ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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P0A2X3 | MKLISWNIDSLNAALTSDSARAKLSQEVLQTLVAENADIIAIQETKLSAKGPTKKHVEILEELFPGYENTWRSSQEPARKGYAGTMFLYKKELTPTISFPEIGAPSTMDLEGRIITLEFDAFFVTQVYTPNAGDGLKRLEERQVWDAKYAEYLAELDKEKPVLATGDYNVAHNEIDLANPASNRRSPGFTDEERAGFTNLLATGFTDTFRHVHGDVPERYTWWAQRSKTSKINNTGWRIDYWLTSNRIADKVTKSDMIDSGARQDHTPIVLEIDL | Cofactor: Probably binds two magnesium or manganese ions per subunit.
Function: In addition to 3'- to 5'-exonuclease and 3'-phosphatase activities, ExoA was shown to make single-strand breaks at apurinic sites in DNA.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 31064
Sequence Length: 275
Subcellular Location: Cytoplasm
EC: 3.1.11.2
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Q59083 | MTDQTAASPRVLVTGGAGYIGSHVLHALTDAGIPAVTIDDLSAGRREAIPAAVPLVEGDIGSAELLDRVMRDHRVDAVMHFAGSIVVPESVVKPLDYYRNNTANSLTLLGACLRAGIDKVVFSSTAAVYGAPESVPIREDAPTVPINPYGASKLMTEQMLRDAGAAHGLRSVILRYFNVAGADPAGRTGQATPVATHLIKVACQALLGRRPPLAIFGTDYDTPDGTCIRDYIHVSDLADAHVLALLHLRRGGGSLLMNCGYGRGASVREVVRTLEEVSGEQVPATFADRRPGDPPQLVAGADRIREQLGWVPKHDRLDGIVRSALSWERSLEQSVGQAGAPGGSASRS | Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Mass (Da): 36701
Sequence Length: 348
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
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Q59745 | MAGETVLVVGGAGYIGSHTCLDLANKGYRPVVFDNFSNGHREFVRWGPAEEGDIRDRARLDEVLAKHKPAAILHFAALIEVGESVKDPVSFYENNVIGTLTLLSAAQAAGINAFVFSSTCATYGLPQSVPLDETHRQVPINPYGRTKYIVEQALADYDQYGSLRSVVLRYFNAAGADFEGRIGEWHQPETHAIPLAIDAALGRRQGFKVFGSDYETRDGTCVRDYIHVLDLADAHVRAVEYLLKGGDSVALNLGTGTGTTVKELLGAIEEVSNRPFPVEYIGRREGDSHTLVANNDKARDVLGWVPQYDLSEIIRSAWDWHAKSNQH | Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Mass (Da): 35927
Sequence Length: 327
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
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P26503 | MQNNNILVVGGAGYIGSHTCLQLAAKGYQPVVYDNLSNGHEEFVKWGVLEKGDIRDRQRLDEVLARHKPRAILHFAAMIEVGESVKDPAAFYDNNVIGTLTLLSAALAAGIDAFVFSSTCATYGLPDSVPMDESHKQAPINPYGRTKWICEQALKDYGLYKGLRSVILRYFNAAGADFEGRIGEWHEPETHAIPLAIDAALGRREGFKVFGTDYDTRDGTCVRDYIHVLDLADAHVRAVDYLLEGGESVALNLGTGTGTTVKELLDAIEKVAKRPFNIGYAERREGDSTTLVANNDKARQVLGWEPQYDLAAITESAWNWHSRRNQGG | Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Mass (Da): 36113
Sequence Length: 328
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
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Q96KP1 | MSRSRQPPLVTGISPNEGIPWTKVTIRGENLGTGPTDLIGLTICGHNCLLTAEWMSASKIVCRVGQAKNDKGDIIVTTKSGGRGTSTVSFKLLKPEKIGILDQSAVWVDEMNYYDMRTDRNKGIPPLSLRPANPLGIEIEKSKFSQKDLEMLFHGMSADFTSENFSAAWYLIENHSNTSFEQLKMAVTNLKRQANKKSEGSLAYVKGGLSTFFEAQDALSAIHQKLEADGTEKVEGSMTQKLENVLNRASNTADTLFQEVLGRKDKADSTRNALNVLQRFKFLFNLPLNIERNIQKGDYDVVINDYEKAKSLFGKTEVQVFKKYYAEVETRIEALRELLLDKLLETPSTLHDQKRYIRYLSDLHASGDPAWQCIGAQHKWILQLMHSCKEGYVKDLKGNPGLHSPMLDLDNDTRPSVLGHLSQTASLKRGSSFQSGRDDTWRYKTPHRVAFVEKLTKLVLSQLPNFWKLWISYVNGSLFSETAEKSGQIERSKNVRQRQNDFKKMIQEVMHSLVKLTRGALLPLSIRDGEAKQYGGWEVKCELSGQWLAHAIQTVRLTHESLTALEIPNDLLQTIQDLILDLRVRCVMATLQHTAEEIKRLAEKEDWIVDNEGLTSLPCQFEQCIVCSLQSLKGVLECKPGEASVFQQPKTQEEVCQLSINIMQVFIYCLEQLSTKPDADIDTTHLSVDVSSPDLFGSIHEDFSLTSEQRLLIVLSNCCYLERHTFLNIAEHFEKHNFQGIEKITQVSMASLKELDQRLFENYIELKADPIVGSLEPGIYAGYFDWKDCLPPTGVRNYLKEALVNIIAVHAEVFTISKELVPRVLSKVIEAVSEELSRLMQCVSSFSKNGALQARLEICALRDTVAVYLTPESKSSFKQALEALPQLSSGADKKLLEELLNKFKSSMHLQLTCFQAASSTMMKT | Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Sequence Mass (Da): 104066
Sequence Length: 924
Domain: Interacts with RALA through the TIG domain.
Subcellular Location: Midbody
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Q9D4H1 | MSRSRQPPLVTGISPNEGIPWTKVTIRGENLGTGPTDLIGLTICGHNCLLTAEWMSASKIVCRVGQAKNDKGDIIVTTKSGGKGTSTVSFKLLKPEKIGILDQSAVWVDEMNYYDMRTDRNKGIPPLSLRPANPLGIEIEKCKLPQKNLEVLFHGMSADFTSENFSAAWYLIENHSTTSFEQLKMAVTNLKRQANKKSEGSLAYVKGGLSTFFEAQDALSAIHQKLEADGTEKVEGSMTQKLENVLNRASNTADTLFQEVLGRKDKADSTRNALNVLQRFKFLFNLPLNIKRNIQKGDYDVVINDYEKAKSLFGKTEVQVFKKYYAEVEAGIEDLRELLLKKLLETPSTLHDQKRYIRYLSDLHAPGDPAWQCIGAQHKWTLKLMQDCKEGHMKSLKGHPGPHSPMLDLDNDVRPSVLGHLSQTASLKRGSSFQSGRDDTWRYKTPHRVAFVEKLTKLVLSQLPNFWKLWISYVNGSLFSETAEKSGQSERSKNVRQRQNDFKKMIQEVMHSLVKLIRGALLPLSLREGDGRQYGGWEVQAELSGQWLAHVIQTIRLTYESLTALEIPNDMLQIIQDLILDLRIRCIMVTLQHTAEEIKRLAEKEDWVVDNEGLTSLPCQFEQSIVHSLQSLKGVVDCKPGEASVFQQPKTQEEVCQLCINIMQVFIYCLEQLSTKPDADIDTTHLSVDVSSPDLFGSIHEDFSLTSEQRLLIVLSNCCYLERHTFLNIAEHFEKHNFQGIEKITQVSMASLKELDQRLFENYIELKADPIVGSLEPGIYAGYFDWKDCLPPAGVRNYLKEALVNIIAVHAEVFTISKELVPRVLARVVEAVSEELSRLMQCVSSFSRNGALQARLEICALRDTVAIYLTSESRSSFKQALEALPQLASGADKKSLEELLNKFKSSMHLQLTCFQAASPAVMKT | Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Sequence Mass (Da): 103959
Sequence Length: 924
Domain: Interacts with RALA through the TIG domain.
Subcellular Location: Midbody
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Q9SKU2 | MQLFPVILPTLCVFLHLLISGSGSTPPLTHSNQQVAATRWLPATATWYGSAEGDGSSGGACGYGSLVDVKPFKARVGAVSPILFKGGEGCGACYKVRCLDKTICSKRAVTIIATDQSPSGPSAKAKHTHFDLSGAAFGHMAIPGHNGVIRNRGLLNILYRRTACKYRGKNIAFHVNAGSTDYWLSLLIEYEDGEGDIGSMHIRQAGSKEWISMKHIWGANWCIVEGPLKGPFSVKLTTLSNNKTLSATDVIPSNWVPKATYTSRLNFSPVL | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29108
Sequence Length: 271
Subcellular Location: Secreted
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P58738 | MGSLANNIMVVGAVLAALVAGGSCGPPKVPPGPNITTNYNGKWLTARATWYGQPNGAGAPDNGGACGIKNVNLPPYSGMTACGNVPIFKDGKGCGSCYEVRCKEKPECSGNPVTVYITDMNYEPIAPYHFDLSGKAFGSLAKPGLNDKIRHCGIMDVEFRRVRCKYPAGQKIVFHIEKGCNPNYLAVLVKYVADDGDIVLMEIQDKLSAEWKPMKLSWGAIWRMDTAKALKGPFSIRLTSESGKKVIAKDVIPANWRPDAVYTSNVQFY | Function: May aid fertilization by loosening the cell wall of the stigma and style, thereby facilitating penetration of the pollen tube. Acts selectively on grass cell walls, which are relatively poor in pectins and xyloglucans and rich in glucuronoarabinoxylans and (1-3),(1-4)-beta-D-glucans, when compared with cell walls of other angiosperms, including other monocots.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29085
Sequence Length: 269
Subcellular Location: Secreted
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B8PYF3 | MGSLAKIVAVAAVLAALVAGGSCGPPKVPPGPNITTNYNGKWLPAKATWYGQPNGAGPDDNGGACGIKNVNLPPYNGFTACGNPPIFKDGKGCGSCYEIRCNKPECSGQPVTVFITDMNYEPIAPYHFDLSGKAFGAMAKPGLNDKLRHYGIFDLEFRRVRCKYQGGQKIVFHVEKGSNPNYLAMLVKFVADDGDIVLMELKEKSSDWKPMKLSWGAIWRMDTPKALVPPFSIRLTSESGKKVIAQDVIPVNWKPDTVYNSNVQF | Function: May cause loosening of the cell walls.
PTM: Glycosylated.
