKSELMRNRAITDTFEPGSTVKPFVVLTALQRGVVKRDEIIDTTSFKLSGKEIVDVAPRAQQTLDEILMNSSNRGVSRLALRMPPSALMETYQNAGLSKPTDLGLIGEQVGILNANRKRWADIERATVAYGYGITATPLQIARAYATLGSFGVYRPLSITKVDPPVIGKRVFSEKITKDIVGILEKVAIKNKRAMVEGYRVGVKTGTARKIENGHYVNKYVAFTAGIAPISDPRYALVVLINDPKAGEYYGGAVSAPVFSNIMGYALRANAIPQDAEAAENTTTKSAKRIVYIGEHKNQKVN | Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 67166
Sequence Length: 610
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 3.4.16.4
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G3XD46 | MKLNYFQGALYPWRFCVIVGLLLAMVGAIVWRIVDLHVIDHDFLKGQGDARSVRHIAIPAHRGLITDRNGEPLAVSTPVTTLWANPKELMTAKERWPQLAAALGQDTKLFADRIEQNAEREFIYLVRGLTPEQGEGVIALKVPGVYSIEEFRRFYPAGEVVAHAVGFTDVDDRGREGIELAFDEWLAGVPGKRQVLKDRRGRVIKDVQVTKNAKPGKTLALSIDLRLQYLAHRELRNALLENGAKAGSLVIMDVKTGEILAMTNQPTYNPNNRRNLQPAAMRNRAMIDVFEPGSTVKPFSMSAALASGRWKPSDIVDVYPGTLQIGRYTIRDVSRNSRQLDLTGILIKSSNVGISKIAFDIGAESIYSVMQQVGLGQDTGLGFPGERVGNLPNHRKWPKAETATLAYGYGLSVTAIQLAHAYAALANDGKSVPLSMTRVDRVPDGVQVISPEVASTVQGMLQQVVEAQGGVFRAQVPGYHAAGKSGTARKVSVGTKGYRENAYRSLFAGFAPATDPRIAMVVVIDEPSKAGYFGGLVSAPVFSKVMAGALRLMNVPPDNLPTATEQQQVNAAPAKGGRG | Function: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin .
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 62856
Sequence Length: 579
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 3.4.16.4
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Q9JU31 | MTEKSHKKTAKGRAGSPSPTSARNKKADNGARGNKVSERLKAVKELQKTETKKARPEHVVNLIGDALWLMGLAATLYLVISLISFDMGDPSWSHSSPVVEDVANWGGLFGAYVADVGYYLFGWSFWWWIAAACVMLYKNFRLHAKQTENEAYNHKIAAAALFVLTVFSPVLEYFVLGGKYADSLPVGAGGMVGIRVGAVFAWLLGKSGSLLIILVVLLLSLSLLVQISWLEFLNGAGRAVQNRLSALSGKVMALGKRRPNTKTDGVDTQNTRRMVKEAKNITAKPVALPEGSSSNRKSVAVSVAPPPKIQVSLFEDDEPRQAGEYHKPTLNLLRIPDSEPVSINPAELERTAELIESKLAEFGIGVQVVSATSGPVITRYEIEPAQGVKGSQIVALSKDLARSMSLQSVRIVETIAGKNTMGIELPNDKRQDVMLSEILSSPVFAEAKSKLTVALGKDIAGTPVVGDLAKMPHLLVAGMTGSGKSVGVNGMIMSMLFKATPDEVRFIMIDPKMLELSIYDGIPHLLCPVVTDMREAGQALNWCVAEMEKRYRLLSHAGVRNLEGFNQKVEAAKAAGKPLLNPFSLNPDNPEPLEKLPMIVVVIDELADLMMTERKAVEQQIARLAQKARAAGIHMIVATQRPSVDVVTGLIKANIPTRMAFTVQSKIDSRTILDQMGADELLKYGDSLFLQPGSAEPTRLQGAFVSDDEVHHVVAFVKEQAPANYVEGLLTGEAAQETANIVSPNADSDELFDQAVAYVLESKKTSISSLQRQLRIGYNRAANLMEALENAGVVSPSDLNGSRKILAHKDHL | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Translocation stops specifically at Xer-dif sites, where FtsK interacts with the Xer recombinase, allowing activation of chromosome unlinking by recombination. FtsK orienting polar sequences (KOPS) guide the direction of DNA translocation. FtsK can remove proteins from DNA as it translocates, but translocation stops specifically at XerCD-dif site, thereby preventing removal of XerC and XerD from dif (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87996
Sequence Length: 812
Domain: Consists of an N-terminal domain, which is sufficient for the localization to the septal ring and is required for cell division, followed by a linker domain, and a C-terminal domain, which forms the translocation motor involved in chromosome segregation. The C-terminal domain can be further subdivided into alpha, beta and gamma subdomains. The alpha and beta subdomains multimerise to produce a hexameric ring, contain the nucleotide binding motif and form the DNA pump. The gamma subdomain is a regulatory subdomain that controls translocation of DNA by recognition of KOPS motifs and interacts with XerD recombinase (By similarity).
Subcellular Location: Cell inner membrane
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Q8XRH0 | MGLGWFGISSVWLLPMVWRYVARVMAGERGLKGPGTVRIWLATLAVLCASASLEALTSGRDLHGKAGGAVGRGLASLFGHMLGWTGAFLLMLGVLLWVAPMVFGHSWRQLLARLRQAGEAPPVQADARHDEADDGLKPTALGLGGAEQAMGSGHAGASRRHGIEAGSAWRQPAWQPPPRTRESPPQPGEIWPLLNAQGRPEMPLPVAAQPAPVPVPAPAATPKAATQAPSSRSALRATIVSSPFHRPQPSDGDQPPSSPEADDAPSAPVEDAAPAISPAAEPDAPASAPPEPAEPSPPTVDLEAVRQEAEALLAELRGLMTPLAAAPVASPEPEPEPEPEAETEVTPEAEAEPEAEPEAEAEPEAEAEAEAEAEAEPEAEAPAPESVAPALQEAEAATAAEAPLPAPEPAPAIEADDAAPPPPAVPAQKPRIVLPAVVGQVVSNAMPAPAPAAAPVAAAPPAPPRVVDYRLPNVALLTAASPDTVAVPAEHLEETSHLIAQRLAEFKVPVTVAGASAGPVITRFEVDPAIGVRGAQVVGLMKDLARALGVTSIRVVETIPGKTCMGLELPNARRAMIRLSEVVNAPDFQSHASHLVLAMGKDITGNPVVTDLARAPHLLVAGTTGSGKSVAVNAMILSMLYKATPEDVRLIMIDPKMLELSVYEGIPHLLAPVVTDMKQAAHALNWCVGEMEKRYRLMSALGVRNLAGYNQKIRAAQQAGHKVPNPFSLTPDAPEPLSTLPMIVVVIDELADLMMVAGKKIEELIARLAQKARAAGIHLILATQRPSVDVITGLIKANIPTRVAFQVSSKIDSRTILDQMGAETLLGQGDMLFLPPGTGYPQRVHGAFVADEEVHRVVEHWKQFGEPEYDEAILAGDPAEAAAGELFGEGGDAEADPLYDEAAAFVLNTRRASISAVQRQLRIGYNRAARLIEQMEAAGLVSPMGRNGSREVIAPGGGD | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Translocation stops specifically at Xer-dif sites, where FtsK interacts with the Xer recombinase, allowing activation of chromosome unlinking by recombination. FtsK orienting polar sequences (KOPS) guide the direction of DNA translocation. FtsK can remove proteins from DNA as it translocates, but translocation stops specifically at XerCD-dif site, thereby preventing removal of XerC and XerD from dif (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 100247
Sequence Length: 959
Domain: Consists of an N-terminal domain, which is sufficient for the localization to the septal ring and is required for cell division, followed by a linker domain, and a C-terminal domain, which forms the translocation motor involved in chromosome segregation. The C-terminal domain can be further subdivided into alpha, beta and gamma subdomains. The alpha and beta subdomains multimerise to produce a hexameric ring, contain the nucleotide binding motif and form the DNA pump. The gamma subdomain is a regulatory subdomain that controls translocation of DNA by recognition of KOPS motifs and interacts with XerD recombinase (By similarity).