Sequence Mass (Da): 28775
Sequence Length: 265
Subcellular Location: Secreted
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P85909 | MAGASAKVVAMLLSLQGPXSLRMVSESG | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 2803
Sequence Length: 28
Subcellular Location: Secreted
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Q9SHY6 | MTILVVDRYYMLMNLLFALTCLLLNLTHCFSPKKFNISAATTSDSDWSIAGSTWYGNPTGYGSDGGACGYGNAVAQPPFSKMVSAGGPSLFKSGKGCGACYQVKCTSKSACSKNPVTVVITDECPGCVKESVHFDLSGTAFGAMAISGQDSQLRNVGELQILYKKVECNYIGKTVTFQVDKGSNANSFAVLVAYVNGDGEIGRIELKQALDSDKWLSMSQSWGAVWKLDVSSPLRAPLSLRVTSLESGKTVVASNVIPANWQPGAIYKSNVNF | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29127
Sequence Length: 273
Subcellular Location: Secreted
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O24230 | MAGASAKVVAMLLSVLATYGFAAGVVYTNDWLPAKATWYGQPNGAGPDDNGGACGFKNTNQYPFMSMTSCGNEPLFQDGKGCGACYQIRCTNNPSCSGQPRTVIITDMNYYPVARYHFDLSGTAFGAMARPGLNDQLRHAGIIDIQFRRVPCYHRGLYVNFHVEAGSNPVYLAVLVEFANKDGTVVQLDVMESLPSGKPTRVWTPMRRSWGSIWRLDANHRLQGPFSLRMVSESGQTVIAHQVIPANWRANTNYGSKVQFR | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28686
Sequence Length: 261
Subcellular Location: Secreted
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Q9M0I2 | MQLFPVMLATLCIVLQLLIGSSALATTNRHVSNSHWLPAVATWYGSPNGDGSDGGACGYGTLVDVKPLHARVGAVNPILFKNGEGCGACYKVRCLDKSICSRRAVTVIITDECPGCSKTSTHFDLSGAVFGRLAIAGESGPLRNRGLIPVIYRRTACKYRGKNIAFHVNEGSTDFWLSLLVEFEDGEGDIGSMHIRQAGAREWLEMKHVWGANWCIIGGPLKGPFSIKLTTLSAGKTLSATDVVPRNWAPKATYSSRLNFSPVL | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28425
Sequence Length: 264
Subcellular Location: Secreted
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Q336T5 | MAFSISKKAAVAALFSFLVVTCVAGARPGNFSASDFTADPNWEVARATWYGAPTGAGPDDDGGACGFKNTNQYPFSSMTSCGNEPIFKDGKGCGSCYQIRCVNHPACSGNPETVIITDMNYYPVSKYHFDLSGTAFGAMAKPGQNDQLRHAGIIDIQFKRVPCNFPGLKVTFHVEEGSNPVYFAVLVEYEDGDGDVVQVDLMEANSQSWTPMRESWGSIWRLDSNHRLTAPFSLRITNESGKQLVASQVIPANWAPMAVYRSFVQYSS | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29192
Sequence Length: 268
Subcellular Location: Secreted
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Q9SHD1 | MASSQRYFALLALFAVSLKFCYCQNETIDVAGSGTAGVTWYGEPFGAGSTGGACGYGSAVANPPLYAMVSAGGPSLFNNGKGCGTCYQVVCIGHPACSGSPITVTITDECPGGPCASEPVHIDLSGKAMGALAKPGQADQLRSAGVIRVNYKRAACLYRGTNIVFRMDAGANPYYISFVVEYENGDGDLSNVEIQPAGGSFISMQEMRSAVWKVNSGSALRGPFNIRLTSGESHKVIVAYNVIPANWKPDESYRSIVNF | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27204
Sequence Length: 259
Subcellular Location: Secreted
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Q94LR4 | MGSLSSLAAAAVFLSLLAVGHCAAADFNATDADADFAGNGVDFNSSDAAVYWGPWTKARATWYGQPNGAGPDDNGGACGFKHTNQYPFMSMTSCGNQPLFKDGKGCGSCYKIRCTKDQSCSGRSETVIITDMNYYPVAPFHFDLSGTAFGRLAKPGLNDKLRHSGIIDIEFTRVPCEFPGLKIGFHVEEYSNPVYFAVLVEYEDGDGDVVQVDLMESKTAHGPPTGRWTPMRESWGSIWRLDTNHRLQAPFSIRIRNESGKTLVANNVIPANWRPNTFYRSFVQYS | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31358
Sequence Length: 286
Subcellular Location: Secreted
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Q9M203 | MASSSLKCFSFIVVLTTFFAISLKPCYCHNKTHWNTAGITWYGDREGPGTTGGACGYGDAVAKHPYRCMVSAGGPSLFKDGKGCGACYRLKCDHPLCTKKPIKVMISDECPGCTKESVHFDLSGKAFGALAKRGKGDQLRNLGELKVSYKRACCKHPKTMIAIHVDAGANPYYMSFAVKFANGDGNFACIEVQPAGGQYMKMEEMRSAVWRLSPGVPLKGPFNIRLTSAVSGKKIIAKGVIPEKWSPGAIYHSKVNFPVQRKQK | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28688
Sequence Length: 264
Subcellular Location: Secreted
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Q7XT39 | MVSRGTFVFAVLVALPILSLPVSGYEQNYTAGRRSTMSLGRGYGWSSGGATWYGGPQGDGSEGGACGYQSAVGQRPFSSMIAAGGPSLFKNGKGCGSCYQIKCTGNRACSGRPVTVVITDSCPGGVCLNEAAHFDMSGTAFGAMANRGMGDRLRSAGVLKIQYKRVPCRFAMNVAFKVDAGSNPYYLAILVQYANGDGDLAAVHIMEARGGGGWKAMQQSWGATWRLNSNTGKPLSPPFSIRLTSGSGKVLVANNVIPSGWQAGLTYRSTVNYAA | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28718
Sequence Length: 275
Subcellular Location: Secreted
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Q7XCA7 | MAARMGSKVAAILAILSVLVVHGSCKGHPVNYNVSDASAYGSGWLPARATWYGAPTGAGPDDNGGACGFKNVNQYPFSSMTSCGNEPIFKDGKGCGSCYQIRCNKDPSCSGNIETVIITDMNYYPVARYHFDLSGTAFGAMAKPGLNDKLRHSGIIDIQFRRVPCNYPGLKINFHVEEGSNPVYFAVLVEYEDLDGDVVQVDLMESKSAYGGATGVWTPMRESWGSIWRLDSNHRLQAPFSLRIRSDSGKTLVANNVIPANWSPNSNYRSIVQFS | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29884
Sequence Length: 275
Subcellular Location: Secreted
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Q9LD07 | MAGRSRRRSFWSVGVAAALLCLLAAHGCSAKHHKPKPTPGGISGNASSSSSNSSTPSIPPPVAPTPTAPTPPIPSPGTGSSNGSSGGGGGGWLNARATWYGAPNGAGPDDNGGACGFKNVNLPPFSAMTSCGNEPLFKDGKGCGSCYQIRCVGHPACSGLPETVIITDMNYYPVSLYHFDLSGTAFGAMAKDNRNDELRHAGIIDIQFRRVPCQYPGLTVTFHVEQGSNPVYMAILVEYENGDGDVVQVDLMESRYSTGGVDGTPTGVWTPMRESWGSIWRLDTNHPLQGPFSLRITNESGKTLIADQVIPADWQPNTVYSSIVQFD | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34447
Sequence Length: 327
Subcellular Location: Secreted
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Q10T32 | MVSGDVGVVVYYLLLVLVVVQGCKGSSAVQGEGRWYNESEAIGGAAAWGNAKATWYGQPNGAGAADNGGACGFKKVNQYPFMGMTSCGNQPLYKGGKGCGSCYRVRCNRNPACSGNAQTVAITDMNYFPLSQYHFDLSGIAFGRLAKPGRADDLRRAGIIDVQFARVPCEFPGLKVGFHVEEGSSPVYLAVLVEYENGDGDVAQVDLKEAGAGGGRWTPMRESWGSVWRLDSNHRLRAPFSIRIRSDSGKTLVAPDVIPLNWTPNTFYRSFVQYSS | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29762
Sequence Length: 276
Subcellular Location: Secreted
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P00488 | MSETSRTAFGGRRAVPPNNSNAAEDDLPTVELQGVVPRGVNLQEFLNVTSVHLFKERWDTNKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPVPIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVWTPYGVLRTSRNPETDTYILFNPWCEDDAVYLDNEKEREEYVLNDIGVIFYGEVNDIKTRSWSYGQFEDGILDTCLYVMDRAQMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDILLEYRSSENPVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLQMDIFLEEDGNVNSKLTKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASVQAIKHGHVCFQFDAPFVFAEVNSDLIYITAKKDGTHVVENVDATHIGKLIVTKQIGGDGMMDITDTYKFQEGQEEERLALETALMYGAKKPLNTEGVMKSRSNVDMDFEVENAVLGKDFKLSITFRNNSHNRYTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLIQAGEYMGQLLEQASLHFFVTARINETRDVLAKQKSTVLTIPEIIIKVRGTQVVGSDMTVTVEFTNPLKETLRNVWVHLDGPGVTRPMKKMFREIRPNSTVQWEEVCRPWVSGHRKLIASMSSDSLRHVYGELDVQIQRRPSM | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.
PTM: The activation peptide is released by thrombin.
Catalytic Activity: L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 83268
Sequence Length: 732
Subcellular Location: Cytoplasm
EC: 2.3.2.13
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P36316 | MGNIFKPIPKADYQIVETVPQSLTAINSTNLSTYECFKRLIDLAKKEIYIATFCCNLSTNPEGTDILNRLIDVSSKVSVYILVDESSPHKDYEKIKSSHISYIKVDIGVLNNESVGNLLGNFWVVDKLHFYIGSASLMGNALTTIKNMGIYSENNSLAMDLYFRSLDYKIISKKKCLFFTRMATKYHFFKNHNGIFFSDSPEHMVGRKRTFDLDCVIHYIDAAKSTIDLAIVSLLPTKRTKDSIVYWPIIKDALIRAVLERGVKLRVLLGFWKKTDVISKASIKSLNELGVDHIDISTKVFRFPVNSKVDDINNSKMMIIDGRYAHVMTANLDGSHFNHHAFVSFNCMDQQFTKKIAEVFERDWISPYAKEIDMSQI | Function: Envelope protein associated with the inner side of the enveloped virion (EV) membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 43022
Sequence Length: 377
Subcellular Location: Virion membrane
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P26579 | MGNLTSARPAGCKIVETLPATLPLALPTGSMLTYDCFDTLISQTQRELCIASYCCNLRSTPEGGHVLLRLLELARADVRVTIIVDEQSRDADATQLAGVPNLRYLKLDVGELPGGKPGSLLSSFWVSDKRRFYLGSASLTGGSISTIKSLGVYSECEPLARDLRRRFRDYERLCARRCVRCLSLSTRFHLRRHCENAFFSDAPESLIGSTRTFDADAVLAHVQAARSTIDMELLSLVPLVRDEDSVQYWPRMHDALVRAALERNVRVRLLVGLWHRSDVFSLAAVKGLHELGVGHADISVRVFAIPGAKGDAVNNTKLLVVDDEYVHVTSADMDGTHYARHAFVSFNCAERAFARALGALFERDWQSSFSSPLPRAPPPEPATLLPVN | Function: Envelope protein associated with the inner side of the enveloped virion (EV) membrane.
Location Topology: Lipid-anchor
Sequence Mass (Da): 42808
Sequence Length: 388
Subcellular Location: Virion membrane
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Q0PA50 | MQEVISYIQKAVLEISNALKFPDTSYSQNQNFTGDTQLKFDVLSDEIITKTLSQCSSIKAIISEEKDEILTLNERANFIVAYDPLDGSSLMDVNFAIGSIFAIYEEKASAKNLRAALYSMYGARLELVICKDQPKLYRLNANNEFIFIKDLRMNEKGKINATGGTQKFWEEKHAKFIKSLFDEGYRLRYSGAMVSDINQILLKGGGIFSYPATQDAPNGKLRAFFEVFPLAFIIEKAGGKTTNGKNRSLLELEFDKIHATTPCFFGSEYEISKLLKAYNE | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 31586
Sequence Length: 280
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
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Q9EXV4 | MSGATLEAYLASCTARGDDLSRDVAAVIQRLAKAALDIRKLVNQGALGTAFNGTHGGSNTDGDLQKDLDILCDDQFLTCLQGAPVACYASEELENPVLLDPSARLAVAIDPLDGSSNIDNNVSIGTIFSVLPAAKGPDVDPSQSFLQPGNRQLAAGFFIYGPQTALVLSLGKGTEIFIFSSRLGCFVEAYKSAIIPERAHEFAINMSNYRHWEEAIRLYVDDCLAGSEGPRERDFNMRWIASLVAETYRILIRGGIFLYPADGRKGYSQGRLRLVYEANPIAFIIENAGGAATTSIDRILDLVPENLHQRVPLVFGSRREVARITRYHVDPNMIGERAPLFGKRGLFRA | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 38025
Sequence Length: 349
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
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O34011 | MAIELEGLGLSPELADVMTRLARVGADLARTIARNGVETDLAAGVGTNAGGDGQKALDVMADDAFREALTGTAVAYYASEEQDEVVTLGKGTLALAIDPLDGSSNIDVNVSIGTIFSIFPATDDPNTSFLRKGSEQIAGGYIIYGPQCALVCSFGRGVHHWVLDLDSRSFKRLPDIKALPQDTSEYAINASNYRHWPSPIRAFIDDLVAGAEGPRGRNFNMRWIASLVAETHRILMRGGVFLYPGDERKGYARGRLRHVYECAPIAFLITQVGGGATDGCEDILSALPDKLHARTPFVFGCAAKVARVTAYHDLPGEETSALFNTRGLFRS | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 35566
Sequence Length: 331
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
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Q2RRP2 | MLATDRTTLAQFLVEECRGRAGDDSELLGLLLDVAQACKTISKMTAMGSLAGVHGYNGDVNPQGENQARLDLMSNQAFVRATERTGHAAGLASEEMEEVLGFPESYARGTLLLVFDPLDGSSNIDINGTVGSIFSILPMPRPGEAPQTADFLQSGRQQVAAGYALYGPSTMFVLTIGSGVHGFTLDPLLGDFILTHPSMTVIPESGEFAINSSNSRFWEPPIRAYVDELLAGRSGPRSKDYNMRWIAALVADVHRILLRGGIYLYPRDTKTPDLAGRLRLLYEAAPVAFLMEQAGGRCTTGTRTMLDLVPGSLHERVPLIFGSAVEVERVETLYREPQRREFATPLFNQRGLFRD | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Mass (Da): 38757
Sequence Length: 355
Pathway: Carbohydrate biosynthesis; Calvin cycle.
Subcellular Location: Cytoplasm
EC: 3.1.3.11
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M1KXD0 | MEFISFVYTLIAFSSLLYFYLIWSESAKPKTTTHKAPPEASGAWPVIGHLRIMSGHPSAGIPHVNLGMLADKHGPIFSIRLGVHRVVVVSSPEVIKELFTTNDVAVSSRPSVKAGKHLAYDNAMLGFASYGAYWRQLRKIVSLELLSNRRLELQSHVSMSETGQFVKELYKLWEKKKSDGSGTEVGEGVVVDMKRWLGELNMNVVMRMVAGKRFGSGDNAEETKRCRRVMGDFFYLAGFFVPADALPYLGWLDLGGHEKRMKKAAKELDEVVGEWLAEHREREFSGEGKAQDFMDVMISVVKGADLQCEFDVDTIIKATCGTLIAGGTDTTAVVFVWALSLLLNHSHVLKKAQQELDKHVGKDRRVKESDLNNLIYLQAIVKETLRLYPPGPLAGTRRFTEDCVVGGYYIPKDTWLIVNLWKLQRDPRVWSDPLEFRPERFLAGDKTFDVKGQDFELIPFGAGRRICPGLSFGLQMLHLVLASLLQAFDMSTVSDEAVDMSESAGLTNMKATPLDVVVTPRLPPRLYNEIVEIY | Function: Hydroxylase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects . Catalyzes the 6-hydroxylation of 7-O-methylated precursors such as the conversion of genkwanin (GENK) to scutellarein-7-methyl ether (SCU7Me) . Can also use, with a lower efficiency, apigenin-7,4'-dimethyl ether (AdM), naringenin-7-methyl ether (SAK) and naringenin-7,4'-dimethyl ether (NdM) as substrates .
Catalytic Activity: genkwanin + O2 + reduced [NADPH--hemoprotein reductase] = H2O + oxidized [NADPH--hemoprotein reductase] + scutellarein 7-methyl ether
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59807
Sequence Length: 534
Pathway: Flavonoid metabolism.
Subcellular Location: Membrane
EC: 1.14.14.-
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A0A0B6CGH9 | MRITLQYIKLESKNTKERDMAESKAIGRSLEVPNVQELAKGKLASVPARYVRYSDRENTTLPPLTQIPVIDMQALLHPNSFEAELNSLHKACKQWGFFQLINHGVEAAVMEKMKLEMQEFFNLPLEEKQKFRQSADDMEGYGQSFVVSDEQKLDWADGFSVISLPTYLRKPHLIPKLPAPFRDAIDAYGAQLKELAIKILGFMAEALGMDPHEMTALFEEGIQALRMNYYPPCPQPEMVSGLCPHSDAGGLTILMQVNEVEGLQVRKDGGWVPVSPLPDAFIINLGDILEIVTNGEYFSVEHQATVNGDKERLSVAAFLNPKMEDNIGPAASFISGETPAKFKTITAAEYFKGLFSKELDGKSYLDLMRIQN | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Oxoglutarate-dependent dioxygenase (2-ODD) acting as a flavonoid 7-O-demethylase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects . Catalyzes the 7-O-demethylation of methoxylated flavones; mediates the conversion of 8-hydroxysalvigenin (8-OH-SALV) to pilosin (PIL) and of gardenin B (GARD B) to nevadensin (NEV) .
Catalytic Activity: 2-oxoglutarate + gardenin B + O2 = CO2 + formaldehyde + H(+) + nevadensin + succinate
Sequence Mass (Da): 41648
Sequence Length: 372
Pathway: Flavonoid metabolism.
Subcellular Location: Cytoplasm
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A0A076FFM5 | MPFPMEVLQASSLSFPLLRRHSRNNLINKFRNPTLPRIDIPRQNIDLKTFAATTPTVACPPSDPEIIPEKKEDKFDWYENWYPVATVCDLDKRRPHGRKVIGIDVVVWWDRKENAWKVFDDTCPHRLAPLSEGRIDQWGRLQCVYHGWCFDGVGACKFIPQAPHDGPPVETSKKACVKGVYPSCVRNGIVWFWPNSDPKYKDIYLTNKPHYIPELDDPSFTCTTITREVPYGYEILAENLMDPSHVPYAHYGILELEKVKESSKRDREGGHEMEISVGTIDVNGFSAKHVSADYYFVPPYVYYGRITPNAATKTKDATLPVVPEEKTAMIVFYCIPVTPGYSRLIYAGARNFAVQIDRFVPRWITHMSHNLIFDSDLFLLHVEEQKLKDLDWHKSCYIPTKADGQVVAFRRWLNKYGGTQVDWRNNFTPALPPTPSREQLFDRYWSHTAECSSCSVACKRLNALEIGLQAMSLVFVAMAAAVSAPATRYSMVAMAVLSFLASKWLSHFIHKTFYNHGYDHAFV | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Rieske-type, PAO-family oxygenase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects . Catalyzes the 8-hydroxylation of salvigenin (SALV) to produce 8-hydroxysalvigenin (8-OH-SALV) . Can also use cirsimaritin (CIRM) as substrate with low efficiency .
Catalytic Activity: 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] + salvigenin = 8-hydroxysalvigenin + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59910
Sequence Length: 523
Pathway: Flavonoid metabolism.
Subcellular Location: Plastid
EC: 1.14.15.-
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Q9UBU6 | MAEGPEEARGHPPGQDDGGGDHEPVPSLRGPPTTAVPCPRDDPQAEPQAPGRPTAPGLAAAAAADKLEPPRELRKRGEAASGSGAELQEQAGCEAPEAAAPRERPARLSAREYSRQVHEWLWQSYCGYLTWHSGLAAFPAYCSPQPSPQSFPSGGAAVPQAAAPPPPQLGYYNPFYFLSPGAAGPDPRTAAGISTPAPVAGLGPRAPHVQASVRATPVTRVGSAAPSRSPSETGRQAGREYVIPSLAHRFMAEMVDFFILFFIKATIVLSIMHLSGIKDISKFAMHYIIEEIDEDTSMEDLQKMMVVALIYRLLVCFYEIICIWGAGGATPGKFLLGLRVVTCDTSVLIAPSRVLVIPSSNVSITTSTIRALIKNFSIASFFPAFITLLFFQHNRTAYDIVAGTIVVKRNGVR | Function: Plays a role in the assembly of the HRD1 complex, a complex involved in the ubiquitin-proteasome-dependent process of ER-associated degradation (ERAD).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44123
Sequence Length: 413
Subcellular Location: Membrane
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A4XJW0 | MAQNVKILSTGRYVPDRVLTNYDLEKMVDTSDEWITQRTGIKERRIVDGTTSTTDLAVRAAKNAMDKAGILPDDIDLVIVATVTPEMFFPSTACLVQKELKLKNAFAFDISAACSGFIYAMAIATHFIQNGFCKNALVIGAEALSRITNWSDRSTCVLFGDGAGAAILSSSDEQGILGFELGSDGENGLLLYCHAFGLSDVTYSQVKENPNFRKIYMEGNEVYKFAVKIMPYAVEKVLEKVGLSSSDIDVFIPHQANIRIIESAAKRLKIPMEKVFVNLHKYGNTSAASIPIALDEAVEEGRIKKGDKVVLVGFGGGLTWASTVIKWV | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 35809
Sequence Length: 328
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
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A7ZC01 | MPKASLISIASYVPEKILTNFDFEKMVDTSDEWIVKRTGIEQRHIATTEITSDLGTKAAELAIKRSGLEKSQIDAVICATISPDHLCMPSTACKIAANLGLNFGITAFDISAACTGFIYLLELANSLIVSGAKKNVLIIGAEKLSSIIDYTDRSTCILFGDGAGAAVISASEENEIIDIHTASDGRQAELLITPGCGSAFPASDETLKNRLNFIHMSGNEVFKIAVQTLSKSVIEILHANKMQSEDIDFFIPHQANIRIIDAVKNRLNFTDEQCVLTVAKYGNTSSASIPMAINDAYEDGRIKNGSVLLLDAFGGGFTWGSAILKFGGRNFSDL | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 35936
Sequence Length: 334
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
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Q9PIH1 | MLKASLKSIASYIPEKILSNADLEKMVDTTDEWITRRTGIKERRIASENENTSDLGTKAALKAIERANLKPEDIDAILVATLSPDYFTMPSTACKIASNLGLVNISAFDISAACSGFIYLLEQAKALVESGLKKNVLIIGAEKTSSIMDYNDRSICILFGDGAGAGVVSLDNENHILDVHTASNGNYGDLLMTQRSQKSSLCQTLSMQMKGNEVFKIAVNTLSNDVVEILAKNNILAQEIDLFIPHQANLRIIKAVQEKLNLSDEKCVITVQKYGNTSAASIPMAMNDAYEEGRLKKGNLILLDAFGGGFTWGSALLKFGGENF | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 35165
Sequence Length: 324
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
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Q9ZCH1 | MTCKIIGSGGYLPPKIISNDELTKFVDTNDKWIRTRTGILQRHIAGDAEYTSHLAFKSAQKAIEDAMISVDDIDLIIICTTTPDNSFPSVATKLHGYLGLTNIPSFDLQAVCAGFIYGLQLAHSLIVSGKYKTILLIGAEKMTSLLDWNDRSTCVLFGDGAGSVILQRSNDDSGLIDSNIFSSGTDYEILYTSGGTSMNGTSGKIVMQGQKLFRHAIEKMLQSIEDLLYANQFSVSDIDYFIPHQANIRIINKLAELLNIEEHKVVKTVEKHANCSAASIPLALSALKESGKIKKGDILLFSAIGAGLTWGGALIRW | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 34507
Sequence Length: 317
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
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Q1AW87 | MNRAYGKMLGVGRALGGRVVTNRDLEAVLDTSDEWISTRTGIRERRFVAEGQSCVTLAVEAARRALEHAGVPGASVDLVVCATSTNPESMPSVACLVGEAVGAAGVGAMDLSAACAGFAYAASVAGAMLASGLASRVLLVGADEMTSIVNVRDRSTGILFGDGAGAVVLDRGDGSSGFVDHILGADGRMAPLGRAGHPGDGKRPLYQNGREIFRFAVRMFPEMVEKIMARNGISLDEVQYIIPHQANARIIQAAARKLEVPEEKLVVNVDRFGNTSAASIPLSYPDIFDGLEPGKYIITVGFGFGLTWAANLYRI | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 33115
Sequence Length: 315
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
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Q1GI69 | MTRRAVVIGAGHYLPDRIVENAEFEATLDTSDEWIRSRSGIERRHFAAEGETTSHMATRAAEAALKSAGRSADDVDAIVLATSTADLTFPSAATMVQSQLGMTKGFAFDVQAVCAGFVYALSNANALIASGQADRVLVIGAETFSRIMDWTDRSTCVLFGDGAGALLLEAQEGEGTSKDRGILATDLNSDGRYKDLLYVDGGVSTQSTGYLRMQGNQVFRHAVEKLASTAHTALERAGASTDEVDWIVPHQANIRIIQGTAKKMGLPMDKVVVTVQDHGNTSAASIPLALSVGVERGQIKPGDLIVTEAIGGGLAWGAVVLRW | Function: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
Catalytic Activity: acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA
Sequence Mass (Da): 34239
Sequence Length: 323
Domain: The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.180
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O15540 | MVEAFCATWKLTNSQNFDEYMKALGVGFATRQVGNVTKPTVIISQEGDKVVIRTLSTFKNTEISFQLGEEFDETTADDRNCKSVVSLDGDKLVHIQKWDGKETNFVREIKDGKMVMTLTFGDVVAVRHYEKA | Function: B-FABP could be involved in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. It is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers (By similarity).
Sequence Mass (Da): 14889
Sequence Length: 132
Domain: Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.
Subcellular Location: Cytoplasm
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P10790 | MVDAFVGTWKLVDSKNFDDYMKSLGVGFATRQVGNMTKPTTIIEVNGDTVIIKTQSTFKNTEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHVQKWNGQETSLVREMVDGKLILTLTHGTAVCTRTYEKQA | Function: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
Sequence Mass (Da): 14779
Sequence Length: 133
Domain: Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.
Subcellular Location: Cytoplasm
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P05413 | MVDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEKEA | Function: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
Sequence Mass (Da): 14858
Sequence Length: 133
Domain: Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.
Subcellular Location: Cytoplasm
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O13008 | MAEAFAGTWNLKDSKNFDEYMKALGVGFATRQVGGMTKPTTIIEVAGDTVTLKTQSTFKNTEISFKLGAEFDETTADDRKVKSLITIDGGKMVHVQKWDGKETTLVREVSGNALELTLTLGDVVSTRSYVKAE | Function: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
Sequence Mass (Da): 14529
Sequence Length: 133
Domain: Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.
Subcellular Location: Cytoplasm
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P07483 | MADAFVGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDTITIKTHSTFKNTEISFQLGVEFDEVTADDRKVKSVVTLDGGKLVHVQKWDGQETTLTRELSDGKLILTLTHGNVVSTRTYEKEA | Function: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
Sequence Mass (Da): 14775
Sequence Length: 133
Domain: Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.
Subcellular Location: Cytoplasm
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P12104 | MAFDSTWKVDRSENYDKFMEKMGVNIVKRKLAAHDNLKLTITQEGNKFTVKESSAFRNIEVVFELGVTFNYNLADGTELRGTWSLEGNKLIGKFKRTDNGNELNTVREIIGDELVQTYVYEGVEAKRIFKKD | Function: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor.
Sequence Mass (Da): 15207
Sequence Length: 132
Domain: Forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior.
Subcellular Location: Cytoplasm
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A6X0K0 | MSDANQTKLEAADIQDLLAVLPHRYPFLLIDRIVDIDGDVSATGIKNVTINEPHFTGHFPEKPIMPGVLIVEAMAQTAGAISLLQRKTGRPGVVYFMTIDNAKFRRPVIPGDRLLLHVKKIKQRANISKYECIAEVDGVKVAEAEVAAMISTAEESQ | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17234
Sequence Length: 157
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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Q8K9S4 | MNSDEYIFNIKDILNILPHRYPFLLIDRILDFKAFQYLKALKNCTVNEPFFQGHFIKEPVFPGVLMIEAMSQAAAVLIFKSIGKLNINQLYYFVGIENTRFKKIVVPGDQIFIEVIYLKSKKNFIKFKIFAIVNKKNVCKSTIIFYKKNIFN | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17857
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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Q89AN9 | MYNSNITDITTLLPHRYPFLLIDRIIAYQKNFNILTIKNISYSEFCFTGHFYKNPVFPGVLILEAIAQSACLLVYKSFGMSYKNNLFYLTNIIDVKFKKKVIPGDQMLINVFVDKHHHRLIRFVGHVSVSKYIVCKATISCLLTNDVVSR | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs (By similarity).
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17358
Sequence Length: 150
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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B8INJ5 | MEPDAMTETPTELGTADIMRVMELLPHRYPFLLVDRITAINGDDSCIGIKNVTINEPQFTGHFPAMPVFPGVLLVEGMAQTAGAICCAHKLQNNTKPSRVYLMTIDKVKFRKPVVPGDTVEYHMKKVSNRRFMWWFRGEAKVNGVLVAEAEIGAMLVTE | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17765
Sequence Length: 159
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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B0JIT3 | MTIVTEALTELEPVIKTTFTVEEIRQLLPHRYPFALVDRIIDYVPGQKAVGLKNVTINEPFFPGHIPNRPLMPGVLIVESMAQVGGVILTQLPGMKGKFFAFAGIDKTRFRRPVVPGDQLIMTVELLSFKMNKIAKMQGEARVDGQLAAQGEMMFSIFD | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 17717
Sequence Length: 159
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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Q2RLY7 | MDWNAIQGILPHRYPFLLVDRVLEVEAGRRAVGQKNVSGNEWYFSGHFPGQPVMPGVLIMEALAQVGAVALLSLPEFQGRLALFGGMDRVRFRRQVVPGDVLRLETEIIKLKGRVGKGYGRAFVGEELAAEGELLFAVGEKIE | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 15789
Sequence Length: 143
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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Q1D386 | MDIGEILNLLPHRYPFLLVDRVVEIIPGQKLTAYKNVTINEPFFNGHFPGHPVMPGVLILEALAQATAILAYKSENMDPSRKLTYLMGVDGARFRKPVLPGDRLQLEIEVVRHKGAVWKTKGLATVDGARVAEGEFLATVVDKDADAAESAAS | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 16734
Sequence Length: 153
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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B2A8L3 | MKDINEIKELIPHRYPILMVDRLEELEPGHRAKGVKNVSANEPFLQGHFPDRPLMPGVLQIEAMAQVGACALMSLPENEGKLAVFGGVDKVKFKRQVQPGDVLSIEVELTRVKGSIGKGEGKVYVGDELAAQGQLTFALVEK | Function: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O
Sequence Mass (Da): 15545
Sequence Length: 142
Subcellular Location: Cytoplasm
EC: 4.2.1.59
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Q9SZ42 | MAVSLPTKYPLRPITNIPKSHRPSLLRVRVTCSVTTTKPQPNREKLLVEQRTVNLPLSNDQSLQSTKPRPNREKLVVEQRLASPPLSNDPTLKSTWTHRLWVAAGCTTLFVSLAKSVIGGFDSHLCLEPALAGYAGYILADLGSGVYHWAIDNYGDESTPVVGTQIEAFQGHHKWPWTITRRQFANNLHALAQVITFTVLPLDLAFNDPVFHGFVCTFAFCILFSQQFHAWAHGTKSKLPPLVVALQDMGLLVSRRQHAEHHRAPYNNNYCIVSGAWNNVLDESKVFEALEMVFYFQLGVRPRSWSEPNSDWIEETEISNNQA | Function: Fatty acid desaturase involved in the production of chloroplast-specific phosphatidylglycerol molecular species containing 16:1(3E). Catalyzes the formation of a trans double bond introduced close to the carboxyl group of palmitic acid, which is specifically esterified to the sn-2 glyceryl carbon of phosphatidylglycerol.