Subcellular Location: Cell inner membrane
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C6XMG3 | MSQVRSKSQQGKRQAKPQEVVPATILTEQLSTYAFGTVTAGAVMVAVAAWMGGSLASIDERIQGGLDATAKSAGFTVTKISIEGLDPRTKADVLNAVAIPVDSNMFRADPFVIKERIEASVENVSEVRVLRQWPNDIWILAENRRPLALWQTDGEWKVVDQVGKPMDGEDPAEYVELPRVVGPAGGYAAPELLAQLKLHPQISEHLEVAMRVGGRRWDLRLDSGLEIALPEDAQVDEALLAVYNLDEATGVLAEDSEVTRIDARDLERFAVGLGEARAAYDQSSQIDDKSGGA | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31760
Sequence Length: 293
Subcellular Location: Cell inner membrane
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Q28NP3 | MTTRSPARPLIARRSTPAPTPAPHDPAPSRLSYRVTRLWLTPIFRKALHLGIPVFALFAAVTWYLGDETRVAELFEAVQEIRREVENRPEFRVNVLGIDGASDDVTEQVRAALALDLPISSFDLDLDELRGRLEALPPVRTADLRIQSGGYLAVRIDERIPAAVWLTHEGLSIVDGDGIFVAGFGTRELAAPLPLLGGEGANLAVPEALALMEASSILDDRVHGLVRMGERRWDVVLTNGSRILLPEIGAAAALDRVLALDDMGEILSRDVTAVDVRNPGRLTVRLTDAAMEELQRLQTLAAERPDGDTRG | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 33933
Sequence Length: 311
Subcellular Location: Cell inner membrane
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E3EYX6 | MRPVDKKPVDRKIERETRYLRRDPAPSRWSYRYQRLMLTPAFRAGVRLGTPVIIIALAVAVVFGRADSRDWIMGHYNAAIAAVTQRPEFMVGSFAITGASPDLALAIEGLVDIPFPISTFNLDLQDLRTNIAALSPVRNVNVQAGGGVLQIVIEERQPVAVWRHVDGLRLMDGEGIATGMILNRADRPELPLIAGDGAQAAIPEAMELFRIASPLGARVLALVRMGERRWDLVLDREQIVQLPAVDAVAALQRVIAQEEAQQLLSRDVAVVDMRNDARQTIRMTQRARDALRSMPGRSAGRG | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 33349
Sequence Length: 302
Subcellular Location: Cell inner membrane
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Q1IKZ6 | MARNGNPQFPDERSTATRAKATEPEELDDRFSDLEPEEDSPFLRSQKRVPVRRGPLPSKKAANRVKIALIVLGVLVVIGGVWMALSAYGEHSWRFRLESSDSIEVGGNEHMSRGEITRVFGGDISRNIFAVPLDERKKQVEELPWVESATVMRILPDRIRVQVTERKPVAFAQIGSRVQLIDAHGVLMEMPFSTTNKYSFPVISGMHENEPLSTRSARMKIYQELVKELDASGEHNSKSLSEVDVSDPDDVKVTVEDADGAVLVHLGSQNFADRFHLYVTHLKEWRSQYQHLDSVDLRYDRQVILNPDSHPSAAKPTAPAVAPAVEKPAVAKPAVAKPTAHTSGRRH | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 38706
Sequence Length: 347
Subcellular Location: Cell inner membrane
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F9ZZP5 | MKFILFALLVSAGSWYGWKQLHSQDAVSKPIRYVKIEGAFQYTNKETLKRILTPEMKRGFYHVDMDAIHQLISQLPLVAAVDVNRVWPDAVHIKITEQKPIVRWGDKAVLNKQGEVLIPDDIDEFKNLPLITGPEGQEKKLLEIMKGVYIVLKDKSMQLAEFHVNDRRAWRIKLASGLEMQLGRKAPLENMQRFLKTMDLLGEEQVAMMASVDTRYPNGYAVTWKPDTPEIDWKAIAENYKNVMKERRI | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 28808
Sequence Length: 249
Subcellular Location: Cell inner membrane
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A0R014 | MTGTGPHGDPAEDPAGPDDTAAETDGPAEPTEPVDASEAEMTDTTETTAQTGTTAEADASEEFEGPRRRARRERAERRAARDRAMAIEQARREAKRRAVAGALDPTKSVPRNTIRGLKVLMWAALVSVLAVALGLLLYFTPIMSARNVEVSGLAEIPQEEVLTAAAVAPGTPLLQVDTDAVAERVATIRRVATARVQREYPSTLKISIVERVPVVVKDYPDGPHLFDRDGVDFATGPAPLALPYLDADNPGPNDPATRAALDVMMALPPDVAAQVGRIAAPSVASITLTLIDGRVVVWGTDDRTQEKALKLAALLTQPGTTYDVSSPDLPTVK | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 35307
Sequence Length: 333
Subcellular Location: Cell membrane
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F8CLT8 | MAFGKSKNRRRQDAAQQKEAVRGAVRSQGPRALKVLGLTLGTGLLVWGGAALREWTLTSPRFELEAVSFSGLQRASRVELLRLAALTKGQNLWTLDVDALERAMDQHPWLRTVEVTRRFPNRVSVEVTEHTPVAMAVLGELYVLDEEGEPFKRVTPGDGLDLPLVTGLDREGYVADPAAARERLRSALAVASAYARLSPDQAEQLSEVRLEAQSLALVTASGQEVRLGEGDSEVKLQRLARVRRELGARGLAAEIIHLDNRARPGWVAVKISSPASERSGASMR | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31057
Sequence Length: 284
Subcellular Location: Cell inner membrane
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Q9K0X9 | MERLTRWLLVMMAMLLAASGLVWFYNSNHLPVKQVSLKGNLVYSDKKTLGSLAKEYIHGNILRTDINGAQEAYRRYPWIASVMVRRRFPDTVEVVLTERKPVARWGDHALVDGEGNVFEARLDRPGMPVFRGAEGTSAEMLRRYDEFSTVLAKQGLGIKEMTYTARSAWIVVLDNGITVRLGRENEMKRLRLFTEAWQHLLRKNKNRLSYVDMRYKDGFSVRYASDGLPEKESEE | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 27135
Sequence Length: 235
Subcellular Location: Cell inner membrane
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Q2Y642 | MWDNHQALNQVADWLFTLAGLTTIYLMVQWTIHLPLLPLKEVHIRSNSGSGELRHVTREQVSDVVHREVGGNFLTIDLEAARHTFEKLAWVRVASVRRIWPNGLDVVVEEHVPLAHWGDSALVNRQGEIFNATSDEPMPIFEGPRESVREMVHQHAVFTKLLQPLKQDVEQVELSPRRAWRVRLGNGTILELGREHLEKRLERYVQTHDLVVARLNQRLSYVDLRYVSGFAARGTR | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 27222
Sequence Length: 236
Subcellular Location: Cell inner membrane
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Q2G991 | MAQTIKRGGKGVRRATAARSAQRKVQTARQQTGSVLDSVLRWLPFSEETLHRILMTLILAAAAGLVWTVAVMAGIPALVSEQAAIIASDAGFKVSHLEVRGVNRMNEAKIYERILGQNDRAMTTLDLAALRDELNQLPWVKDARVSRKLPDTLVIDIVERTPHAVLRKPDRMVLIDDTGVELESVRADRAKGMLVLSGMGVGQRVEDLTRLLDAAPALKPQVSEAEWVGNRRWNLTFKTGQVLALPEGDETAASALLSFARMDGVNRLLGGKVAAFDMRAPDRIYMRVPGHADEVAAEKRAEEQARAEAKRAASAKSDEG | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 34941
Sequence Length: 320
Subcellular Location: Cell inner membrane
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A1BAK9 | MQGLNPFHRDQGAGGRPAPVRPAPARPAPVAPRTPRKDPAPSRLAYRLNRMMLRPLVRRLVHVGLPAFLAALVAGIWLSDDTRRANLTGGIDAIVDRIQHRDEFMVKMMTIEGASPVVDKGLRAMLPVELPASSFEIDLEKLRERVLKLDAVETVDLRIKPGGVLSAVVTERVPVVLWRHARGIELLDKTGHRVASVTSREVRGDLPIIAGEGADRAAPEALALIDAAGPILPRLRGLERMGERRWDVVLDHGQRIKLPEDKALQALERAIALNGALHMLDRDISVVDLRQEARPVVRLGLEAQNAIRQARGQPELGPDGTPLAPEATAGNAAKAKKKSG | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 36986
Sequence Length: 340
Subcellular Location: Cell inner membrane
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G3XDA7 | MNGVLLRHQQPGGLGRAPRKPMPRGASRLVAKEPLSVRLPKADFSFLKYLAWPLLLAVLGYGAYRGAEYILPYADRPIAKVSVEGDLSYISQRAVQQRISPYLAASFFTIDLAGMRGQLEQMPWIAHAEVRRVWPDQVVIRLDEQLPIARWGDEALLNNQGQAFTPKELANYEHLPRLHGPQRAQQQVMQQYQLLSQLLRPLGFSIARLEMSDRGGWALTTAQGVEIQIGRDHVVDKIRRFVSIYDKALKDQISNIARIDLRYPNGLAVAWREPVTPATVATASAVQ | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 32250
Sequence Length: 287
Subcellular Location: Cell inner membrane
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O30993 | MLALRGRRGKRVRYPADGVAEADEAFVLPRPLRRGVRFLISLGAGRIRFPNHTGTVAAAAFMVATGLYGMSLGGHTQSFAQVSTTAAGFAIEDVRVSGNAQTSEIDILQQLGLDGTTSLVALDIEEARRLIGELPWVETVTVRKVYPGTIEVVLKEREAFGIWQHGSDLSLIERSGSVIAPLRDNKFASLPLFVGRDAETAAAAFYDEFSRWPEFRSRVKAFVRVAGRRWDLRLNNGVVVKLPEKDVARAMSVLAGMQDTHQLLERDIAAVDLRLEDRTTVQLTPEAVKRREVALKAREKMLKAQEKRI | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 34205
Sequence Length: 309
Subcellular Location: Cell inner membrane
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P11553 | MKQEVILVLDCGATNVRAIAVNRQGKIVARASTPNASDIAMENNTWHQWSLDAILQRFADCCRQINSELTECHIRGIAVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMDNIERLISAQRLQAISGVGAFSFNTLYKLVWLKENHPQLLERAHAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPQILQATGIPRRLFPRLVEAGEQIGTLQNSAAAMLGLPVGIPVISAGHDTQFALFGAGAEQNEPVLSSGTWEILMVRSAQVDTSLLSQYAGSTCELDSQAGLYNPGMQWLASGVLEWVRKLFWTAETPWQMLIEEARLIAPGADGVKMQCDLLSCQNAGWQGVTLNTTRGHFYRAALEGLTAQLQRNLQMLEKIGHFKASELLLVGGGSRNTLWNQIKANMLDIPVKVLDDAETTVAGAALFGWYGVGEFNSPEEARAQIHYQYRYFYPQTEPEFIEEV | Function: Catalyzes the phosphorylation of L-fuculose. Can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose.
Catalytic Activity: ATP + L-fuculose = ADP + H(+) + L-fuculose 1-phosphate
Sequence Mass (Da): 52259
Sequence Length: 472
Pathway: Carbohydrate degradation; L-fucose degradation; L-lactaldehyde and glycerone phosphate from L-fucose: step 2/3.
EC: 2.7.1.51
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P44399 | MAIALIFDCGATNLRTIAINEKGQILASHHLANNTKQGIESSDYHIWDIEEIWQKLTSCATQTLNQLMQQGIDLKDIVGISVTTFGVDGAPFDENDQQLYPIISWKCPRTIPVMENLSNQLDIKSLYQRNGIGQYSFNTLFKLHWLKTHKPDVFQKMAKFVFISSMLTQRLTGQFTTDHTMAGTSMMTNLTSGNWDPSILASLGLSNNHFPPMRYAGEKVGKLRTPLAQKWGLNPVPVISCGHDTQFAVFGSGAGLNQPVLSSGTWEILMARTQHAEPRFEFVSQGLTTEFDAQSNCFNPAVQWVGSGVIEWLGKLLFSDVYGSDHYYTTMIKEGEKAFNAGKRAVNFEGIFSQLGQGNISGLSMFATRGEIYVSALQHMANKLKNGLSVLHQVSQFQAKSLICVGGGSKNVLWNQIRANTLNLPIDVVDISESTVLGAAMFTFAGVGIYENVNAAQQAMQPTRKRIYPN | Function: Catalyzes the phosphorylation of L-fuculose.
Catalytic Activity: ATP + L-fuculose = ADP + H(+) + L-fuculose 1-phosphate
Sequence Mass (Da): 51949
Sequence Length: 470
Pathway: Carbohydrate degradation; L-fucose degradation; L-lactaldehyde and glycerone phosphate from L-fucose: step 2/3.
EC: 2.7.1.51
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Q9FBN6 | MSEYRIEHDSMGEVRVPADAKWRAQTQRAVENFPVSGQRIERAHIEALARIKSAAAKVNAELGVLDEDVAGAIQEAAGEVAEGKWDEHFPVDVFQTGSGTSSNMNTNEVVATLATERLGRDVHPNDHVNASQSSNDVFPSSIHIAATAAVTRDLIPALDHLAGALERKAGEFADVVKSGRTHLMDATPVTLGQEFGGYAAQVRYGIERLQASLPRLAELPLGGTAVGTGINTPPGFSAAVIEEVARATGLPLTEARDHFEAQGARDGIVETSGQLRTIGVGLTKIANDLRWMASGPRTGLAEISLPDLQPGSSIMPGKVNPVIPEAVLMVAAQVTGNDATVAAAGAAGNFELNVMLPVIAKNVLESVRLLANVSRLLADRTVDGIVAHPERAREYAESSPSVVTPLNKYLGYEEAAKVAKRALAERKTIRQTVLEGGYVERGDLTREQLDQALDVLRMTRP | Function: Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
Catalytic Activity: (S)-malate = fumarate + H2O
Sequence Mass (Da): 49068
Sequence Length: 461
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.2.1.2
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O66271 | MEYRIERDTMGEVRVPADKYWGAQTQRSLENFRIGTDRFRMPLEIIRAYGMLKKAAARANLELGELPEEIAKAIIQAAEEVVQGKWDDHFPLVVFQTGSGTQTNMNVNEVIANRASEILGKPLGSKYVHPNDHVNRGQSSNDTFPTAMYVAVALALHQRLYPAVEGLIRTFTAKAQAFDQIVKVGRTHLMDAVPITLGQEIGSWAAQLKTTLAAVKEMEKGLYNLAIGGTAVGTGLNAHPRFGELVAKYLAEETGLPFRVAENRFAALAAHDELVNVMGAIRTLAGALMKIGNDVRWLASGPYAGIGEITIPANEPGSSIMPGKVNPTQVEALTMVVVRVYGNDHTVAFAGSQGNFQLNVYKPVMAYSTLESINLLADAVASFDAHLAQGIEPNLERIEEHLQKNPMLATALNKAIGYDKAAEIVKKALKEKKTLKQAALELGYLTEEEFDRIVVPMRLAKPHEGA | Function: Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
Catalytic Activity: (S)-malate = fumarate + H2O
Sequence Mass (Da): 50882
Sequence Length: 466
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.2.1.2
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Q9PD25 | MEMQMSNSDRYRIEHDSMGDLRVPIDALWGAQTQRAIENFPISGRSMPQGFIHALGFIKAAAAKVNAELGLLPKPMAKEIEAAALDVAAGRYDADFPVDIYQTGSGTSSNMNANEVIATLAMRATKEPIHPNDHVNLGQSSNDVVPTAIRISATLAVQGRLLPALKHLRKMINKRARGLGSVVKTGRTHLMDAMPLTFAQEFGAWSAQIVSAEARLNDTLKRLHRLPLGGTAIGTGINTDPHFGRNAVKVLSALTGIHFESANNKFEGLAAQDDLVELSGQFNALAVALMKIANDLRWMNAGPLAGLGEIELPALQPGSSIMPGKVNPVIPEAVVMVASQVIGHHTAVTVAGQSGNFQLNVTLPLIAYNLLESATLLGNVVMLLADKVIVGLKVRQDRVQEVLERNPILVTALNPIIGYEKAAVIAKRAYKEHRPVLEVACEESNLNPVELARLLDPTALTEGGIYVVGGGGG | Function: Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
Catalytic Activity: (S)-malate = fumarate + H2O
Sequence Mass (Da): 50505
Sequence Length: 473
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.2.1.2
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Q8ZEB6 | MATTRSEKDSMGSIDVPANQLWGAQTQRSLAHFRISQEKMPTELIHALALTKRAAAQVNMDLGLLPAERAKAIMRAADEVLDGAHPTEFPLAIWQTGSGTQTNMNMNEVLANRASELLGGARGNNRLVHPNDDVNKSQSSNDVFPTAMHVAAVMGVSEHLLPELKVLQKTLADKAEAYRDIVKIGRTHLQDATPLTLGQEISGWAAMLSHSVRHIEATLPHLCELALGGTAVGTGLNTHPEYAVRVANEIATLTRQPFITAPNKFESLGTCDALVHGHGALKGLAASLMKIANDVRWLSSGPRCGIGEISIPENEPGSSIMPGKVNPTQCEAMTMLCAQVMGNDVAINIGGASGNFELNVFRPLVIHNFLQSVRLLADGMRGFNEHCALGIEPNRDRITQLLNESLMLVTALNTHIGYDKAAEIAKKAHKEGLTLKAAAMALGYLTDAEFDEWVRPEDMVGSMKK | Function: Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate.
Catalytic Activity: (S)-malate = fumarate + H2O
Sequence Mass (Da): 50129
Sequence Length: 465
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.2.1.2
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P0ACX7 | MGNRTKEDELYREMCRVVGKVVLEMRDLGQEPKHIVIAGVLRTALANKRIQRSELEKQAMETVINALVK | Function: In vitro catalyzes the addition of water to fumarate, forming malate. Cannot catalyze the reverse reaction. Cannot use the cis-isomer maleate as substrate.
Catalytic Activity: (S)-malate = fumarate + H2O
Sequence Mass (Da): 7907
Sequence Length: 69
EC: 4.2.1.2
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P35637 | MASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYSGYSQSTDTSGYGQSSYSSYGQSQNTGYGTQSTPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGSSSQSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQGYGQQNQYNSSSGGGGGGGGGGNYGQDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQQDRGGRGRGGSGGGGGGGGGGYNRSSGGYEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTIESVADYFKQIGIIKTNKKTGQPMINLYTDRETGKLKGEATVSFDDPPSAKAAIDWFDGKEFSGNPIKVSFATRRADFNRGGGNGRGGRGRGGPMGRGGYGGGGSGGGGRGGFPSGGGGGGGQQRAGDWKCPNPTCENMNFSWRNECNQCKAPKPDGPGGGPGGSHMGGNYGDDRRGGRGGYDRGGYRGRGGDRGGFRGGRGGGDRGGFGPGKMDSRGEHRQDRRERPY | Function: DNA/RNA-binding protein that plays a role in various cellular processes such as transcription regulation, RNA splicing, RNA transport, DNA repair and damage response . Binds to nascent pre-mRNAs and acts as a molecular mediator between RNA polymerase II and U1 small nuclear ribonucleoprotein thereby coupling transcription and splicing . Binds also its own pre-mRNA and autoregulates its expression; this autoregulation mechanism is mediated by non-sense-mediated decay . Plays a role in DNA repair mechanisms by promoting D-loop formation and homologous recombination during DNA double-strand break repair . In neuronal cells, plays crucial roles in dendritic spine formation and stability, RNA transport, mRNA stability and synaptic homeostasis (By similarity).
PTM: Arg-216 and Arg-218 are dimethylated, probably to asymmetric dimethylarginine.
Sequence Mass (Da): 53426
Sequence Length: 526
Subcellular Location: Nucleus
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Q8V3T9 | MAFLTILVLFLFKEVLCEPCICENPTCLGITIPQAGFVRSAPGGVLLTETITERPQLTEWTTSRPKLEETLWLDGETKNGKVSQTLFEAIQGTQMENCAVKAVLDTTFVNLTKQDIVLGKIKVSEFGGDSDISKCGRKGLKVFICGGTVGYVTRGCPPEECKGKKGRMMALEPTTDCGVEKGLTTDRIKTGMLDITSCCTQHGCTKGIRVEVPSPVLVSSKCQEVTFRVVPFHSVPDKLGFARTSSFTLKANFVNKHGWSKYNFNLRGFPGEEFIKCCGFTLGVGGAWFQAYLNGMVQGDGAASADDVKEKLNGIIDQINKANTLLEGEIEAVRRIAYMNQASSLQNQVEIGLIGEYLNISSWLETTTLTKTEEGLMKNGWCQSNTHCWCPPKPTIVPTIGYVDSIKEVTGTSWWMVMIHYIIVGLIVIVVVVFGLKLWGCLRR | Function: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. The trimer of F1-F2 (F protein) probably interacts with HE at the virion surface. Upon HE binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes.
PTM: The inactive precursor F0 is glycosylated and proteolytically cleaved into F1 and F2 to be functionally active. The cleavage is mediated by cellular proteases during the transport and maturation of the polypeptide.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 48773
Sequence Length: 444
Subcellular Location: Virion membrane
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Q786F3 | MGLKVNVSAIFMAVLLTLQTPTGQIHWGNLSKIGVVGIGSASYKVMTRSSHQSLVIKLMPNITLLNNCTRVEIAEYRRLLRTVLEPIRDALNAMTQNIRPVQSVASSRRHKRFAGVVLAGAALGVATAAQITAGIALHQSMLNSQAIDNLRASLETTNQAIEAIRQAGQEMILAVQGVQDYINNELIPSMNQLSCDLIGQKLGLKLLRYYTEILSLFGPSLRDPISAEISIQALSYALGGDINKVLEKLGYSGGDLLGILESRGIKARITHVDTESYFIVLSIAYPTLSEIKGVIVHRLEGVSYNIGSQEWYTTVPKYVATQGYLISNFDESSCTFMPEGTVCSQNALYPMSPLLQECLRGSTKSCARTLVSGSFGNRFILSQGNLIANCASILCKCYTTGTIINQDPDKILTYIAADHCPVVEVNGVTIQVGSRRYPDAVYLHRIDLGPPISLERLDVGTNLGNAIAKLEDAKELLESSDQILRSMKGLSSTSIVYILIAVCLGGLIGIPALICCCRGRCNKKGEQVGMSRPGLKPDLTGTSKSYVRSL | Function: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).