Catalytic Activity: a 1-acyl-2-hexadecanoyl-glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a 1-acyl-2-[(3E)-hexadec-3-enoyl]-glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36380
Sequence Length: 323
Domain: The histidine box domains are involved in binding the catalytic metal ions.
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Plastid
EC: 1.14.19.43
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Q9Y1W0 | MYYSNKMSKVITGKQYSWSELAKHNTENDCWVAVDGKVYDITRWVPLHPGGKEVLLLAAGRDVTNLFESYHPMSDKPTSILKNYEIGYISSYEHPKFVQKSDFYKTLKERVRKHFKATDQDPQMAVSIFSRLALVYLLVFVTYYLAHYTSNNFYLNCFLAIVYALCNSLFSMHMMHDSCHAAISHYPGVWKWMGASFDFVTGASFLSWCHQHVIGHHIYTNVRNADPDLGQGEVDFRIVTPFQTRSWYHKYQHIYAPLLYGIYTLKYRTQDWEAFVKDGKNGAIRVSVATNFDKAAYVIGKLSFVFFRFILPLRYHSFTDLICYFLIAEFVFGWYLTINFQVSHVAEDLKFFATPERPDEPSQINEDWAILQLKTTQDYGHGSLLCTFFSGSLNHQVVHHLFPSIAQDFYPQLVPIVKEVCKEHNITYHIKPNFTEAIMSHINYLYKMGNDPDYVKKPLASKDD | Function: Specific for desaturation of the 5 position in C16 and C18 fatty acids.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54005
Sequence Length: 464
Domain: The histidine box domains may contain the active site and/or be involved in metal ion binding.
Subcellular Location: Membrane
EC: 1.14.19.-
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P46312 | MASRIADSLFAFTGPQQCLPRVPKLAASSARVSPGVYAVKPIDLLLKGRTHRSRRCVAPVKRRIGCIKAVAAPVAPPSADSAEDREQLAESYGFRQIGEDLPENVTLKDIMDTLPKEVFEIDDLKALKSVLISVTSYTLGLFMIAKSPWYLLPLAWAWTGTAITGFFVIGHDCAHKSFSKNKLVEDIVGTLAFLPLVYPYEPWRFKHDRHHAKTNMLVHDTAWQPVPPEEFESSPVMRKAIIFGYGPIRPWLSIAHWVNWHFNLKKFRASEVNRVKISLACVFAFMAVGWPLIVYKVGILGWVKFWLMPWLGYHFWMSTFTMVHHTAPHIPFKPADEWNAAQAQLNGTVHCDYPSWIEILCHDINVHIPHHISPRIPSYNLRAAHESIQENWGKYTNLATWNWRLMKTIMTVCHVYDKEENYIPFDRLAPEESQPITFLKKAMPNYTA | Function: Chloroplast omega-6 fatty acid desaturase introduces the second double bond in the biosynthesis of 16:3 and 18:3 fatty acids, important constituents of plant membranes. It is thought to use ferredoxin as an electron donor and to act on fatty acids esterified to galactolipids, sulfolipids and phosphatidylglycerol.
Catalytic Activity: a (9Z)-octadecenoyl-containing glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51226
Sequence Length: 448
Domain: The histidine box domains may contain the active site and/or be involved in metal ion binding.
Pathway: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
Subcellular Location: Plastid
EC: 1.14.19.23
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P48629 | MESAITISNHVNLAFSLSRNPSLSTKNSAGISCIKWQRPCLRNLGHVRLNQQRKGTRRKSTLVQAVAVPVAQPSAFPPTDNTEHLKQLAERYGFQQIGEPLPDDVTMRDIITSLPKQVFEINDTKAWGTVLISVTSYALGIFMIAKAPWYLLPLAWAWTGTAITGFFVIGHDCAHKSFSKNKLVEDIVGTLAFMPLIYPYEPWRFKHDQHHTKTNMLREDTAWLPIMKEDIESSPGLRKALIYAYGPLRTWMSIAHWLKVHFNLKDFRQSEVKRATISLAAVFAFMVIGWPLIIYKTGIVGWIKFWLMPWLGYHFWMSTFTIVHHTAPHIPFKSSKEWNAAQAQLSGTVHCDYPRWIEILCHDISVHIPHHISPKIPSYNLRAANQSLNENWGEYLNKPKSNWRLMRTIMTTCHIYDKDGNYVSFEKAVPEESQPISIPKRVMPDYA | Function: Chloroplast omega-6 fatty acid desaturase introduces the second double bond in the biosynthesis of 16:3 and 18:3 fatty acids, important constituents of plant membranes. It is thought to use ferredoxin as an electron donor and to act on fatty acids esterified to galactolipids, sulfolipids and phosphatidylglycerol.
Catalytic Activity: a (9Z)-octadecenoyl-containing glycerolipid + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = a (9Z,12Z)-octadecadienoyl-containing glycerolipid + 2 H2O + 2 oxidized [2Fe-2S]-[ferredoxin]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 51306
Sequence Length: 447
Domain: The histidine box domains may contain the active site and/or be involved in metal ion binding.
Pathway: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
Subcellular Location: Plastid
EC: 1.14.19.23
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P46313 | MGAGGRMPVPTSSKKSETDTTKRVPCEKPPFSVGDLKKAIPPHCFKRSIPRSFSYLISDIIIASCFYYVATNYFSLLPQPLSYLAWPLYWACQGCVLTGIWVIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKQKSAIKWYGKYLNNPLGRIMMLTVQFVLGWPLYLAFNVSGRPYDGFACHFFPNAPIYNDRERLQIYLSDAGILAVCFGLYRYAAAQGMASMICLYGVPLLIVNAFLVLITYLQHTHPSLPHYDSSEWDWLRGALATVDRDYGILNKVFHNITDTHVAHHLFSTMPHYNAMEATKAIKPILGDYYQFDGTPWYVAMYREAKECIYVEPDREGDKKGVYWYNNKL | Function: ER (microsomal) omega-6 fatty acid desaturase introduces the second double bond in the biosynthesis of 18:3 fatty acids, important constituents of plant membranes . Delta(12)-desaturase with regioselectivity determined by the double bond (delta(9) position) and carboxyl group of the substrate. Can use both 16:1 and 18:1 fatty acids as substrates . It is thought to use cytochrome b5 as an electron donor and to act on fatty acids esterified to phosphatidylcholine (PC) and, possibly, other phospholipids . Very low constitutive hydroxylation activity . Required for desaturation of fatty acids present in extraplastidial membranes, including mitochondria . Required for salt tolerance during seed germination and early seedling growth .
Catalytic Activity: (9Z)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (9Z,12Z)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44048
Sequence Length: 383
Domain: The histidine box domains may contain the active site and/or be involved in metal ion binding (Probable). The C-terminal sequence (-YNNKL) is necessary and sufficient for maintaining localization in the endoplasmic reticulum .
Pathway: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.19.22
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Q39287 | MGAGGRMQVSPSPKKSETDTLKRVPCETPPFTVGELKKAIPPHCFKRSIPRSFSYLIWDIIVASCFYYVATTYFPLLPHPLSYVAWPLYWACQGVVLTGVWVIAHECGHHAFSDYQWLDDTVGLIFHSFLLVPYFSWKYSHRRHHSNTGSLERDEVFVPKKKSDIKWYGKYLNNPLGRTVMLTVQFTLGWPLYWAFNVSGRPYPEGFACHFHPNAPIYNDRERLQIYVSDAGILAVCYGLYRYAAAQGVASMVCLYGVPLLIVNAFLVLITYLQHTHPSLPHYDSSEWDWLRGALATVDRDYGILNKVFHNITDTHVAHHLFSTMPHYHAMEVTKAIKPILGDYYQFDGTPWVKAMWREAKECIYVEPDRQGEKKGVFWYNNKL | Function: ER (microsomal) omega-6 fatty acid desaturase introduces the second double bond in the biosynthesis of 18:3 fatty acids, important constituents of plant membranes. It is thought to use cytochrome b5 as an electron donor and to act on fatty acids esterified to phosphatidylcholine and, possibly, other phospholipids (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44315
Sequence Length: 384
Domain: The histidine box domains may contain the active site and/or be involved in metal ion binding.
Pathway: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.19.-
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I6XHI4 | MGYPVIVEATRSPIGKRNGWLSGLHATELLGAVQKAVVDKAGIQSGLHAGDVEQVIGGCVTQFGEQSNNISRVAWLTAGLPEHVGATTVDCQCGSGQQANHLIAGLIAAGAIDVGIACGIEAMSRVGLGANAGPDRSLIRAQSWDIDLPNQFEAAERIAKRRGITREDVDVFGLESQRRAQRAWAEGRFDREISPIQAPVLDEQNQPTGERRLVFRDQGLRETTMAGLGELKPVLEGGIHTAGTSSQISDGAAAVLWMDEAVARAHGLTPRARIVAQALVGAEPYYHLDGPVQSTAKVLEKAGMKIGDIDIVEINEAFASVVLSWARVHEPDMDRVNVNGGAIALGHPVGCTGSRLITTALHELERTDQSLALITMCAGGALSTGTIIERI | Function: Involved in the beta-oxidation of the cholesterol side chain . It is important for utilization of cholesterol as a sole carbon source in vitro and for full virulence in the chronic stage of mouse lung infection . Catalyzes the thiolysis of 3,22-dioxochol-4-en-24-oyl-CoA to yield 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA) and acetyl-CoA . Also able to use acetoacetyl-CoA (AcAcCoA) as substrate .
Catalytic Activity: acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA
Sequence Mass (Da): 41329
Sequence Length: 391
Pathway: Steroid metabolism; cholesterol degradation.
EC: 2.3.1.16
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I6XHJ3 | MPRVDDDAVGVPLTGNGRGAVMTEAYVIDAVRTAVGKRGGALAGIHPVDLGALAWRGLLDRTDIDPAAVDDVIAGCVDAIGGQAGNIARLSWLAAGYPEEVPGVTVDRQCGSSQQAISFGAQAIMSGTADVIVAGGVQNMSQIPISSAMTVGEQFGFTSPTNESKQWLHRYGDQEISQFRGSELIAEKWNLSREEMERYSLTSHERAFAAIRAGHFENEIITVETESGPFRVDEGPRESSLEKMAGLQPLVEGGRLTAAMASQISDGASAVLLASERAVKDHGLRPRARIHHISARAADPVFMLTGPIPATRYALDKTGLAIDDIDTVEINEAFAPVVMAWLKEIKADPAKVNPNGGAIALGHPLGATGAKLFTTMLGELERIGGRYGLQTMCEGGGTANVTIIERL | Function: May be involved in the final steps of cholesterol and steroid degradation . Catalyzes the formation of 4-methyl-5-oxo-octanedioyl-CoA (MOODA-CoA) and acetyl-CoA from 6-methyl-3,7-dioxodecanedioyl-CoA (MeDODA-CoA) and coenzyme A (Probable).
Catalytic Activity: acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA
Sequence Mass (Da): 42981
Sequence Length: 407
Pathway: Steroid metabolism; cholesterol degradation.
EC: 2.3.1.16
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P46154 | MSGNRGVVYLGSGKVEVQKIDYPKMQDPRGKKIEHGVILKVVSTNICGSDQHMVRGRTTAQVGLVLGHEITGEVIEKGRDVENLQIGDLVSVPFNVACGRCRSCKEMHTGVCLTVNPARAGGAYGYVDMGDWTGGQAEYLLVPYADFNLLKLPDRDKAMEKIRDLTCLSDILPTGYHGAVTAGVGPGSTVYVAGAGPVGLAAAASARLLGAAVVIVGDLNPARLAHAKAQGFEIADLSLDTPLHEQIAALLGEPEVDCAVDAVGFEARGHGHEGAKHEAPATVLNSLMQVTRVAGKIGIPGLYVTEDPGAVDAAAKIGSLSIRFGLGWAKSHSFHTGQTPVMKYNRALMQAIMWDRINIAEVVGVQVISLDDAPRGYGEFDAGVPKKFVIDPHKTFSAA | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the NAD(+)-dependent oxidation of formaldehyde and acetaldehyde, and, to a lesser extent, long-chain alcohols, but is inactive against propionaldehyde, butyraldehyde, methanol and ethanol. Can also catalyze the dismutation of a wide range of aldehydes such as formaldehyde.
Catalytic Activity: formaldehyde + H2O + NAD(+) = formate + 2 H(+) + NADH
Sequence Mass (Da): 42082
Sequence Length: 399
EC: 1.2.1.46
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P10384 | MSQKTLFTKSALAVAVALISTQAWSAGFQLNEFSSSGLGRAYSGEGAIADDAGNVSRNPALITMFDRPTFSAGAVYIDPDVNISGTSPSGRSLKADNIAPTAWVPNMHFVAPINDQFGWGASITSNYGLATEFNDTYAGGSVGGTTDLETMNLNLSGAYRLNNAWSFGLGFNAVYARAKIERFAGDLGQLVAGQIMQSPAGQTQQGQALAATANGIDSNTKIAHLNGNQWGFGWNAGILYELDKNNRYALTYRSEVKIDFKGNYSSDLNRAFNNYGLPIPTATGGATQSGYLTLNLPEMWEVSGYNRVDPQWAIHYSLAYTSWSQFQQLKATSTSGDTLFQKHEGFKDAYRIALGTTYYYDDNWTFRTGIAFDDSPVPAQNRSISIPDQDRFWLSAGTTYAFNKDASVDVGVSYMHGQSVKINEGPYQFESEGKAWLFGTNFNYAF | Function: Involved in translocation of long-chain fatty acids across the outer membrane. It is a receptor for the bacteriophage T2. FadL may form a specific channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48542
Sequence Length: 446
Subcellular Location: Cell outer membrane
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P77712 | MQTQIKVRGYHLDVYQHVNNARYLEFLEEARWDGLENSDSFQWMTAHNIAFVVVNININYRRPAVLSDLLTITSQLQQLNGKSGILSQVITLEPEGQVVADALITFVCIDLKTQKALALEGELREKLEQMVK | Function: Long-chain acyl-CoA thioesterase that could be involved in beta-oxidation of fatty acids . Is most active with 3,5-tetradecadienoyl-CoA, a metabolite of oleic acid that is hydrolyzed during oleate beta-oxidation, but can also use other substrates such as 3,5-dodecadienoyl-CoA, 9-cis-octadecenoyl-CoA, octadecanoyl-CoA, hexadecanoyl-CoA, 3-hydroxytetradecanoyl-CoA and tetradecanoyl-CoA .
Catalytic Activity: (3E,5Z)-tetradecadienoyl-CoA + H2O = (3E,5Z)-tetradecadienoate + CoA + H(+)
Sequence Mass (Da): 15088
Sequence Length: 132
EC: 3.1.2.-
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O32178 | MHKHIRKAAVLGSGVMGSGIAAHLANIGIPVLLLDIVPNDLTKEEEKKGLTKDSSEVRSRLSRQAMKKLLKQKPAPLTSAKNTSYITPGNLEDDAEKLKEADWIIEVVVENLEVKKKIFALVDEHRKTGSIVSSNTSGISVQEMAEGRSDDFKAHFLGTHFFNPARYLKLLEIIPIKETDPDILKFMTAFGENVLGKGVVTAKDTPNFIANRIGTYGLLVTVQEMLKGGYQVGEVDSITGPLIGRPKSATFRTLDVVGLDTFAHVARNVYDKADGDEKEVFRIPSFMNDMLEKGWIGSKAGQGFYKKEGKTIYELDPVTLTYGERTKMKSPALEAAKQAKGTKAKMKALIYSDDRAGRLLWNITSQTLLYSAELLGEIADDIHAIDQAMKWGFGWELGPFEMWDAIGLKQSAEKLEQLGADMPGWIKEMLDKGNETFYIKENGTVFYYDRGEYRAVKENKKRIHLQALKETKGVIAKNSGASLIDLGDDVALLEFHSKSNAIGLDIIQMIHKGLEETERNYKGLVIGNQGKNFCVGANLAMILMEVQDDNFLEVDFVIRRFQETMMKIKYSAKPVVAAPFGMTLGGGTEACLPAARIQAASEAYMGLVESGVGLIPGGGGNKELYINHLRRGHDPMNAAMKTFETIAMAKVSASAQEAREMNILKETDQISVNQDHLLYDAKQLAASLYDTGWRPPVKEKVKVPGETGYAALLLGAEQMKLSGYISEHDFKIAKKLAYVIAGGKVPFGTEVDEEYLLEIEREAFLSLSGEAKSQARMQHMLVKGKPLRN | Function: Involved in the degradation of long-chain fatty acids.
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH
Sequence Mass (Da): 87085
Sequence Length: 789
Pathway: Lipid metabolism; fatty acid beta-oxidation.
EC: 1.1.1.35
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Q2HJ98 | MAASRPLSRFWEWGKNIVCVGRNYADHVREMQSAAPSEPVLFLKPSTAYAPEGSPVLVPAYTRNLHHELELAVVMGKRCRAVSEAAAMDYVAGYALCLDMTARDVQDECKKKGLPWTLAKSFTASCPVSAFVPKEKIPDPHNLKLWLKVNGELRQEGETSSMIFSIPYIISYVSKIMTLEEGDIILTGTPKGVGPVKENDEIQAGIHGVLSMKFKVERPEY | Function: Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro. Also has oxaloacetate decarboxylase activity.
Catalytic Activity: a 3-acylpyruvate + H2O = a carboxylate + H(+) + pyruvate
Sequence Mass (Da): 24499
Sequence Length: 221
Subcellular Location: Mitochondrion
EC: 3.7.1.5
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Q86I22 | MNKFWETGRKIVAVGRNYAQHAKELGNEIPSEPFFFLKPTSSYLLQGTGPIEIPLESSDIHHEVELGIVIGKKGRDIDLKSAMDYVSGYTLALDMTSRDQQSIAKAKSLPWTVSKGYDTFCPISGFIPKDKIKDLNNVELWCSVDGQIKQKGNTNQMIFDVPHLIQYISSIMTLESGDLILTGTPSGVGPVKPGQVIKCGITGLDTDMQFDIILRKRN | Function: Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro.
Catalytic Activity: a 3-acylpyruvate + H2O = a carboxylate + H(+) + pyruvate
Sequence Mass (Da): 24149
Sequence Length: 218
Subcellular Location: Mitochondrion
EC: 3.7.1.5
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Q6P587 | MGIMAASRPLSRFWEWGKNIVCVGRNYADHVREMRSAVLSEPVLFLKPSTAYAPEGSPILMPAYTRNLHHELELGVVMGKRCRAVPEAAAMDYVGGYALCLDMTARDVQDECKKKGLPWTLAKSFTASCPVSAFVPKEKIPDPHKLKLWLKVNGELRQEGETSSMIFSIPYIISYVSKIITLEEGDIILTGTPKGVGPVKENDEIEAGIHGLVSMTFKVEKPEY | Function: Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro . Also has oxaloacetate decarboxylase activity .
Catalytic Activity: a 3-acylpyruvate + H2O = a carboxylate + H(+) + pyruvate
Sequence Mass (Da): 24843
Sequence Length: 224
Subcellular Location: Mitochondrion
EC: 3.7.1.5
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Q9LUR3 | MATSMIQRLFKQGTKIVGVGLNYASHAKELGNALPKDPIVFLKPTSSYLENGGTIEIPHPLDSLHHEVELAVVIGQKARDVPERLAMNYIGGYALALDMTARELQVSAMASGLPCTLAKGQDTFTPISSVLPKAMVLDPNNLELWLKVDDETRQKGWTKDMIFKVPYLISYISSVMTLFKGDVILTGTPEGIGPVKIGQKITAGITGLSEVQFDVGRRLKPLLR | Function: Probable acylpyruvase. Binds copper in vitro.
Catalytic Activity: a 3-acylpyruvate + H2O = a carboxylate + H(+) + pyruvate
Sequence Mass (Da): 24417
Sequence Length: 224
Subcellular Location: Mitochondrion
EC: 3.7.1.5
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Q10B63 | MAAAAQRLLAASTKIVGVGRNFVAHAKELGNPVPKEPVLFLKPTSSFLHAGVAGAAIEVPEPVESLHHEVELAVVISQRARDVPEASAMDFVGGYALALDMTARELQSAAKSAGLPWTLGKAQDTFTPISAVIPKSDVANPDDLELWLKVDDELRQKGSTSDMIFKIPSLISYISSIMTLMEGDVILTGTPEGVGPVRPGQKIKAGITGLIDVEFDVQKRKRSFST | Function: Probable acylpyruvase.
Catalytic Activity: a 3-acylpyruvate + H2O = a carboxylate + H(+) + pyruvate
Sequence Mass (Da): 24071
Sequence Length: 226
Subcellular Location: Mitochondrion
EC: 3.7.1.5
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Q8RW90 | MALLKSFIDVGSDSHFPIQNLPYGVFKPESNSTPRPAVAIGDLVLDLSAISEAGLFDGLILKDADCFLQPNLNKFLAMGRPAWKEARSTLQRILSSNEPILRDNDVLRRKSFHQMSKVEMIVPMVIGDYTDFFASMHHAKNCGLMFRGPENAINPNWFRLPIAYHGRASSIVISGTDIIRPRGQGHPQGNSEPYFGPSKKLDFELEMAAVVGPGNELGKPIDVNNAADHIFGLLLMNDWSARDIQAWEYVPLGPFLGKSFGTTISPWIVTLDALEPFGCQAPKQDPPPLPYLAEKESVNYDISLEVQLKPSGRDDSCVITKSNFQNLYWTITQQLAHHTVNGCNLRPGDLLGTGTISGPEPDSYGCLLELTWNGQKPLSLNGTTQTFLEDGDQVTFSGVCKGDGYNVGFGTCTGKIVPSPP | Function: Converts fumarylacetoacetate to acetoacetate and fumarate . Involved in tyrosine catabolic pathway. Catalyzes the final step in the tyrosine degradation pathway .
Catalytic Activity: 4-fumarylacetoacetate + H2O = acetoacetate + fumarate + H(+)
Sequence Mass (Da): 46095
Sequence Length: 421
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 6/6.
EC: 3.7.1.2
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Q9UTM9 | MSRTIVIVGCGVFGLSTAVELAKNHSFDNIIAIDAEPVPSSMSAANDINKIVRPEYADLKYMKLALEAMEKWRNDPELSSVYFECGRLSTISKDPYRARFDEVAQRNLRKLLGDSALINLSSSEEIRKKYPSLFSNSPLRSDMQAVVNEHAGYANSAASLKLLELKARELGVEFVFGKAGKFKKFVVNHSETDIDKNDNHVSVQTEDGTIYHADTILLAVGAYLNAYLNTSHRVCAKGLPVAHIQLTDEEFKTYKNMPIIFDPDCAYAFPPYPVTKLIKLASTGYEYVCNVETDYDENSKVVSIPHSGPSKSSLPKYAIIQMRRFLDTFLPDLADRSLINTKMCWISDTEDANFLIDKVPQFDNVFVANGDSGHAFKFLPNIGRYIAQRILGDLSEEWKDAWRWREDDKASELKWRCVRSLIDYKDAEFTYDK | Catalytic Activity: H2O + L-saccharopine + O2 = (S)-2-amino-6-oxohexanoate + H2O2 + L-glutamate
Sequence Mass (Da): 48974
Sequence Length: 433
Subcellular Location: Secreted
EC: 1.5.3.18
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O31724 | MDQQIYSLQKKVEEHKEELIQLAKTLISYQTPAPPARNTEGIQSWIAGYLNELGFSIDKWDVYPGDPNVVGKLKGTDSADYYSLIINGHVDVAEVKEDEEWKHDPFHPIEKNGLLIGRGASDMKGGMACVLFAVKLIREASIELPGDLILQSVIGEEVGEAGTLECCKRGYHADFAIVADTSDMHIQGQGGVITGWIEIKSSQTFHDGTRRNMIHAGGGTFGASAIEKMAKIIAGLGELERHWSIMKSYPGFKPGTNTINPAVIEGGRHAAFIADECRLWITVHFYPNETHDQVAAEIEDYVNRLSDSDIWLRENRPVFKWGGSSMIEDRGEIFPALEVDPGHPGVLALTASHQKVKRECPIIDVSQSVTDGGWLYDAGIPCVIYGPGDLHNAHSVNEKVSIEQLVEYTKIILDFIISWCSRKKEQ | Cofactor: Binds 2 Zn(2+) or Co(2+) ions per subunit.
Function: Catalyzes the deformylation of the formylaminopyrimidine N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine (FAMP) to give the corresponding aminopyrimidine.
Catalytic Activity: H2O + N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine = 4-amino-5-aminomethyl-2-methylpyrimidine + formate
Sequence Mass (Da): 47153
Sequence Length: 426
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
EC: 3.5.1.-
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P21268 | MKTPTRVSFEKKIHTPPSGDRDAERSPPKKFLRGLSGKVFRKTPEFKKQQMPTFGYIEESQFTPNLGLMMSKRGNIPKPLNLSKPISPPPSLKKTAGSVASGFSKTGQLSALQSPVNITSSNKYNIKATNLTTSLLRESISDSTTMCDTLSDINLTVMDEDYRIDGDSYYEEDSPTFMISLERNIKKCNSQFSPKRYIGEKCLICEESISSTFTGEKVVESTCSHTSHYNCYLMLFETLYFQGKFPECKICGEVSKPKDKDIVPEMVSKLLTGAGAHDDGPSSNMQQQWIDLKTARSFTGEFPQFTPQEQLIRTADISCDGFRTPRLSNSNQFEAVSYLDSPFLNSPFVNKMATTDPFDLSDDEKLDCDDEIDESAAEVWFSKTGGEHVMVSVKFQEMRTSDDLGVLQDVNHVDHEELEEREKEWKKKIDQYIETNVDKDSEFGSLILFDKLMYSDDGEQWVDNNLVILFSKFLVLFDFEEMKILGKIPRDQFYQVIKFNEDVLLCSLKSTNIPEIYLRFNENCEKWLLPKWKYCLENSSLETLPLSEIVSTVKELSHVNIIGALGAPPDVISAQSHDSRLPWKRLHSDTPLKLIVCLNLSHADGELYRKRVLKSVHQILDGLNTDDLLGIVVVGRDGSGVVGPFGTFIGMINKNWDGWTTFLDNLEVVNPNVFRDEKQQYKVTLQTCERLASTSAYVDTDDHIATGYAKQILVLNGSDVVDIEHDQKLKKAFDQLSYHWRYEISQRRMTPLNASIKQFLEELHTKRYLDVTLRLPQATFEQVYLGDMAAGEQKTRLIMDEHPHSSLIEIEYFDLVKQQRIHQTLEVPNL | Function: Inhibitor of the cyclin-dependent kinase CDC28. Necessary for cell cycle arrest. Involved in pheromone response. Contributes to mating efficiency. Required for oriented polarization of yeast cells in response to mating pheromones.
PTM: Thought to be phosphorylated by MAP kinase FUS3. Thought to enhance the binding of FAR1 to G1-specific cyclin-dependent kinase (CDK) complexes.
Sequence Mass (Da): 94572
Sequence Length: 830
Domain: There is evidence to suggest that the N-terminal part may be sufficient for cell cycle arrest and the C-terminal may be necessary for some step in mating.