PTM: The inactive precursor F0 is glycosylated and proteolytically cleaved into F1 and F2 to be functionally active. The cleavage is mediated by cellular proteases during the transport and maturation of the polypeptide (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 59532
Sequence Length: 550
Subcellular Location: Virion membrane
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P56959 | MASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYSGYGQSADTSGYGQSSYGSSYGQTQNTGYGTQSAPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGGSSQSSSYGQPQSGGYGQQSGYGGQQQSYGQQQSSYNPPQGYGQQNQYNSSSGGGGGGGGGNYGQDQSSMSGGGGGGGYGNQDQSGGGGGGYGGGQQDRGGRGRGGGGGYNRSSGGYEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTIESVADYFKQIGIIKTNKKTGQPMINLYTDRETGKLKGEATVSFDDPPSAKAAIDWFDGKEFSGNPIKVSFATRRADFNRGGGNGRGGRGRGGPMGRGGYGGGGSGGGGRGGFPSGGGGGGGQQRAGDWKCPNPTCENMNFSWRNECNQCKAPKPDGPGGGPGGSHMGGNYGDDRRGRGGYDRGGYRGRGGDRGGFRGGRGGGDRGGFGPGKMDSRGEHRQDRRERPY | Function: DNA/RNA-binding protein that plays a role in various cellular processes such as transcription regulation, RNA splicing, RNA transport, DNA repair and damage response. Binds to nascent pre-mRNAs and acts as a molecular mediator between RNA polymerase II and U1 small nuclear ribonucleoprotein thereby coupling transcription and splicing. Binds also its own pre-mRNA and autoregulates its expression; this autoregulation mechanism is mediated by non-sense-mediated decay. Plays a role in DNA repair mechanisms by promoting D-loop formation and homologous recombination during DNA double-strand break repair (By similarity). In neuronal cells, plays crucial roles in dendritic spine formation and stability, RNA transport, mRNA stability and synaptic homeostasis .
PTM: Phosphorylated in its N-terminal serine residues upon induced DNA damage. ATM and DNA-PK are able to phosphorylate FUS N-terminal region.
Sequence Mass (Da): 52673
Sequence Length: 518
Subcellular Location: Nucleus
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P35949 | MIPGRIFLVLLVIFNTKPIHPNTLTEKYYESTCSVETAGYKSALRTGWHMTVMSIKLSQINIESCKSSNSLLAHELAIYSSAVDELRTLSSNALKSKRKKRFLGLILGLGAAVTAGVALAKTVQLESEIALIRDAVRNTNEAVVSLTNGMSVLAKVVDDLKNFISKELLPKINRVSCDVHDITAVIRFQQLNKRLLEVSREFSSNAGLTHTVSSFMLTDRELTSIVGGMAVSAGQKEIMLSSKAIMRRNGLAILSSVNADTLVYVIQLPLFGVMDTDCWVIRSSIDCHNIADKYACLARADNGWYCHNAGSLSYFPSPTDCEIHNGYAFCDTLKSLTVPVTSRECNSNMYTTNYDCKISTSKTYVSTAVLTTMGCLVSCYGHNSCTVINNDKGIIRTLPDGCHYISNKGVDRVQVGNTVYYLSKEVGKSIVVRGEPLVLKYDPLSFPDDKFDVAIRDVEHSINQTRTFFKASDQLLDLSENRENKNLNKSYILTTLLFVVMLIIIMAVIGFILYKVLKMIRDNKLKSKSTPGLTVLS | Function: Inactive precursor that is cleaved by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins.
PTM: The F glycoprotein is synthesized as a F0 inactive precursor that is heavily N-glycosylated and processed by a host furin-like protease probably in the Golgi.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59367
Sequence Length: 537
Domain: The N-terminus is a hydrophobic fusion peptide that inserts into the target host membrane (By similarity). It is buried in the center of the trimer cavity before cleavage by host furin. The coiled coil (heptad repeat) regions are probably involved in homotrimerization, heterodimerization and in the formation of a fusion-active hairpin structure (By similarity).
Subcellular Location: Host Golgi apparatus membrane
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P11236 | MKVFLVTCLGFAVFSSSVCVNINILQQIGYIKQQVRQLSYYSQSSSSYIVVKLLPNIQPTDNSCEFKSVTQYNKTLSNLLLPIAENINNIASPSSGSRRHKRFAGIAIGIAALGVATAAQVTAAVSLVQAQTNARAIAAMKNSIQATNRAVFEVKEGTQRLAIAVQAIQDHINTIMNTQLNNMSCQILDNQLATSLGLYLTELTTVFQPQLINPALSPISIQALRSLLGSMTPAVVQATLSTSISAAEILSAGLMEGQIVSVLLDEMQMIVKINIPTIVTQSNALVIDFYSISSFINNQESIIQLPDRILEIGNEQWSYPAKNCKLTRHHIFCQYNEAERLSLESKLCLAGNISACVFSPIAGSYMRRFVALDGTIVANCRSLTCLCKSPSYPIYQPDHHAVTTIDLTACQTLSLDGLDFSIVSLSNITYAENLTISLSQTINTQPIDISTELSKVNASLQNAVKYIKESNHQLQSVNVNSKIGAIIVAALVLSILSIIISLLFCCWAYVATKEIRRINFKTNHINTISSSVDDLIRY | Function: Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with HN at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).
PTM: The inactive precursor F0 is glycosylated and proteolytically cleaved into F1 and F2 to be functionally active. The cleavage is mediated by cellular proteases including host FURIN during the transport and maturation of the polypeptide.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 58712
Sequence Length: 538
Subcellular Location: Virion membrane
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Q96IV6 | MKGEAGHMLHNEKSKQEGHIWGSMRRTAFILGSGLLSFVAFWNSVTWHLQRFWGASGYFWQAQWERLLTTFEGKEWILFFIGAIQVPCLFFWSFNGLLLVVDTTGKPNFISRYRIQVGKNEPVDPVKLRQSIRTVLFNQCMISFPMVVFLYPFLKWWRDPCRRELPTFHWFLLELAIFTLIEEVLFYYSHRLLHHPTFYKKIHKKHHEWTAPIGVISLYAHPIEHAVSNMLPVIVGPLVMGSHLSSITMWFSLALIITTISHCGYHLPFLPSPEFHDYHHLKFNQCYGVLGVLDHLHGTDTMFKQTKAYERHVLLLGFTPLSESIPDSPKRME | Function: Promotes megakaryocyte differentiation by enhancing ERK phosphorylation and up-regulating RUNX1 expression.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39002
Sequence Length: 333
Subcellular Location: Cytoplasm
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Q9GKT2 | MKGEAGHMLHNEKSKQEGYIWGSMRRTAFILGSGLLSFVAFWNSVTWHLQRFWGASGYFWQAQWERLLTTFEGKEWILFFIGAIQVPCLFFWSFNGLLLVVDTTGKPNFISRYRIQVGKNEPVDPVKLRQSIRTVLFNQCMVSFPMVVFLYPFLKWWGDPCRRELPTFHWFLLELAIFTLIEEVLFYYSHRLLHHPTFYKKIHKKHHEWTAPIGVISLYAHPIEHVVSNMLPAIVGPLVMGSHLSSITMWFSLALIITTISHCGYHLPFLPSPEFHDYHHLKFNQCYGVLGVLDHLHGTDTMFKQTKAYEKHVLLLGFTPLSESIPDSPKRMQ | Function: Promotes megakaryocyte differentiation by enhancing ERK phosphorylation and up-regulating RUNX1 expression.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38885
Sequence Length: 333
Subcellular Location: Cytoplasm
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O75084 | MRDPGAAAPLSSLGLCALVLALLGALSAGAGAQPYHGEKGISVPDHGFCQPISIPLCTDIAYNQTILPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLDQAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDGSGGPGGGPTAYPTAPYLPDLPFTALPPGASDGRGRPAFPFSCPRQLKVPPYLGYRFLGERDCGAPCEPGRANGLMYFKEEERRFARLWVGVWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAHVAGFLLEDRAVCVERFSDDGYRTVAQGTKKEGCTILFMVLYFFGMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAVKTITILAMGQVDGDLLSGVCYVGLSSVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVLACYFYEQAFREHWERTWLLQTCKSYAVPCPPGHFPPMSPDFTVFMIKYLMTMIVGITTGFWIWSGKTLQSWRRFYHRLSHSSKGETAV | Function: Receptor for Wnt proteins. Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Activation by WNT8 induces expression of beta-catenin target genes (By similarity). Following ligand activation, binds to CCDC88C/DAPLE which displaces DVL1 from FZD7 and leads to inhibition of canonical Wnt signaling, activation of G-proteins by CCDC88C and triggering of non-canonical Wnt responses . May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues.
PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63620
Sequence Length: 574
Domain: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway.
Subcellular Location: Cell membrane
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Q61090 | MRGPGTAASHSPLGLCALVLALLGALPTDTRAQPYHGEKGISVPDHGFCQPISIPLCTDIAYNQTILPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLDQAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDGSGGAGGSPTAYPTAPYLPDPPFTAMSPSDGRGRLSFPFSCPRQLKVPPYLGYRFLGERDCGAPCEPGRANGLMYFKEEERRFARLWVGVWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAHVAGFLLEDRAVCVERFSDDGYRTVAQGTKKEGCTILFMVLYFFGMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAVKTITILAMGQVDGDLLSGVCYVGLSSVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVLACYFYEQAFREHWERTWLLQTCKSYAVPCPPGHFSPMSPDFTVFMIKYLMTMIVGITTGFWIWSGKTLQSWRRFYHRLSHSSKGETAV | Function: Receptor for Wnt proteins. Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Activation by WNT8 induces expression of beta-catenin target genes. Following ligand activation, binds to CCDC88C/DAPLE which displaces DVL1 from FZD7 and leads to inhibition of canonical Wnt signaling, activation of G-proteins by CCDC88C and triggering of non-canonical Wnt responses (By similarity). May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues.
PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63733
Sequence Length: 572
Domain: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway.
Subcellular Location: Cell membrane
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Q9IA03 | AGAAELQPELAVAEHVRYESTGPALCTVVFLLVYFFGMASSIWWVILSLTWFLAAGMKWGNEAIAGYAQYFHLAAWLLPSVKSIAVLALSSVDGDPVAGICYVGNQSLENLRGFVLAPLVVYLFTGSLFLLAGFVSLFRIRSVIKQGGTKTDKLEKLMIRIGIFTVLYTVPATIVIACYIYEQHNREAWEQAQNCSCPGDPHRPKPDYAVFMLKYFM | Function: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24044
Sequence Length: 217
Domain: The FZ domain is involved in binding with Wnt ligands.