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G5EGH6 | MTVKTRASIAKKIEKDGLDSQYLFMDPNEVLQVQEESKKIPYKMEIVWRNVALFAALHVAAAIGLYELVFHAKWQTAVFSFALYVFSGFGITAGAHRLWSHKSYKATTPMRIFLMLLNNIALQNDIIEWARDHRCHHKWTDTDADPHNTTRGFFFTHMGWLLVRKHPQVKEHGGKLDLSDLFSDPVLVFQRKHYFPLVILFCFILPTIIPVYFWKETAFIAFYVAGTFRYCFTLHATWCINSAAHYFGWKPYDTSVSAVENVFTTVVAVGEGGHNFHHTFPQDYRASEYSLIYNWTRVLIDTAAVLGLVYDRKTIADEFISRQVANHGSEESRKKSIM | Function: Delta(9)-fatty acid desaturase that acts preferentially on stearoyl-CoA (octadecanoyl-CoA) producing the monounsaturated oleoyl-CoA ((9Z)-octadecenoyl-CoA), one of the most abundant monounsaturated fatty acid in Caenorhabditis elegans phospholipids and triacylglycerols . Also acts on palmitoyl-CoA (hexadecanoyl-CoA), heptadecanoyl-CoA and (11E)-octadecenoyl-CoA (trans-vaccenoyl-CoA), the monounsaturated fatty acids (MUFAs) produced are further used by several other desaturases and elongases as substrates to synthesize polyunsaturated fatty acids (PUFAs) endogenously (PUFAs are essential for membrane structure and many cellular and physiological processes) . Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (By similarity). Partially inhibits expression of genes involved in beta-oxidation, such as ech-1 and acs-2, perhaps signaling via the actions of one of its fatty acid products . May form part of a negative feedback loop with the transcription factor nhr-49 to limit beta-oxidation, in which nhr-49 stimulates expression of fat-7 and acs-2, and in turn fat-7 indirectly inhibits acs-2 and other genes also involved in beta-oxidation .
Catalytic Activity: 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39062
Sequence Length: 338
Domain: The histidine box domains may contain the active site and/or be involved in metal ion binding.
Pathway: Lipid metabolism; monounsaturated fatty acid biosynthesis.
Subcellular Location: Membrane
EC: 1.14.19.-
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Q42561 | MLKLSCNVTDSKLQRSLLFFSHSYRSDPVNFIRRRIVSCSQTKKTGLVPLRAVVSADQGSVVQGLATLADQLRLGSLTEDGLSYKEKFVVRSYEVGSNKTATVETIANLLQEVGCNHAQSVGFSTDGFATTTTMRKLHLIWVTARMHIEIYKYPAWGDVVEIETWCQSEGRIGTRRDWILKDSVTGEVTGRATSKWVMMNQDTRRLQKVSDDVRDEYLVFCPQEPRLAFPEENNRSLKKIPKLEDPAQYSMIGLKPRRADLDMNQHVNNVTYIGWVLESIPQEIVDTHELQVITLDYRRECQQDDVVDSLTTTTSEIGGTNGSATSGTQGHNDSQFLHLLRLSGDGQEINRGTTLWRKKPSS | Function: Plays an essential role in chain termination during de novo fatty acid synthesis. Possesses high thioesterase activity for oleoyl-ACP versus other acyl-ACPs. Substrate preference is 18:1 > 18:0 > 16:1.
Catalytic Activity: (9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP]
Sequence Mass (Da): 40819
Sequence Length: 362
Subcellular Location: Plastid
EC: 3.1.2.14
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Q42712 | VYPHFKTPIQCRFLTSDSISIRRRTAVSRWRSPTFSANYNGVNAQVLGVLKQEQKEIEEEKRSSSLAEKLRLGSLTEDGLSYKEKFIVRCYEVGINKTATVETIANLLQEVGGNHAQSVGFSTDGFATTPTMRKLHLIWVTARMHIEIYRYPAWSDVVEIETWCQSEGRIGTRRDWIIKDFATDEVIGRATSKWVMMNQDTRRLQKVSDDVRDEYLVFCPKTPRLSFPEENNKSLKKISKLEDPAQHSRLGLSPRRADLDMNQHVNNVAYIGWVLESIPKEVLYTHELETITLDYRRECQHDDVVDSLTSPEVDEDTAVTKIIGTNGHAAAATEARDDSLKFLHFLRVSGQGLEINRGRTEWRKKSEKR | Function: Plays an essential role in chain termination during de novo fatty acid synthesis. High thioesterase activity for oleoyl-ACP versus other acyl-ACPs.
Catalytic Activity: (9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP]
Sequence Mass (Da): 42348
Sequence Length: 369
Subcellular Location: Plastid
EC: 3.1.2.14
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P11461 | MTHQVATCHKKQSFSGKPTLSRIALLVALQISASALPISITHAEEQADESITVYGQANEAYAAGKISKASSIGMLGDKDFLDTPFNAIGYTDKHIQDQHAQDISDVISASDPSVFTSGETGLNKESFKIRGFSSDIGDVMFNGLYGIAPYYRSSPEMYQRIDVLKGPASLLNGMPPNGSVGGSINLVTKRAQEAPITSFTGTYMSDSQFGGHIDIGRRFGENEQFGVRFNGVFRDGDASVDGQSRKAQLASLSLDWRNDIALIEADLYFSTERVDGPNRGLSIASGVDVPSPPSSDTLLSPSWAYNDSEDKGMMIRAELDLSNSVTAYGAVGASRTDFDSNVPQRVKIIDDSGTLEVSLGSVKLESKRTSGEVGIRSSFDTGPIEHYLVLNSTYFREDKNDSPTGNNNPGSWNPNIYNPVWGPEDSTYDNYYELPVDSTQISFGVADTLSLANGKYQVTLGLRHQSIDYESGVTWNGNAFPTTKLKESTYTPAIVALYKVSDSVSLYGNYTEGLTNGKTAGSGAANVGEAFEPQKTKQTEAGLKLDMNDFAHTFSLFEIKKPNGYQDPDTNIYSFGGEQRNRGIEWGFYGTVLEDYTLTGGIAYTDAEITKATDVTTEGKQATKLPDLQAKLALEWNLPVMRQLTLIGQANYMSEQYIDAQNTQSLSAQTIFDLGARYNSTIANQSVIWRLAVNNVTDEAYWTTTHYASLALGAPRTVMLSATADF | Function: Involved in the uptake of iron in complex with the siderophore anguibactin. Binds and transports ferric-anguibactin from the cell surface to the periplasm.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 78894
Sequence Length: 726
Subcellular Location: Cell outer membrane
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G3ESV0 | TAASSAFFPVPSADTSSRPGKLGNGPSSFSPLKPKSIPNGGLQVKASASAPPKINGSSVGLKSGGLKTHDDAPSAPPPRTFINQLPDWSMLLAAITTAFLAAEKQWMMLDRKPKRLDMLEDPFGLGRVVQDGLVFRQNFSIRSYEIGADRTASIETVMNHLQETALNHVKTAGLSNDGFGRTPEMYKRDLIWVVAKMQVMVNRYPTWGDTVEVNTWVAKSGKNGMRRDWLISDCNTGEILTRASSVWVMMNQKTRKLSKIPDEVRREIEPHFVDSAPVIEDDDRKLPKLDEKSADSIRKGLTPRWNDLDVNQHVNNAKYIGWILESTPPEVLETQELCSLTLEYRRECGRESVLESLTAVDPSGEGYGSQFQHLLRLEDGGEIVKGRTEWRPKNAGINGVVPSEESSPGDYS | Function: Plays an essential role in chain termination during de novo fatty acid synthesis (Probable). Possesses thioesterase activity for medium chain acyl-ACPs. Substrate preference is 14:0 > 16:0 > 16:1 .
Catalytic Activity: H2O + tetradecanoyl-[ACP] = H(+) + holo-[ACP] + tetradecanoate
Sequence Mass (Da): 45564
Sequence Length: 412
Subcellular Location: Plastid
EC: 3.1.2.-
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Q9SJE2 | MVATSATSSFFPVPSSSLDPNGKGNKIGSTNLAGLNSAPNSGRMKVKPNAQAPPKINGKKVGLPGSVDIVRTDTETSSHPAPRTFINQLPDWSMLLAAITTIFLAAEKQWMMLDWKPRRSDMLVDPFGIGRIVQDGLVFRQNFSIRSYEIGADRSASIETVMNHLQETALNHVKTAGLLGDGFGSTPEMFKKNLIWVVTRMQVVVDKYPTWGDVVEVDTWVSQSGKNGMRRDWLVRDCNTGETLTRASSVWVMMNKLTRRLSKIPEEVRGEIEPYFVNSDPVLAEDSRKLTKIDDKTADYVRSGLTPRWSDLDVNQHVNNVKYIGWILESAPVGIMERQKLKSMTLEYRRECGRDSVLQSLTAVTGCDIGNLATAGDVECQHLLRLQDGAEVVRGRTEWSSKTPTTTWGTAP | Function: Plays an essential role in chain termination during de novo fatty acid synthesis. Possesses high thioesterase activity for palmitoyl-ACP versus other acyl-ACPs. Substrate preference is 16:0 > 18:1 > 18:0 > 16:1. Plays an essential role in the supply of saturated fatty acids necessary for plant growth and seed development. Contributes to 16:0 production particularly in flowers. May be involved in the synthesis of long chain fatty acid.
Catalytic Activity: H2O + hexadecanoyl-[ACP] = H(+) + hexadecanoate + holo-[ACP]
Sequence Mass (Da): 45687
Sequence Length: 412
Subcellular Location: Plastid
EC: 3.1.2.-
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Q41635 | MATTSLASAFCSMKAVMLARDGRGMKPRSSDLQLRAGNAPTSLKMINGTKFSYTESLKRLPDWSMLFAVITTIFSAAEKQWTNLEWKPKPKLPQLLDDHFGLHGLVFRRTFAIRSYEVGPDRSTSILAVMNHMQEATLNHAKSVGILGDGFGTTLEMSKRDLMWVVRRTHVAVERYPTWGDTVEVECWIGASGNNGMRRDFLVRDCKTGEILTRCTSLSVLMNTRTRRLSTIPDEVRGEIGPAFIDNVAVKDDEIKKLQKLNDSTADYIQGGLTPRWNDLDVNQHVNNLKYVAWVFETVPDSIFESHHISSFTLEYRRECTRDSVLRSLTTVSGGSSEAGLVCDHLLQLEGGSEVLRARTEWRPKLTDSFRGISVIPAEPRV | Function: Plays an essential role in chain termination during de novo fatty acid synthesis. High thioesterase activity for lauroyl-ACP versus other acyl-ACPs.
Catalytic Activity: dodecanoyl-[ACP] + H2O = dodecanoate + H(+) + holo-[ACP]
Sequence Mass (Da): 42915
Sequence Length: 382
Subcellular Location: Plastid
EC: 3.1.2.21
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P11460 | MFKSTLNIAVAIVCSSLVTLTGCEPKVAQSQVIQPLETPIVIEHNLGQTVISNRPQRVAALDMNEVDFLDQLNVPIAGMVKDFVPHFLEKYKNTPDISDLGAIVQPNMEKIYALKPDLVLMTPLHANQYEELSKLAPTVHFDIDFRNSHGHHVDIIKQHVIDLGEIFNKQTLAQKKVAEIDAKVDEVQALTAERSEKALVVMHNNGSFSSFGIESRYGFVFDVLGVKPASTEIAASLHGQPISSEFINQANPDILYIIDRTAVMEGKPVIDAEHLANPLLRQTKAWKNGKVIFVDADAWYITSASITSLKIVIDDIIKGYQS | Function: Involved in the uptake of iron in complex with the siderophore anguibactin. Binds ferric-anguibactin in the periplasm and mediates its transport into the cytoplasm.
Location Topology: Lipid-anchor
Sequence Mass (Da): 35635
Sequence Length: 322
Subcellular Location: Cell inner membrane
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Q81XB2 | MITLDYRNKENVEVDSSLHNESRSASAFRSKKEARRYWIVLITLIALGLLSSYGLLVYNNPVPIDSPSFIPVVKRRIVAIVAMIIAAVCHSLSTVAFQSITNNKIITPSLLGFESLYSAIQTSTVFFFGASALINFNGIGSFLFQVVVMVFMSLILYGWLLSGKYGNLQLMLLVGIIIGTGLNSVSTFMRKLLAPSEFDILQARLFGSVNHADPAYFPIVIPMIIIVAVLIFAHSKNLNVLSLGKDVATSFGVKYQPSVIYTLVLVAILMSISTALIGPLTFYGFLVATLSYQAAATYDHRYIFPMAFAIGFLIMTSAYFLMYHVFHAQGVVSVIIELFGGIIFLTIVLRKRAL | Function: Part of an ABC transporter complex involved in ferric-petrobactin uptake. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39001
Sequence Length: 354
Subcellular Location: Cell membrane
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P37737 | MTSLNLNFRVSVVLVILLSIAFIFINSGFDLEYIIPRRLIKLSAIIIGGSCVAISAVIFQALARNRILTPSIMGYESIYLVWQALLLLFVGTSGSAVLGVVGNFVVSAVLILLYSFVIQFWVLKRFQHDMHQVLLIGFVLTMVLTTVAQFIQIRISPGEFSIFQGLSYTSFERAKPSTLLFAGTVLSILALFANKWVSELDVIGLGRDQAMSLGLNDAHYIPKYFSVIAILVAISTSLIGPTAFMGVFIANIAYSITGSPQYRHTLPVACTIAIVMFLTAQLMVEHFFNYKTTVSILVNVLCGGYFLIITMRARSQL | Function: Involved in the uptake of iron in complex with the siderophore anguibactin. Responsible for the translocation of ferric-anguibactin across the cytoplasmic membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34930
Sequence Length: 317
Subcellular Location: Cell inner membrane
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Q81XB1 | MISRVENISQPQFYNHNKIWTKPFIIAIIVVIILGIISLFTGVYDIRGQEDGMEMFFITRVPRTVALMLTGAAMAMAGLVMQLITQNRFVEPTTTGTIEWSSLGLLFVYLLFPAPTLVQRMTGAIIFSFIGTMIFFLFLRRVKLRSSLIVPIIGLMLGAVISAVSTFLGLLFQMTQSIETWFVGSFANIQVGRYEYLWLIVIVTLLIFMYANRLTLAGLGEDVATSLGVNYNRIVLFGTALISVAVGIVAAVIGNLPFLGLIVPNIVSMFRGDDLRSNLPWVCVIGMGTITACDIISRTIIKPFELPVSLILASVGAVVFITILLRKRKPRRLR | Function: Part of an ABC transporter complex involved in ferric-petrobactin uptake. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37020
Sequence Length: 334
Subcellular Location: Cell membrane
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P37738 | MTFRMILAFFTLCATSLFFGANQIEWSLLPTFNEKAWLPIIASRLPRLVALILTGSGLAMCGVILQHIVRNRFVEPGTTGSLDAAKLGILVSIVMLPSSDKLERMFFAVLFCFAAGLVYIAIIRKVKFSNTALVPVIGLMFGSVLSALAEFYAYQNNILQSMSGWLMGDFSKVVQEHYEIIFLILPITLLTYLYAHRFTVMGMGEDIASNLGISYAMTAALGLILVSITVAVTVVTVGAIHFVGLVIPNLVALKYGDHLKNTLPIVALGGASLLIFCDVISRVVLFPFEVPVGLTASAVGGVMFLAFLLKGAKA | Function: Involved in the uptake of iron in complex with the siderophore anguibactin. Responsible for the translocation of ferric-anguibactin across the cytoplasmic membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33923
Sequence Length: 314
Subcellular Location: Cell inner membrane
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Q5T0N5 | MSWGTELWDQFDSLDKHTQWGIDFLERYAKFVKERIEIEQNYAKQLRNLVKKYCPKRSSKDEEPRFTSCVAFFNILNELNDYAGQREVVAEEMAHRVYGELMRYAHDLKTERKMHLQEGRKAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNATKADVEKAKQQLNLRTHMADENKNEYAAQLQNFNGEQHKHFYVVIPQIYKQLQEMDERRTIKLSECYRGFADSERKVIPIISKCLEGMILAAKSVDERRDSQMVVDSFKSGFEPPGDFPFEDYSQHIYRTISDGTISASKQESGKMDAKTTVGKAKGKLWLFGKKPKPQSPPLTPTSLFTSSTPNGSQFLTFSIEPVHYCMNEIKTGKPRIPSFRSLKRGWSVKMGPALEDFSHLPPEQRRKKLQQRIDELNRELQKESDQKDALNKMKDVYEKNPQMGDPGSLQPKLAETMNNIDRLRMEIHKNEAWLSEVEGKTGGRGDRRHSSDINHLVTQGRESPEGSYTDDANQEVRGPPQQHGHHNEFDDEFEDDDPLPAIGHCKAIYPFDGHNEGTLAMKEGEVLYIIEEDKGDGWTRARRQNGEEGYVPTSYIDVTLEKNSKGS | Function: Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by activating the WASL/N-WASP-WASPIP/WIP complex, the predominant form of WASL/N-WASP in cells. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Essential for autophagy of intracellular bacterial pathogens.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 70065
Sequence Length: 605
Domain: The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation (By similarity).