Subcellular Location: Membrane
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Q61091 | MEWGYLLEVTSLLAALAVLQRSSGAAAASAKELACQEITVPLCKGIGYNYTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPICLEDYKKPLPPCRSVCERAKAGCAPLMRQYGFAWPDRMRCDRLPEQGNPDTLCMDYNRTDLTTAAPSPPRRLPPPPPPGEQPPSGSGHSRPPGARPPHRGGSSRGSGDAAAAPPSRGGKARPPGGGAAPCEPGCQCRAPMVSVSSERHPLYNRVKTGQIANCALPCHNPFFSQDERAFTVFWIGLWSVLCFVSTFATVSTFLIDMERFKYPERPIIFLSACYLFVSVGYLVRLVAGHEKVACSGGAPGAGGAGGAGGAAAAGAGAAGAGASSPGARGEYEELGAVEQHVRYETTGPALCTVVFLLVYFFGMASSIWWVILSLTWFLAAGMKWGNEAIAGYSQYFHLAAWLVPSVKSIAVLALSSVDGDPVAGICYVGNQSLDNLRGFVLAPLVIYLFIGTMFLLAGFVSLFRIRSVIKQQGGPTKTHKLEKLMIRLGLFTVLYTVPAAVVVACLFYEQHNRPRWEATHNCPCLRDLQPDQARRPDYAVFMLKYFMCLVVGITSGVWVWSGKTLESWRALCTRCCWASKGAAVGAGAGGSGPGGSGPGPGGGGGHGGGGGSLYSDVSTGLTWRSGTASSVSYPKQMPLSQV | Function: Receptor for Wnt proteins. Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalosomes (By similarity). The beta-catenin canonical signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Coreceptor along with RYK of Wnt proteins, such as WNT1.
PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73045
Sequence Length: 685
Domain: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway.
Subcellular Location: Membrane
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O93274 | MESLSLSLLLLVSWLQGSQCAAAKELSCQEITVPLCKDIGYNYTYMPNQFNHDTQDEAGMEVHQFWPLVVIHCSPDLKFFLCSMYTPICLEDYKKPLPPCRSVCERARAGCAPLMRQYGFAWPDRMRCDRLPEQGNPDTLCMDYYNRTEQTTAAPSHPEPPKPPARSVPKGRTRVEPPRSRSRATGCESGCQCRAPMVQVSNERHPLYNRVRTGQIPNCAMPCHNPFFSPEERTFTEFWIGLWSVLCFASTFATVSTFLIDMERFKYPERPIIFLSACYLLVSTGYLIRLIAGHEKVACSRGELDLEHIIHYETTGPALCTLVFLLIYFFGMASSIWWVILSLTWFLAAGMKWGNEAIAGYSQYFHLAAWLVPSIKSIAVLALSSVDGDPVAGICFVGNQNLDNLRGFVLAPLVIYLFIGSMFLLAGFVSLFRIRSVIKQGGTKTDKLEKLMIRIGIFSVLYTVPATIVVACFFYEQHNRQGWEVAHNCNSCQPEMAQPHRPDYAVFMLKYFMCLVVGITSGVWIWSGKTLESWRAFCTRCCWGSKATGGSMYSDVSTGLTWRSGTGSSVSCPKQMPLSQV | Function: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Activation by Wnt8, Wnt5A or Wnt3A induces expression of beta-catenin target genes. Displays an axis-inducing activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65379
Sequence Length: 581
Domain: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway.
Subcellular Location: Membrane
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Q9IA02 | ACDNPEKFQYVEKSLSCAPRCSPGVDVYWSREDKDFAFVWMAVWSTLCFVSTAFTVLTFLLDPHRFQYPERPIIFLSMCYNVYSVAFIIRSVAGAETIACDRENGELYIIQEGLESTGCTIVFLILYYFGMASSLWWVVLTLTWFLAAGKKWGHEAIEAHSSYFHMAAWGIPAMKTIVILTMRKVAGDELTGLCYVGSMDVSALTGFVLIPLSCYLVVGTSFILTGFVALFHIRKIMKTGGTNTEKLEKLMVKIGVFSILYTVPATCVIVCYFYERLNVDYWNLRALERACVPLPGRRAADCSLEASVPTVAVFMLKIFMSLVVGITSGVWVWSSKTLQTWQSLCNRKLGVRTRGKPCSGVSCGGVHCHYKAPTVMLHMTKTDPYLDNPTHV | Function: Receptor for WNT2 that is coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43899
Sequence Length: 392
Domain: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway.
Subcellular Location: Cell membrane
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Q9R216 | MAVPPLLRGALLLWQLLATGGAALEIGRFDPERGRGPAPCQAMEIPMCRGIGYNLTRMPNLLGHTSQGEAAAQLAEFSPLVQYGCHSHLRFFLCSLYAPMCTDQVSTPIPACRPMCEQARLRCAPIMEQFNFGWPDSLDCARLPTRNDPHALCMEAPENATAGPTEPHKGLGMLPVAPRPARPPGDSAPGPGSGGTCDNPEKFQYVEKSRSCAPRCGPGVEVFWSRRDKDFALVWMAVWSALCFFSTAFTVFTFLLEPHRFQYPERPIIFLSMCYNVYSLAFLIRAVAGAQSVACDQEAGALYVIQEGLENTGCTLVFLLLYYFGMASSLWWVVLTLTWFLAAGKKWGHEAIEAHGSYFHMAAWGLPALKTIVVLTLRKVAGDELTGLCYVASMDPAALTGFVLVPLSCYLVLGTSFLLTGFVALFHIRKIMKTGGTNTEKLEKLMVKIGVFSILYTVPATCVIVCYVYERLNMDFWRLRATEQPCTAATVPGGRRDCSLPGGSVPTVAVFMLKIFMSLVVGITSGVWVWSSKTFQTWQSLCYRKMAAGRARAKACRTPGGYGRGTHCHYKAPTVVLHMTKTDPSLENPTHL | Function: Receptor for WNT2 that is coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (By similarity). Plays a role in neuromuscular junction (NMJ) assembly by negatively regulating the clustering of acetylcholine receptors (AChR) through the beta-catenin canonical signaling pathway . May play a role in neural progenitor cells (NPCs) viability through the beta-catenin canonical signaling pathway by negatively regulating cell cycle arrest leading to inhibition of neuron apoptotic process (By similarity). During hippocampal development, regulates neuroblast proliferation and apoptotic cell death . Controls bone formation through non canonical Wnt signaling mediated via ISG15 . Positively regulates bone regeneration through non canonical Wnt signaling .
PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64995
Sequence Length: 592
Domain: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway.
Subcellular Location: Cell membrane
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Q1KPV0 | MRTLISHRQCVTSPFLISAASPPFPGRCFKLSSFTPPRHRRFSSLSIRNISHESADQTSSSRPRTLYPGGYKRPELAVPGLLLRLDADEVMSGNREETLDLVDRALAKSVQIVVIDGGATAGKLYEAACLLKSLVKGRAYLLIAERVDIASAVGASGVALSDEGLPAIVARNTLMGSNPDSVLLPLVARIVKDVDSALIASSSEGADFLILGSGEEDTQVADSLLKSVKIPIYVTCRGNEEAKEELQLLKSGVSGFVISLKDLRSSRDVALRQSLDGAYVVNNHETQNMNELPEKKNSAGFIKLEDKQKLIVEMEKSVLRETIEIIHKAAPLMEEVSLLIDAVSRIDEPFLMVIVGEFNSGKSTVINALLGKRYLKEGVVPTTNEITFLCYSDLESEEQQRCQTHPDGQYVCYLPAPILKDINIVDTPGTNVILQRQQRLTEEFVPRADLLVFVLSADRPLTESEVAFLRYTQQWKKKFVFILNKSDIYRDARELEEAISFVKENTRKLLNTENVILYPVSARSALEAKLSTASLVGRDDLEIADPGSNWRVQSFNELEKFLYSFLDSSTATGMERIRLKLETPMAIAERLLSSVEALVRQDCLAAREDLASADKIISRTKEYALKMEYESISWRRQALSLIDNARLQVVDLIGTTLRLSSLDLAISYVFKGEKSASVAATSKVQGEILAPALTNAKELLGKYAEWLQSNTAREGSLSLKSFENKWPTYVNSKTQLGIDTYDLLQKTDKVSLKTIQNLSAGTTSKRLEQDIREVFFVTVGGLGAAGLSASLLTSVLPTTLEDLLALGLCSAGGYVAIANFPYRRQAIIGKVNKVADALAQQLEDAMQKDLSDATSNLVNFVNIVAKPYREEAQLRLDRLLGIQKELSDIRSKLQLLQVDIDNLHVSRDEMRL | Function: Probable membrane-remodeling GTPase that plays a unique role in the in the determination of thylakoid and chloroplast morphology and regulates organization of the thylakoid network. Not involved in the determination of mitochondrial morphology or ultrastructure.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 100731
Sequence Length: 912
Subcellular Location: Plastid
EC: 3.6.5.-
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Q23424 | MSGTASLVHTLPASGDSNHRGLHSLKNSRRAADNEPLLRFREAKKVLGDVYGELKDNVAELEGVYKDIKENDFVSSEQREEIEAIGDSIKTIMDTFQRDNMKVVFFGRTSNGKSTTINAMLHEKVLPQGMGHTTCCFLQVEGSEGEVGHLQLDDNPQKIDMKMLGKIGHALSDENSDLPAMGQDSLLKVFHPKKSESGECRLLQNDVVILDSPGVDLSPEFDSWIDKHCLDADVFVLVSNAESTLTQAEKNFFLRVAKKLSKPNVFILNNRWDASAAETENIEDVKKQHLTRFRQFLVDELEVCSEREVNDRIFFVSSREVLESRLKARGLVQKAYQAEGHGTRALEFQNFERHFEHCISRSAIHTKFEAHNRRAHEMIGKMRLNLNSVLTSAAEQRSKLQNNLNESTRTFNECRVNFTQFEKAYREQTEQLRAEVHLKVSADFFEEIARLDAIIDRFEQPFDGSSSGMTKYKEDLAIFVDKCLSSDLEARCTGGLMSRIWNLENDMFQYVTKILAEPYQNKLEEVWRYRAPFKFSICVDVPALVNDFHEDLEFRFTFGLHAIIRRIIAYRSGQPVTAINTNLLTPLSLKQQSEKNSVRDAEASAASEEQAMMTQMVLTSAAFLANGSLGVLVVGGIVYKAVGWRVIAVGGAAYAGLYAWERMRWNSGAKEQHLKEQFRSHLAARMQQVSTAHTHHCETQAIREMDQVFDGLKATVGGVHREMKNDLDVQKTQIDAVDSTIRTLGTIKGKAVFLLRNLEQFASSYLRSDSPPTP | Function: Probable transmembrane GTPase (By similarity). Mediates mitochondrial fusion . Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission (By similarity). Dispensable for normal apoptotic processes during embryonic development .
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87462
Sequence Length: 774
Subcellular Location: Mitochondrion outer membrane
EC: 3.6.5.-
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Q9USY7 | MEKSARQLSVAEQNGESGRLNNGYTSNNIQQYKDETNRHQFEYNQNRNQLLRSIHIIQNLLNELDNYVDRSDCLFHSVWRTDKEKSKFSGNYYPFSPSKMNVITIDLSLRSSSTADEKLISQLGEEAHESLLKVHIEKANKHLFSLFSRVEDTSSKILITGDLNAGKSTLCNALVHKDILPEDQQPCTEVFCEVHDAELNDGKDCVHAIPHGLTYSHTDSSTYKVFPIEDLKRLVYETENWSMLIVYVNDGRPAHESLLHNGITDIALIDAPGLNTDSMKTTSVFACQEEIDVVVFVVNAENHFTLSATDFLRNASTEKSHIFIIVNKFDNIRDKERCKRLILEQIHTLSPGTFADAKDLVHFVSCRVARDPNNREDALYSSFFQMENSLRSFILENRSKSKLAPVRRYLSGLVGDILNICEYNIKLIDFDINHLQQRLTDLSPKFRKVKHEQQFTYQKNESLVEATVQSISQHTHSELEDAIDSLGSFASVKYSGFFFAYQYAISVRDAMQQYLEEKLLESEDYARKRTEEAVLCIQKDVKDNFDSAVLPVFHANQMFIKKHRLQLQKHFRFELGLLDFIDLDLTERLGTWSASLSTILLVLGKTTPSFTTLGAFTGNLGYPIFKYFQNNSLQHLLVPVLGLASICVFGYVIYDIPRALPLKVAEKIKKSLRETDFCHNASIWIGTESRKVLNIPLNDLRRMFHQQWDKQRETISVAENDLRICQKARKFFGEIESRTREAKKKIMMVQLEGCDINY | Function: Probable transmembrane GTPase, which mediates mitochondrial fusion. Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondrial morphology, which is balanced between fusion and fission (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87102
Sequence Length: 758
Subcellular Location: Mitochondrion outer membrane
EC: 3.6.5.-
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P38297 | MSEGKQQFKDSNKPHKDSTDQDDDAATIVPQTLTYSRNEGHFLGSNFHGVTDDRTTLFDGEEGRREDDLLPSLRSSNSKAHLISSQLSQWNYNNNRVLLKRSILKTQAFMDQLQEENNIRPIFIAANDEREKLHVLQLNIKLDGQYNTKEKNGFNIEKKALSKLFHSQIVSVTNHLNALKKRVDDVSSKVFITGDVNTGKSALCNSLLKQRLLPEDQLPCTNVFSEILEARENDGIEEVHAIPLNIAPTLKEAIDMYSIQNPKTYEIHTLKELPDLVPQNGKYALLKIYIKDDKRPASTSLLRNGTVDISLIDSPGLNMDSLQTAEVMSRQEEIDLVIFVVNAENQLTLSAKEFISLASREKKLMFFVVKKFDKIRDKQRCKELILKQIRDLSPETYKRAADFVHFVSKNGDELPHYHNENDNEDHGDRKPDDDPYSSSDPDPDFDSLEDSLRNFVLKKRSLSKLLPAKTYLSKLLSDIIMISKSNMKMYSEEEIKINEQLETLRPEILSARAKCNDLTTSVDQMAEQTITMTYNNTKEALLNALDVPLHEYPKYQGLGQIYDFIFSTEAFIANQIDESIGSSELFAKQKTDLLVKKIYEIGKNELGDDFMCERVFRSELMFRKRKHLIGKRLKVSLSITDLFAPTWKGFLSYLSWQKPVTAPLPDIEGQTNEGQIGLMKYLGLKNYPLTQYWSRPSLLFTSKIPTLTLYFLGSTKVVGNIILNGIKLSSWSSLKKLSVPVIVVGSLLGLTYLIHDLPRALPMNLSIKYKRKLQELDYIHLNAQRTSNEVRDVLRVPTREILRSCEIIMDKKQITKKELENKKESNLLSIKFFQSLYEGTVAQKLMVEEINLDID | Function: Essential transmembrane GTPase, which mediates mitochondrial fusion . Fusion proceeds through several steps; first mitochondria are tethered together, then brought into close contact, followed by the formation of a docking ring around contact areas, and finally membrane fusion . Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondrial morphology, which is balanced between fusion and fission, mediated by FZO1 and DNM1, respectively . Functions antagonistically with DNM1 . Probably acts by forming membrane contact sites that mediate mitochondrial membrane fusion . Mitochondrial docking and fusion requires GTP hydrolysis . Mitochondrial fusion promotes also increased lifespan.
PTM: Ubiquitinated at Lys-398 and Lys-464 . MDM30 and UGO1 are involved in ubiquitination . Deubiquitinated by UBP2 and UBP12 . UBP2 and UBP12 recognize distinct ubiquitin chains on FZO1 that have opposing effects on mitochondrial fusion . UBP2 removes ubiquitin chains that initiate proteolysis of FZO1 and inhibit fusion . UBP12 recognizes ubiquitin chains that stabilize FZO1 and promote mitochondrial fusion. UBP12 deubiquitylates FZO1 only after oligomerization .
Location Topology: Multi-pass membrane protein
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 97808
Sequence Length: 855
Domain: The GTPase domain may regulate the interaction with UGO1 since FZO1 lacking the GTPase domain binds 5-fold higher amount of UGO1 than full-length FZO1. The coiled-coil heptad repeat domains HRN, HR1 and HR2 are required for the oligomerization and function in mitochondrial fusion.
Subcellular Location: Mitochondrion outer membrane
EC: 3.6.5.-
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O18412 | MAESDSGESTSSVSSFISSSSSSRLSEFVDAKTELQDIYHDLSNYLSNFLTILEETVLLKDRQMLEHLCAFSSRVEAIAKVLSRDRMKVAFFGRTSNGKSAVINALLHEKILPSAMGHTTSCFCQVQANGSNETEHVKVEQEDEHMELSALSQLASAHSPGALKPSTLLQVNMAKNRCSILDYDVVLMDTPGVDVTAQLDDCLDSYCMDADVFILVLNAESTVSRVERQFFKDVASKLSRPNLFILNNRWDKASSLEPEMEQKVKDQHMERCVNLLVDELGVYSTAQEAWERIYHVSALEALHIRNGQITNPSGQTQQRYQEFLRFENDFSNCLAVSALKTKFGPHLLSAQKILNQLKSTLICPFIEKVSRLIDENKERRANLNAEIEDWLILMQEDREALQYCFEELTEMTQRVGRCVLNDQIKTLIPSSVLSFSQPFHPEFPAQIGQYQRSLCAHLDKLLEDRVLQCLSIPLQRKILDIEKEIGLPIAENSCDWQLIYGLDCQSYMSDFQPDLRFRFSLGFTALWHRLEGNLPLHASPFRIQKLQNGHKKCSPLPPLVNGNHWQMLESLVKSKGSLGTVLLSAMAIRSFNWPIVLILGGLVGSFYIYEYAAWTTAAQERSFKSQYARLLQQRLRSDVQQTVSGFELQLRQHLATVRNCWEAQSNETLNDLNVRTAELTKQIQSMEVLQLSLKKFRDKGQLLASRLGDFQETYLTKS | Function: Essential transmembrane GTPase, which mediates mitochondrial fusion during spermatogenesis . In early spermatocytes, fusion of mitochondria give rise to two organelles named Nebenkern and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission . Essential for fertility .
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81565
Sequence Length: 718
Subcellular Location: Mitochondrion outer membrane
EC: 3.6.5.-
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Q96UF1 | MSTINTGINGFRSHWPYCLACSLENPKVKVVAINDPFIDLEYMVYMFKYDSTHGRFKGTVEHKDGKLVVNGHEIAVHAERDPAQIPWGSHGADYVIESTGVFTTKDAASAHLKGGAKKVIISAPSADAPMFVVGVNLDKYTSDLTVISNASCTTNCLAPLAKVIHDNYGILEGLMTTVHATTATQKTVDGPSNKDWRGGRGAGANIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPDVSVVDLTVRLEKPASYDEIKATIKKASESEELKGILGYTEDQVVSTDFVGDAHSSIFDAKAGIQLSPTFVKLISWYDNEFGYSTRVVDLLAYVAGKDGAL | Catalytic Activity: D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH
Sequence Mass (Da): 36302
Sequence Length: 339
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subcellular Location: Cytoplasm
EC: 1.2.1.12
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P58559 | MKVRVGINGFGRMGRLALRAAWDWPELEFVHINEIKGGAVAAAHLLKFDSVHGRWTPEVEAEGERVLIDGTPLSFSEYGKPDDVPWEDFGVDLVLECSGKFRTPATLDPYFKRGVQKVIVAAPVKEEALNIVMGVNDYLYEPEKHHLLTAASCTTNCLAPVVKVIHEGLGIKHGIITTIHDNTNTQTLVDAPHKDLRRARATSLSLIPTTTGSATAIALIYPELKGKLNGIAVRVPLLNASLTDCVFEVTRPTTVEEINALLKAASEQAPLQGILGYEERPLVSIDYKDDPRSSIIDALSTMVVDETQVKILAWYDNEWGYVNRMVELARKVALSLK | Function: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Catalytic Activity: D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH
Sequence Mass (Da): 37117
Sequence Length: 337
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subcellular Location: Cytoplasm
EC: 1.2.1.12
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P25856 | MASVTFSVPKGFTEFSGLRSSSASLPFGKKLSSDEFVSIVSFQTSAMGSSGGYRKGVTEAKLKVAINGFGRIGRNFLRCWHGRKDSPLDIIAINDTGGVKQASHLLKYDSTLGIFDADVKPSGETAISVDGKIIQVVSNRNPSLLPWKELGIDIVIEGTGVFVDREGAGKHIEAGAKKVIITAPGKGDIPTYVVGVNADAYSHDEPIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVSKKTFAEEVNAAFRDSAEKELKGILDVCDEPLVSVDFRCSDFSTTIDSSLTMVMGDDMVKVIAWYDNEWGYSQRVVDLADIVANNWK | Function: Involved in the photosynthetic reductive pentose phosphate pathway (Calvin-Benson cycle). Catalyzes the reduction of 1,3-diphosphoglycerate by NADPH (By similarity).