Subcellular Location: Cytoplasm
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Q94BQ5 | MGRCLTKKVFLIQSPILFLHLLISLSSGAVKPDLKGVCVSKGGRFPPYELEGKPPKSVGRGSKDLTLCRVFRKKTCCSSVQTNPAFVAVRNLATYGEASQECLELFELLECSICNPNVGIQPGPPRICASFCDRVFEACKDAYFASNALKRVIGPCGVNDDIICIKASNWESNGTSFCEAAGFAVQRNDDSREKPCYGSKASLESVVESWSRDSRKETPLKTETLSCFKDLLQWVREMTTIQKISLGMSFLIAGMFLIRQSNNRNQKQRLAAIQRTARRLRGNGNGDSYSAAINRRTSSD | Function: Folic acid-binding protein involved in salicylic acid- (SA-) induced folate accumulation by triggering uptake and accumulation of folic acid in cells . May be implicated in the transport of the folates from the site of production (leaves) to the site of storage (fruits and seeds) and utilization (roots) (Probable).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 33104
Sequence Length: 300
Subcellular Location: Membrane
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Q8TCJ0 | MPFLGQDWRSPGWSWIKTEDGWKRCESCSQKLERENNRCNISHSIILNSEDGEIFNNEEHEYASKKRKKDHFRNDTNTQSFYREKWIYVHKESTKERHGYCTLGEAFNRLDFSSAIQDIRRFNYVVKLLQLIAKSQLTSLSGVAQKNYFNILDKIVQKVLDDHHNPRLIKDLLQDLSSTLCILIRGVGKSVLVGNINIWICRLETILAWQQQLQDLQMTKQVNNGLTLSDLPLHMLNNILYRFSDGWDIITLGQVTPTLYMLSEDRQLWKKLCQYHFAEKQFCRHLILSEKGHIEWKLMYFALQKHYPAKEQYGDTLHFCRHCSILFWKDYHLALLFKDSGHPCTAADPDSCFTPVSPQHFIDLFKF | Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. May play a role in accumulation of expanded polyglutamine (polyQ) protein huntingtin (HTT) (By similarity).
Sequence Mass (Da): 43313
Sequence Length: 367
Domain: The F-box is necessary for the interaction with SKP1.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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Q9D2Y6 | MPFLGQDWRSPGWSWIKTEDGWKRCDPCSHELRSEDSQYTINHSIILNSGEEEIFNNECEYAAKKRKKEHFGNDTAAHSFYREKWIYVHKESTKERHGYCTLGEAFNRLDFSSAIQDIRRFTYVVKLLQLIAKSQLTSLSGVAQKNYFNILDKIVQKVLDDHQNPRLIKGLLQDLSSTLGILVRGVGKSVLVGNINIWICRLETVLSWQQQLQNLQVTKQVNTGLTLSDLPLHMLNNILYRFSDGWDIVTLGQVTPTLYMLSEDRRLWKRLCQYHFAEQQFCRHLILSEKGHIEWKLMYFTLQKYYPTKEQYGDTLHFCRHCSILFWKDSGHPCTAADPDSCFTPVSPEHFIDLFKF | Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. May play a role in accumulation of expanded polyglutamine (polyQ) protein huntingtin (HTT).
Sequence Mass (Da): 41826
Sequence Length: 357
Domain: The F-box is necessary for the interaction with SKP1.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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Q641X7 | MPFLGQDWRSPGWSWIKTEDGWKRCDPCSHEIRSEDNQYPVNHSIILNSGEEEIFNNDCEYAAKKRKKQHFGNDTAAHSFYREKWIYVHKESTKERHGYCTLGEAFNRLDFSSAIQDIRRFTYVVKLLQLIAKSQLTSLSGVAQKNYFNILDKIVQKVLDDHQNPRLIKDLLQDLSSTLCILVRGVGKSVLVGNINIWICRLETVLNWQEKLQNLQMTKQVNTGLTLSDLPLHMLNNILYRFSDGWDIVTLGQVTPTLYMLSEDRRLWKRLCQYHFAEKQFCRHLILSEKGHIEWKLMYFTLQKYYPTKEQYGDTLHFCRHCSILFWKDSGHPCTAADPDSCFTPVSPEHFIDLFKF | Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. May play a role in accumulation of expanded polyglutamine (polyQ) protein huntingtin (HTT) (By similarity).
Sequence Mass (Da): 41984
Sequence Length: 357
Domain: The F-box is necessary for the interaction with SKP1.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
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Q969U6 | MDEGGTPLLPDSLVYQIFLSLGPADVLAAGLVCRQWQAVSRDEFLWREQFYRYYQVARDVPRHPAAMSWYEEFQRLYDTVPCVEVQTLREHTDQVLHLSFSHSGYQFASCSKDCTVKIWSNDLTISLLHSADMRPYNWSYTQFSQFNKDDSLLLASGVFLGPHNSSSGEIAVISLDSFALLSRVRNKPYDVFGCWLTETSLISGNLHRIGDITSCSVLWLNNAFQDVESENVNVVKRLFKIQNLNASTVRTVMVADCSRFDSPDLLLEAGDPATSPCRIFDLGSDNEEVVAGPAPAHAKEGLRHFLDRVLEGRAQPQLSERMLETKVAELLAQGHTKPPERSATGAKSKYLIFTTGCLTYSPHQIGIKQILPHQMTTAGPVLGEGRGSDAFFDALDHVIDIHGHIIGMGLSPDNRYLYVNSRAWPNGAVVADPMQPPPIAEEIDLLVFDLKTMREVRRALRAHRAYTPNDECFFIFLDVSRDFVASGAEDRHGYIWDRHYNICLARLRHEDVVNSVVFSPQEQELLLTASDDATIKAWRSPRTMRVLQAPRPRPRTFFSWLASQRR | Function: Substrate recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. Substrate recognition component of the SCF(FBXW5) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SASS6 during S phase, leading to prevent centriole reduplication. The SCF(FBXW5) complex also mediates ubiquitination and degradation of actin-regulator EPS8 during G2 phase, leading to the transient degradation of EPS8 and subsequent cell shape changes required to allow mitotic progression. Substrate-specific adapter of the DCX(FBXW5) E3 ubiquitin-protein ligase complex which mediates the polyubiquitination and subsequent degradation of TSC2. May also act as a negative regulator of MAP3K7/TAK1 signaling in the interleukin-1B (IL1B) signaling pathway.
PTM: Phosphorylated at Ser-151 by PLK4 during the G1/S transition, leading to inhibit its ability to ubiquitinate SASS6.
Sequence Mass (Da): 63922
Sequence Length: 566
Domain: The F-box domain mediates interaction with components of SCF (SKP1-CUL1-F-box protein) complexes, while WD repeats mediate interaction with components of DCX (DDB1-CUL4-X-box) complexes.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q969H0 | MNQELLSVGSKRRRTGGSLRGNPSSSQVDEEQMNRVVEEEQQQQLRQQEEEHTARNGEVVGVEPRPGGQNDSQQGQLEENNNRFISVDEDSSGNQEEQEEDEEHAGEQDEEDEEEEEMDQESDDFDQSDDSSREDEHTHTNSVTNSSSIVDLPVHQLSSPFYTKTTKMKRKLDHGSEVRSFSLGKKPCKVSEYTSTTGLVPCSATPTTFGDLRAANGQGQQRRRITSVQPPTGLQEWLKMFQSWSGPEKLLALDELIDSCEPTQVKHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKCKEEGIDEPLHIKRRKVIKPGFIHSPWKSAYIRQHRIDTNWRRGELKSPKVLKGHDDHVITCLQFCGNRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWSSQMRDNIIISGSTDRTLKVWNAETGECIHTLYGHTSTVRCMHLHEKRVVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQYDGRRVVSGAYDFMVKVWDPETETCLHTLQGHTNRVYSLQFDGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQSLTSGMELKDNILVSGNADSTVKIWDIKTGQCLQTLQGPNKHQSAVTCLQFNKNFVITSSDDGTVKLWDLKTGEFIRNLVTLESGGSGGVVWRIRASNTKLVCAVGSRNGTEETKLLVLDFDVDMK | Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins . Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter brings them to the SCF complex for ubiquitination . Identified substrates include cyclin-E (CCNE1 or CCNE2), DISC1, JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NFE2L1, NOTCH2, MCL1, RICTOR, and probably PSEN1 . Acts as a negative regulator of JNK signaling by binding to phosphorylated JUN and promoting its ubiquitination and subsequent degradation . Involved in bone homeostasis and negative regulation of osteoclast differentiation . Regulates the amplitude of the cyclic expression of hepatic core clock genes and genes involved in lipid and glucose metabolism via ubiquitination and proteasomal degradation of their transcriptional repressor NR1D1; CDK1-dependent phosphorylation of NR1D1 is necessary for SCF(FBXW7)-mediated ubiquitination . Also able to promote 'Lys-63'-linked ubiquitination in response to DNA damage . The SCF(FBXW7) complex facilitates double-strand break repair following phosphorylation by ATM: phosphorylation promotes localization to sites of double-strand breaks and 'Lys-63'-linked ubiquitination of phosphorylated XRCC4, enhancing DNA non-homologous end joining .
PTM: Phosphorylation at Thr-205 promotes interaction with PIN1, leading to disrupt FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation . Phosphorylated by ATM at Ser-26 in response to DNA damage, promoting recruitment to DNA damage sites and 'Lys-63'-linked ubiquitination of phosphorylated XRCC4 .
Sequence Mass (Da): 79663
Sequence Length: 707
Domain: The WD repeats mediate interaction with substrates of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex.
Subcellular Location: Nucleus
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Q8VBV4 | MNQELLSVGSKRRRTGGSLRGNASSSQVDEGQMNRVVEEDPQQQARHQEEEHTARNGELVGANPRPGDQNDTQQGQVEENNNRFISVDEDSSGNQEEQEEDEEHAGEQEEEEEEEEEEEEMDQESDDFDPSDDSSREDEHTHNSNVTNCSSVSDLPAHQLSSPFYTKTTKMKRKLDHGSEVRSFSLGKKPCKVSDYTSTTGLVPCSATPTTFGDLRAANGQGQQRRRITSVQPPTGLQEWLKMFQSWSGPEKLLALDELIDSCEPTQVKHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKCKEEGIDEPLHIKRRKIIKPGFIHSPWKSAYIRQHRIDTNWRRGELKSPKVLKGHDDHVITCLQFCGNRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWSSQMRDNIIISGSTDRTLKVWNAETGECIHTLYGHTSTVRCMHLHEKRVVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQYDGRRVVSGAYDFMVKVWDPETETCLHTLQGHTNRVYSLQFDGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQSLTSGMELKDNILVSGNADSTVKIWDIKTGQCLQTLQGPSKHQSAVTCLQFNKNFVITSSDDGTVKLWDLKTGEFIRNLVTLESGGSGGVVWRIRASNTKLVCAVGSRNGTEETKLLVLDFDVDMK | Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins . Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter brings them to the SCF complex for ubiquitination . Mediates ubiquitination and subsequent degradation of CCNE1 and MYC . Identified substrates include cyclin-E (CCNE1 or CCNE2), DISC1, JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NOTCH2, MCL1, RICTOR and probably PSEN1 (By similarity). Acts as a negative regulator of JNK signaling by binding to phosphorylated JUN and promoting its ubiquitination and subsequent degradation (By similarity). SCF(FBXW7) complex mediates the ubiquitination and subsequent degradation of NFE2L1 . Involved in bone homeostasis and negative regulation of osteoclast differentiation . Regulates the amplitude of the cyclic expression of hepatic core clock genes and genes involved in lipid and glucose metabolism via ubiquitination and proteasomal degradation of their transcriptional repressor NR1D1; CDK1-dependent phosphorylation of NR1D1 is necessary for SCF(FBXW7)-mediated ubiquitination . Also able to promote 'Lys-63'-linked ubiquitination in response to DNA damage (By similarity). The SCF(FBXW7) complex facilitates double-strand break repair following phosphorylation by ATM: phosphorylation promotes localization to sites of double-strand breaks and 'Lys-63'-linked ubiquitination of phosphorylated XRCC4, enhancing DNA non-homologous end joining (By similarity).
PTM: Phosphorylation at Thr-208 promotes interaction with PIN1, leading to disrupt FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation. Phosphorylated by ATM at Ser-26 in response to DNA damage, promoting recruitment to DNA damage sites and 'Lys-63'-linked ubiquitination of phosphorylated XRCC4.