Catalytic Activity: D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADPH
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42490
Sequence Length: 396
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 1.2.1.13
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P50362 | MAAMMQKSAFTGSAVSSKSGVRAKAARAVVDVRAEKKIRVAINGFGRIGRNFLRCWHGRQNTLLDVVAINDSGGVKQASHLLKYDSTLGTFAADVKIVDDSHISVDGKQIKIVSSRDPLQLPWKEMNIDLVIEGTGVFIDKVGAGKHIQAGASKVLITAPAKDKDIPTFVVGVNEGDYKHEYPIISNASCTTNCLAPFVKVLEQKFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTTTGAAKAVSLVLPSLKGKLNGIALRVPTPTVSVVDLVVQVEKKTFAEEVNAAFREAANGPMKGVLHVEDAPLVSIDFKCTDQSTSIDASLTMVMGDDMVKVVAWYDNEWGYSQRVVDLAEVTAKKWVA | Catalytic Activity: D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADPH
Sequence Mass (Da): 40304
Sequence Length: 374
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 1.2.1.13
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P09315 | MASSMLSATTVPLQQGGGLSEFSGLRSSASLPMRRNATSDDFMSAVSFRTHAVGTSGGPRRAPTEAKLKVAINGFGRIGRNFLRCWHGRGDASPLDVIAINDTGGVKQASHLLKYDSTLGIFDADVKPVGDNAISVDGKVIKVVSDRNPSNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNADQYNPDEPIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPNLKGKLNGIALRVPTPNVSVVDLVVQVSKKTLAEEVNQAFRDAAANELTGILEVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVISWYDNEWGYSQRVVDLADICANQWK | Catalytic Activity: D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADPH
Sequence Mass (Da): 42867
Sequence Length: 403
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 1.2.1.13
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P12858 | MASATFSVAKPAIKANGKGFSEFSGLRNSSRHLPFSRKSSDDFHSLVTFQTNAVGSSGGHKKSLVVEAKQLKVAINGFGRIGRNFLRCWHGRKDSPLDVIAINDTGGVKQASHLLKYDSTLGIFDADVKPVGTDGISVDGKVIKVVSDRNPANLPWKELGIDLVIEGTGVFVDREGAGRHITAGAKKVLITAPGKGDIPTYVVGVNADAYTHADDIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPTLKGKLNGIALRVPTPNVSVVDLVVQVSKKTFAEEVNEAFRESAAKELTGILSVCDEPLVSVDFRCTDVSSTVDSSLTMVMGDDLVKVIAWYDNEWGYSQRVVDLADIVANNWK | Catalytic Activity: D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADPH
Sequence Mass (Da): 43338
Sequence Length: 405
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 1.2.1.13
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P19866 | MASNMLSIANPSLRVYNKGFSEFSGLHTSSLPFGRKGSDDLMAFVSFQTNAVGGKRSSQNGVVEAKLKVAINGFGRIGRNFLRCWHGRKDSPLDVVVINDTGGVKQASHLLKYDSILGTFDADVKTAGDSAISVDGKVIKVVSDRNPVNLPWGDMGIDLVIEGTGVFVDRDGAGKHLQAGAKKVLITAPGKGDIPTYVVGVNEEGYTHADTIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAACLNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVSKKTFAEEVNAAFRESADNELKGILSVCDEPLVSIDFRCTDVSSTIDSSLTMVMGDDMVKVIAWYDNEWGYSQRVVDLADIVANKWQ | Catalytic Activity: D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADPH
Sequence Mass (Da): 43023
Sequence Length: 401
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Plastid
EC: 1.2.1.13
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A0QWW2 | MTIRVGVNGFGRIGRNFYRALATQKAEGKNTDIEIVAVNDLTDNATLAHLLKFDSILGRLPQDVSLEGDDTIVIGDTKIKALEVKEGPAALPWGDLGVDVVVESTGIFTNAAKAKGHLDAGAKKVIISAPATDEDITIVLGVNDDKYDGSQNIISNASCTTNCLGPLAKVLNDEFGIVKGLMTTIHAYTQDQNLQDGPHKDLRRARAAALNIVPTSTGAAKAIGLVLPELKGKLDGYALRVPIPTGSVTDLTAELAKSASVEDINAAMKAAAEGPLKGILKYYDAPIVSSDIVTDPHSSLYDAGLTKVIDNQAKVVSWYDNEWGYSNRLADLVALVGKSL | Function: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Catalytic Activity: D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH
Sequence Mass (Da): 35948
Sequence Length: 340
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subcellular Location: Cytoplasm
EC: 1.2.1.12
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P83601 | VKVGINGFGRIGRXVFRA | Catalytic Activity: D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH
Sequence Mass (Da): 1958
Sequence Length: 18
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subcellular Location: Cytoplasm
EC: 1.2.1.12
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O42259 | MSDLCVGINGFGRIGRLVLRACLQKGIKVVAINDPFIDLQYMVYMFKYDSTHGRYKGEVSMEDGKLIVDDHSISVFQCMKPHEIPWGKAGADYVVESTGVFLSIDKASSHIQGGAKRVVVSAPSPDAPMFVMGVNEDKFDPSSMTIVSNASCTTNCLAPLAKVIHDNFGIEEALMTTVHAYTATQKTVDGPSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADVSVVELTCRLSRPGSYAEIKGAVKKAAEGPMKGYVGYTEYSVVSSDFIGDTHSSMFDAGAGISFNDNFVKLISWYDNEFGYSHRVADLLLYMHFKE | Function: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity).
PTM: S-nitrosylation of Cys-152 leads to translocation to the nucleus.
Catalytic Activity: D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH
Sequence Mass (Da): 36290
Sequence Length: 335
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subcellular Location: Cytoplasm
EC: 1.2.1.12
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Q8X1X3 | MVVKVGINGFGRIGRIVFRNAVEHDDVEIVAVNDPFIETKYAAYMLKYDSTHGQFKGDIQHSSSNNLTVNNKTIHFYQERDPANIPWGKHGVDYVVESTGVFTTTEKAKAHLSGGAKKVIISAPSADAPMFVMGVNEKSYRPDISVLSNASCTTNCLAPLAKVIHDNFGIAEGLMTTIHSYTATQKTVDGPSHKDWRGGRTAAQNIIPSSTGAAKAVGKVIPALNGKLTGMAMRVPTANVSVVDLTCRTEKPVTYDQIKAAVKAASEGELKGILGYSEDALVSTDLNGDPRSSIFDASAGIALNDRFVKLISWYDNEWGYSRRVLDLIAYIAKVDAGK | Catalytic Activity: D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH
Sequence Mass (Da): 36470
Sequence Length: 338
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subcellular Location: Cytoplasm
EC: 1.2.1.12
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Q5R2J2 | MVKIGVNGFGRIGRLVTRAAFTCDKVQIVAINDPFIDLNYMVYMFKYDSTHGRFHGTVKAENGKLVINGQAITIFQERDPANIKWGDAGAEYVVESTGVFTTTEKASAHLKGGAKRVVISAPSADAPMFVMGVNHEKYDNSLKVVSNASCTTNCLAPLAKVIHDNYGMVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLQKPAKYDDIKKVMKAASEGPLKGILGYTEDQVVSSDFNGDSRSSIFDAAAGIALNDNFVKLVSWYDNEFGYSNRVVDLLVHMASKE | Function: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity).
PTM: S-nitrosylation of Cys-150 leads to translocation to the nucleus.
Catalytic Activity: D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH
Sequence Mass (Da): 35844
Sequence Length: 333
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subcellular Location: Cytoplasm
EC: 1.2.1.12
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Q6L125 | MIKVGINGYGTIGKRVAYAASIQDDIHVSGIVKNTPDYMAYLASRSFNIYVPDDDKIKEFEDHGIKVKGTLNDLMESSDIIVDATPEGMGMENIKIYKKKRVKAIFQGGEKSNIGDASFNAYSNYNESFKREYTRVVSCNTTALARTLYPILNDYGIENLNVTLIRRATDPNDNRKGPINAIEPSMSFPSHHADDLKTVLNLNNVYTVALKAPTTLMHVHSIEVLLKDDAKIDDIMESWLKYNRILLIEGKDNFKSTAQIMDMARELRRDRGDLYEIAIWRDSVKVIDKRLYYVQAVHQESDVIPENIDAIRSLSGIDKNESIEKTDKSLRISGGIFYGKE | Catalytic Activity: D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADPH
Sequence Mass (Da): 38559
Sequence Length: 341
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subcellular Location: Cytoplasm
EC: 1.2.1.59
|
Q43793 | MVTLYSSPSTHSSGPVASYSNSSIGLYNYHHNKQIAVSSILSRKFGSLQINQKPFWNAVRMQDGAVATPPSKIENETPLKKLKNGILPVAPPKEQKDTIDFDSNKAKSTVSITVVGASGDLAKKKIFPALFALYYEGCLPEHFTIFGYARSKMTDAELRNMVSKTLTCRIDKRENCGEKMEQFLERCFYHSGQYDSLENFAELDKKLKEHEAGRFSNRLFYLSIPPNIFINAVRCASLSASSAHGWTRVIVEKPFGRDSESSAALTRSLKQYLNEDQIFRIDHYLGKELVENLSVLRFSNLIFEPLWSRQCIRNVQFIFSEDFGTEGRGGYFDHYGIIRDIMQNHLLQILALFAMETPVSLDAEDIRNEKVKVLRSMRPLQLDDVIIGQYKCHTKGDVTYPGYTDDKTVPKDSLTPTFAAAALFIDNARWDGVPFLMKAGKALHTRSAEIRVQFRHVPGNLYNKNFGSDLDQATNELVIRVQPNEAIYLKINNKVPGLGMRLDRSNLNLLYSARYSKEIPDAYERLLLDAIEGERRLFIRSDELDAAWSLFTPVLKELEDKKIVPEYYPYGSRGPIGAHYLAARYKVRWGDLV | Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis which are involved in membrane synthesis and cell division (By similarity).
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 67369
Sequence Length: 593
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subcellular Location: Plastid
EC: 1.1.1.49
|
P48826 | MASTIARTEERQNAGTMELKDDTVIIVLGASGDLAKKKTFPALFGLYRNKFLPKGIKIVGYARTNMDHEEYLRRVRSYIKTPTKEIEEQLDSFCQFCTYISGQYDKDDSFINLNKHLEEIEKGQKEQNRIYYMALPPSVFTTVSDQLKRNCYPKNGVARIIVEKPFGKDLQSSRDLQKALEPNWKEEEIFRIDHYLGKEMVKNILIMRFGNEFFNATWNRHHIDNVQITFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQVLTLLAMERPISFSAEDIRDEKVRVLRAMDAIEPKNVIIGQYGKSLDGSKPAYKEDETVPQDSRCPTFCAMVAYIKNERWDGVPFIMKAGKALNEQKTEIRIQFRDVTSGIFKDIPRNELVIRVQPNESVYIKMNSKLPGLSMQTVVTELDLTYRRRFSDLKIPEAYESLILDALKGDHSNFVRDDELDASWRIFTPLLHYLDDNKEIIPMEYPYGSRGPAVLDDFTASFGYKFSDAAGYQWPLTSTPNRL | Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis (By similarity).
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 58950
Sequence Length: 510
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
EC: 1.1.1.49
|
P54547 | MKTNQQPKAVIVIFGATGDLAKRKLYPSIHRLYQNGQIGEEFAVVGVGRRPWSNEDLRQTVKTSISSSADKHIDDFTSHFYYHPFDVTNPGSYQELNVLLNQLEDTYQIPNNRMFYLAMAPEFFGTIAKTLKSEGVTATTGWSRLVIEKPFGHDLPSAQALNKEIREAFTEDQIYRIDHYLGKQMVQNIEVIRFANAIFEPLWTNRYISNIQITSSESLGVEDRARYYEKSGALRDMVQNHIMQMVALLAMEPPIKLNTEEIRSEKVKVLRALRPIAKDEVDEYFVRGQYHAGEIDGVPVPAYTDEDNVAPDSNTETFVAGKLLIDNFRWAGVPFYIRTGKRMKEKSTKIVVQFKDIPMNLYYGNENNMNPNLLVIHIQPDEGITLYLNAKKLGGAAHAQPIKLDYCSNCNDELNTPEAYEKLIHDCLLGDATNFAHWDEVALSWSFVDSISETWAANKTLSPNYESGSMGPKESDDLLVKDGLHWWNI | Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 55632
Sequence Length: 489
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
EC: 1.1.1.49
|
O51581 | MKERSVSNFDIVIFGVTGNLSRKKLIPSLFNLFKNKCISNFRVIGFSRKIFTDKEFRLYIKDSLWQEETDSLIEIFLNFFVYVFGDFNEKESYKNLFKFLDRSRETIYYLSTSPAFYGPIINHLKKYFLSEKLTLSKIVLEKPFGSSLETAKKLNSLLYSAFKEDQIYRIDHYLGKETVQNIFTFRFGNSIFENIWNNRYVDFVQITVAEELGLDGRVEYYDSVGALKDMVQNHILQLLSLVAMESPIKFDSEFIHDEKVKVLKSLRKISKEDIKNYIVKGQYIGSQVQGVFKKGYKDETEFLGNSNTETYLAMKVFINNWRWSGVPFYLRTGKGLARKFSEIYIQFKKPSFTLFNNSSVDFSNALIFRIQPRDGIEIKFNTKKPGYNYEIQTANMEFSYHGAFKRLFDEAYERLLLDAFLGDGTLYATSDEIESSWEFVSDIANKWADIEICNYFYGSEGPKEIDSILEKDHFWRKI | Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 56113
Sequence Length: 478
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
EC: 1.1.1.49
|
Q27464 | MACKRHSVSDPISKDLVECLRESMQRDLKFETPYVFVIFGASGDLAKKKIYPTLWWLFRDNLLPVNIKFIGYARSDLTVFKLRESFEKNCKVRENEKCAFDDFIKKCSYVQGQYDTSEGFQRLQSSIDDFQKESNNQAVNRLYYLALPPSVFNVVSTELKKNCMDHGDSWTRVIIEKPFGHDLKSSCELSTHLAKLFKEDQIYRIDHYLGKEMVQNLMVMRFGNRILAPSWNRDHIASVMISFKEDFGTGGRAGYFDTAGIIRDVMQNHLMQILTLVAMEKPASLNAEDIRDEKVKVLKAAKVVELKDVVVGQYIASPEFDHPEASQGYKDDKSVPADSTTPTYALAVVHINNERWEGVPFFLRCGKALNEKKAEVRIQFKEVSGDIYPSGELKRSELVMRVQPNEAVYMKLMTKKPGMGFGVEETELDLTYNNRFKEVRLPDAYERLFLEVFMGSQINFVRTDELEYAWRILTPVLEELKKKKVQPVQYKFGSRGPTEGDELMKKYGFIFTGTYKWVAPKL | Function: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty acid and nucleic acid biosynthetic processes.
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 60215
Sequence Length: 522
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subcellular Location: Cytoplasm
EC: 1.1.1.49
|
Q9Z8U6 | MTNVVQETIGGLNSPRTCPPCILVIFGATGDLTARKLLPALYHLTKEGRLSDQFVCVGFARREKSNELFRQEMKQAVIQFSPSELDIKVWEDFQQRLFYHRSEFDNNMGYTSLKDSLEDLDKTYGTRGNRLFYLSTPPQYFSRIIENLNKHKLFYKNQDQGKPWSRVIIEKPFGRDLDSAKQLQQCINENLNENSVYHIDHYLGKETVQNILTTRFANTIFESCWNSQYIDHVQISLSETIGIGSRGNFFEKSGMLRDMVQNHMMQLLCLLTMEPPTTFDADEIRKEKIKILQRISPFSEGSSIVRGQYGPGTVQGVSVLGYREEENVDKDSRVETYVALKTVINNPRWLGVPFYLRAGKRLAKKSTDISIIFKKSPYNLFAAEECSRCPIENDLLIIRIQPDEGVALKFNCKVPGTNNIVRPVKMDFRYDSYFQTTTPEAYERLLCDCIIGDRTLFTGGDEVMASWKLFTPVLEEWDQDSSPSFPNYPAGSSGPKEADALIERDGRSWRPL | Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 58740
Sequence Length: 512
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
EC: 1.1.1.49
|
Q23711 | LWWLFRDNLLPSVTKFVGYARTKLTVAELKEKCHPYMKVDAAHEEKYDEFWALNFYVAGSYDGRRDFELLNQEIGKFEVGKTANRLFYLRLPPSVFETVTVHIRNTCMGLKGWNRIIVEKPFGRDADSSNKLSEHLAKLFTEDQLYRIDHYLG | Function: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty acid and nucleic acid biosynthetic processes.
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 17999
Sequence Length: 153
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subcellular Location: Cytoplasm
EC: 1.1.1.49
|
P37986 | MAVTSTAQACDLVIFGAKGDLARRKLLPSLYQLEKAGHIHPETRIIGVGRAEWDRDAYIKVVREALETFLKEPLDPALWTTLSNRLDFCNLDVEDTEGFKRLGTMLDQQNRTTINYFAMPPSTFGAICRGLGQAGLNKEPARVVMEKPLGTNLASSRVINNQVAEFFNECQVYRIDHYLGKETVLNLLALRFANSLFANNWDNRTIDHVQITVAEEVGIEGRWGYFDQAGQMRDMIQNHLLQILTMIAMSPPADLSTDRIRDEKVKVLRSLRRIDRSNVHEVTVRGQYTSGFVQGKKVPGYLEEEGANKTSNTETFVAIRVDIDDWRWSGVPFYLRTGKRLPSKCSEVVVYFKNPALNLFHDSYQQLPQNKLIIRLQPDEGVEIQILNKIPGLDHKHRLQTTKLDLSFSETFNQQHLADAYERLLLETMRGIQALFVRRDEVEEAWKWVDSIMDAWAMDNDSPKPYQAGTWGPVASVAMITRDGRSWNEVE | Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 56034
Sequence Length: 491
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
EC: 1.1.1.49
|
Q557D2 | MTSTPDSRSVLTVIILGASGDLAKKKTYPALFGLYLRDLLPSNTIIYGYARSHIEIGDFKARISKGLKGDEEKKKQFLNLLHYHSGKYDEKASYDEFEKLILAEEKKQQGVDKFNRLFYMAIPPSIFIEVSIGIHGSLISKNGWSRVIVEKPFGRDLASSRELVSELGKLFKEKDLFRIDHYLGKEMVQNLMVLRFANAVFEPLWSKSHISSITITFKEDIGTEGRGGYFDQFGIIRDVMQNHLLQVLSLVAMEPPVSLNADDITNEKVKLLRCIQPIKMSEVVLGQYTSDPEGKIPAYLDDEGVPKDSTTPTYAAAVFHINNPRWRGMPFILKCGKALDERKTEVRIQFKRPDNFLFSDDDISRNELVMRIQPGEAVYLKLLSKKPGLENKIEQTELDLSYRHRFENLDLPDAYERLILDSIKGDHNLFVRDDELDVAWQIFTPLLDQIEKEKIKPEPYSFGSRGPKSADELSKKFGFIRSLGYNWPGNSPQGSKK | Function: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty acid and nucleic acid biosynthetic processes.
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 56697
Sequence Length: 497
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subcellular Location: Cytoplasm
EC: 1.1.1.49
|
P15588 | MAEQVALSRTQVCGILREELYQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIEPASFQRLNTHMNSLHHGAQANRLFYLALPPIVYEAVTKNIKETCMSQDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKDELQEAWRIFTPLLHHIEREKTQPIPYVYGSRGPPEADELMKRVGFQYEGTYKWVNPHKL | Function: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty acid and nucleic acid biosynthetic processes.
PTM: Acetylated by ELP3; acetylation inhibits its homodimerization and enzyme activity. Deacetylated by SIRT2; deacetylation stimulates its enzyme activity (By similarity).
Location Topology: Peripheral membrane protein
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Mass (Da): 21941
Sequence Length: 191
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Subcellular Location: Cytoplasm
EC: 1.1.1.49
|
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