Sequence Mass (Da): 79848
Sequence Length: 710
Domain: The WD repeats mediate interaction with substrates of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex.
Subcellular Location: Nucleus
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Q8N3Y1 | MDDYSLDEFRRRWQEELAQAQAPKKRRRPEAAERRARRPEVGSGRGEQASGDPALAQRLLEGAGRPPAARATRAEGQDVASRSRSPLAREGAGGGEQLVDQLIRDLNEMNDVPFFDIQLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLWYRLCQQEGHLPDSSISDYSCWKLIFQECRAKEHMLRTNWKNRKGAVSELEHVPDTVLCDVHSHDGVVIAGYTSGDVRVWDTRTWDYVAPFLESEDEEDEPGMQPNVSFVRINSSLAVAAYEDGFLNIWDLRTGKYPVHRFEHDARIQALALSQDDATVATASAFDVVMLSPNEEGYWQIAAEFEVPKLVQYLEIVPETRRYPVAVAAAGDLMYLLKAEDSARTLLYAHGPPVTCLDVSANQVAFGVQGLGWVYEGSKILVYSLEAGRRLLKLGNVLRDFTCVNLSDSPPNLMVSGNMDGRVRIHDLRSGNIALSLSAHQLRVSAVQMDDWKIVSGGEEGLVSVWDYRMNQKLWEVYSGHPVQHISFSSHSLITANVPYQTVMRNADLDSFTTHRRHRGLIRAYEFAVDQLAFQSPLPVCRSSCDAMATHYYDLALAFPYNHV | Function: Substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The Cul7-RING(FBXW8) complex mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain . Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2) . The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation . Associated component of the 3M complex, suggesting that it mediates some of 3M complex functions .
Sequence Mass (Da): 67394
Sequence Length: 598
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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L0N065 | MAKFTVTSLERHLLLISTVIAVLAALIVSRGCNYLLKRWKLSAYPLYEDKKVTPIEELHSSRDLIAKGFAKSQGKEIWRINTTIGEVLVVSPKYIEKFRYGHGCSAAAYTERELPISAPGYEPFTFASNEWRQRNADIILHRLTGLVSNRKIELSEELSNALESRWTNSTDWHAVSLFQTMTAIVAQTTQYFFTNRELCRNDAYIQSLFAYSSLAFTEGRSLMKWPRVLHPLVARFHPASQNLQSALENVNKHIFPFVRERRAEISRRRFEAAQSGKETPLADEWVAWLDEKAGNEDYNPGVAMVSFSVASFHTTTDFMCQLLCDLARNPAIIEQLKEEASDVLRDHTWTKSSFARLDLMDRCMKESQRLKPIGAVFLKSRAQKDISVENGNIIPAGSLFVVSGHWMHDPAIYPEPEKFDPGRHLRHAEESKPNKPKQFTAVSPEHMGWGYGKHSCPGRFFAATVAKMLLTHILFKYEFKLPDGKLNQHAYEFTTEILVRRRIEEGALNLDSFDSIDR | Function: Cytochrome P450 monooxygenase; part of the 2 gene clusters that mediate the biosynthesis of fusicoccins, diterpene glucosides that display phytohormone-like activity and function as potent activators of plasma membrane H(+)-ATPases in plants by modifying 14-3-3 proteins and cause the plant disease constriction canker . The first step in the pathway is performed by the fusicoccadiene synthase PaFS that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and successively converting GGDP into fusicocca-2,10(14)-diene, a precursor for fusicoccin H . The second step is the oxidation at the C-8 position by the cytochrome P450 monooxygenase PaP450-2 to yield fusicocca-2,10(14)-diene-8-beta-ol . The cytochrome P450 monooxygenase PaP450-1 then catalyzes the hydroxylation at the C-16 position to produce fusicocca-2,10(14)-diene-8-beta,16-diol . The dioxygenase fc-dox then catalyzes the 16-oxydation of fusicocca-2,10(14)-diene-8-beta,16-diol to yield an aldehyde (8-beta-hydroxyfusicocca-1,10(14)-dien-16-al) . The short-chain dehydrogenase/reductase fc-sdr catalyzes the reduction of the aldehyde to yield fusicocca-1,10(14)-diene-8-beta,16-diol . The next step is the hydroxylation at C-9 performed by the cytochrome P450 monooxygenase PaP450-3 that leads to fusicoccin H aglycon which is glycosylated to fusicoccin H by the O-glycosyltransferase PaGT . Hydroxylation at C-12 by the cytochrome P450 monooxygenase PaP450-4 leads then to the production of fusicoccin Q and is followed by methylation by the O-methyltransferase PaMT to yield fusicoccin P . Fusicoccin P is further converted to fusicoccin J via prenylation by the O-glucose prenyltransferase PaPT . Cytochrome P450 monooxygenase PaP450-5 then performs hydroxylation at C-19 to yield dideacetyl-fusicoccin A which is acetylated to 3'-O-deacetyl-fusicoccin A by the O-acetyltransferase PaAT-2 . Finally, a another acetylation by the O-acetyltransferase PaAT-1 yields fusicoccin A .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59208
Sequence Length: 518
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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H7CE84 | MANVVLDGSAAPAKAGLPLDLSSPSKQTNFPTELESNSNADFWWRLCRPEMAGLFKQAGGYTELQQESHLRFVREHCAPWMGTVPTGHMANEAVAPVEMSVNYISSRDEGVLRFQMEPFTAVSGPHTQADDPSGKKAVCSMLRSFQHALGDVDLTWTWQLVDKFMVTAPDEVARLREAERTSLPPPLDLYQRTPQFNFAFDLSPDKKSMKTYFLPLAKSLVTGSSALDYCLDAVRSLEPHGEGLSPVADLLHQFFNTSCPGHMSCDYLGIDSTNPKRSRVKLYVSSQQHNSFNFIRAVFTLGGIAKDEATLRGLEFLRSIWHLLVNVDEGELPDSSDRPAKQLPFFLGCLYFSFEWRAGDRLPLVKLYVPQWQYAQSDRKIAKNISASLRKLGRDEAADEYLTHIKQTFPRADLDGNVSIHNQVSYAYSAETGAYLTIYYSVNSKAVARDQIY | Function: O-glucose prenyltransferase; part of the 2 gene clusters that mediate the biosynthesis of fusicoccins, diterpene glucosides that display phytohormone-like activity and function as potent activators of plasma membrane H(+)-ATPases in plants by modifying 14-3-3 proteins and cause the plant disease constriction canker . The first step in the pathway is performed by the fusicoccadiene synthase PaFS that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and successively converting GGDP into fusicocca-2,10(14)-diene, a precursor for fusicoccin H . The second step is the oxidation at the C-8 position by the cytochrome P450 monooxygenase PaP450-2 to yield fusicocca-2,10(14)-diene-8-beta-ol . The cytochrome P450 monooxygenase PaP450-1 then catalyzes the hydroxylation at the C-16 position to produce fusicocca-2,10(14)-diene-8-beta,16-diol . The dioxygenase fc-dox then catalyzes the 16-oxydation of fusicocca-2,10(14)-diene-8-beta,16-diol to yield an aldehyde (8-beta-hydroxyfusicocca-1,10(14)-dien-16-al) . The short-chain dehydrogenase/reductase fc-sdr catalyzes the reduction of the aldehyde to yield fusicocca-1,10(14)-diene-8-beta,16-diol . The next step is the hydroxylation at C-9 performed by the cytochrome P450 monooxygenase PaP450-3 that leads to fusicoccin H aglycon which is glycosylated to fusicoccin H by the O-glycosyltransferase PaGT . Hydroxylation at C-12 by the cytochrome P450 monooxygenase PaP450-4 leads then to the production of fusicoccin Q and is followed by methylation by the O-methyltransferase PaMT to yield fusicoccin P . Fusicoccin P is further converted to fusicoccin J via prenylation by the O-glucose prenyltransferase PaPT . Cytochrome P450 monooxygenase PaP450-5 then performs hydroxylation at C-19 to yield dideacetyl-fusicoccin A which is acetylated to 3'-O-deacetyl-fusicoccin A by the O-acetyltransferase PaAT-2 . Finally, a another acetylation by the O-acetyltransferase PaAT-1 yields fusicoccin A .
Sequence Mass (Da): 50745
Sequence Length: 453
Pathway: Mycotoxin biosynthesis.
EC: 2.5.1.-
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O87838 | MTAKALEGIRVLDMTHVQSGPSATQLLAWLGADVVKLEAPHGDITRGQLRDLPDVDSLYFTMLNCNKRSITLNTKSERGKEILTELIRRSDVMVENFGPGAVDRMGFTWDRVKEINPRIVYASIKGFGEGPYTAFKAYEVVAQAMGGSMSTTGFEDGPPLATGAQIGDSGTGVHVVAGILAALYQREHTGRGQRVNVAMQHAVLNLCRVKLRDQQRLSHGPLAEYPNEDFGDEVPRSGNASGGGQPGWAVKCAPGGPNDYVYVIVQPVGWQPLSELIGRPELAEDPEWATPRARLPKLNKMFQLIEEWSSTLPKWEVLERLNAHNIPCGPILSTKEIIEDDSLVANEMVVTVPHPERGEFVTVGSPLKLSDSPVEVTSSPLLGEHNEEVYVGELGLGDEELRLLKSSGVI | Function: Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate (By similarity).
Catalytic Activity: formyl-CoA + oxalate = formate + oxalyl-CoA
Sequence Mass (Da): 44664
Sequence Length: 410
Pathway: Metabolic intermediate degradation; oxalate degradation; CO(2) and formate from oxalate: step 1/2.
EC: 2.8.3.16
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Q47162 | MHSTRNKQLKKLKSWHKNKKAMPAVLASTLLMAAHAQAAETTGADTMIVSANAGESVTAPLKGIVAKESASGTKTSTPLIKTPQSVTVVTRDQMDAQAVSSVSDALNYSSGVVTNYRGSSNRNDEVIARGFRYAPKFLDGLSYGLSGQGSTIGKMNPWLLERVEMVHGPASVLYGQVNPGGLISMTSKRPTAETIRKVQFSAGNQHLGEAAFDFGGALNDDKTLLYRLDGIASTKHEFVKDSKQERIAVAPSLTWLPNPDTSFTLLTSYQNDPKAGYRNFLPKIGTVVEASAGYIPYDLNVSDPNYNQSKREQGSIGYNLDHSFNDVFSFQQNVRYTQLREKYKYLVYTKNADAPATDTTILRRPQKEENEISEFAIDNQLKATFATGSVNHTVLSGLDYKWLTLEKKMWLDRNNDYSFNWANPTYNVSVNDSMLTELSTNERNKLNQVGVYLQDQLEWNQWNLLLSGRHDWSRVDKQDYAADTTTERNDGKFTGRAGLLYAFDNGISPYVSYSTSFEPNLDSGAPGTPAFKPTTGEQKEVGVKFQPKGSNTLLTVSLFDITQKNITSYNSVTRYNEQIGKVKSKGVETEAHTQLTPEISLMAAYSYTDAVTKESYTASQVNKAPSSIPRHAASAWGSYSFHNGPLKGVTLGTGVRYIGSTYGDNAESFKVPAYTLFDAMARYELGSLASQLKGAAVQLNVNNLTDKHYVASCGGDTACFYGSGRTVVATVSYSW | Function: Involved in the initial step of iron uptake by binding chrysobactin, an iron chelatin siderophore that allows the bacteria to extract iron from the environment.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80724
Sequence Length: 735
Subcellular Location: Cell outer membrane
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Q05202 | MNQTISSRAPQKRLAPRLLCVMIGAALGTLSASSWAAAATDSTAENAKKTSATAATAKAEDSKTNDTITVVGAQETFRAGGNDLIPTYLDGQVANGGRIGFLGQQDARNVPFNVIGYTSKMIEDQQANSIADVVKNDASVQNVRGYGNPSQNYRIRGYNLDGDDISFGGLFGVLPRQIVSTSMVERVEVFKGANAFINGISPSGSGVGGMINLEPKRAGDTPLTRVTVDYGSASQVGGALDVGRRYGDDDQFGVRVNVLHREGESAIHDQKERTTAVSTGLDYRGDRARTSLDVGYQKQTIHHMRTDVAIGGATVIPEPPSSTLNYGQSWVYTDMETTFGMLRSEYDVSQNWTVYGSVGASRNEETGQYGAPMLTNNNGDATISRLYVPYVADSVAGLGGIRGHFDTGPITHKVNLGYAANYRTTKSAWNMSGQEDTNIYNPGVIGFPQTVMGSDSQDPQLTSQVRASGLSLSDTLSMMDDKVSLMLGVRRQEVTIRNFDSGVPNSAGSLDAMKVTPIYGIMVKPWEKVSLYANHIEALGPGKSAPYQYNGKPVVNAGQIPGIIHSKQNEIGVKFDNQRYGGTLALFEITRPTGMVDPATNVYGFYGEQRNRGIELNVFGEPVFGTRLLASATWLDPKLTKAADSANNGNDAVGVANYQLVFGGEYDIPVVEGLTATGTVVRSGSQYANEANTLKLKPWTRLDLGVRYTMPMKDTSLTWRANIENVTNERYWESVEDSGTYIYQGDPRALKLSVSMDF | Function: Receptor for the hydroxamate siderophore, ferrichrome. Binds also to most other ferrichrome derivatives except enantio ferrichrome and ferric rhodotorulate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81749
Sequence Length: 758
Subcellular Location: Cell outer membrane
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Q12178 | MVTGGMASKWDQKGMDIAYEEAALGYKEGGVPIGGCLINNKDGSVLGRGHNMRFQKGSATLHGEISTLENCGRLEGKVYKDTTLYTTLSPCDMCTGAIIMYGIPRCVVGENVNFKSKGEKYLQTRGHEVVVVDDERCKKIMKQFIDERPQDWFEDIGE | Function: Catalyzes the hydrolytic deamination of cytosine to uracil or 5-methylcytosine to thymine. Is involved in the pyrimidine salvage pathway, which allows the cell to utilize cytosine for pyrimidine nucleotide synthesis.
Catalytic Activity: cytosine + H(+) + H2O = NH4(+) + uracil
Sequence Mass (Da): 17507
Sequence Length: 158
Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; uracil from cytosine: step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.4.1
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