ids
stringlengths 6
10
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stringlengths 11
1.02k
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stringlengths 108
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Q7U8A1 | MIEPLLCGIVLGLIPVTLLGLFVAAWNQYRRGGSALGG | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3970
Sequence Length: 38
Subcellular Location: Cellular thylakoid membrane
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Q9TLR5 | MSQEIVTVSLIISILVLSGLTMGFILLKIQK | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3389
Sequence Length: 31
Subcellular Location: Plastid
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Q85FX8 | MNEIVALMIICPLMVMVGLGMGFALLWLQQQA | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3535
Sequence Length: 32
Subcellular Location: Plastid
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P48366 | MGKQIFNTAVICFTLTLIGLSLGFVLLKIQGDE | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3584
Sequence Length: 33
Subcellular Location: Plastid
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Q4G3B3 | MAKEIFTVAGVMWALVLTGLSVGFGLLKIQGE | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3380
Sequence Length: 32
Subcellular Location: Plastid
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Q7NLN8 | MTGEIFFVAGLVFVLTLVGMAIGFGVLKLRGEGKEA | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3772
Sequence Length: 36
Subcellular Location: Cell inner membrane
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O78499 | MGNEFIASASISFIITLIGLTLGFALLKLQGE | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3369
Sequence Length: 32
Subcellular Location: Plastid
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P83796 | MTEEMLYAALLSFGLIFVGWGLGVLLLKIQGAEKE | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3842
Sequence Length: 35
Subcellular Location: Cellular thylakoid membrane
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B0JI68 | MTAESMLFNGAIVAIVLVLVGLAWGFLLLKIQGGEAE | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3876
Sequence Length: 37
Subcellular Location: Cellular thylakoid membrane
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B2J8Q3 | MGGEILNAAILSFGLIFVGWGLGALLLKIQGGEE | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3488
Sequence Length: 34
Subcellular Location: Cellular thylakoid membrane
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P0A3Y1 | MSGELLNAALLSFGLIFVGWALGALLLKIQGAEE | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3546
Sequence Length: 34
Subcellular Location: Cellular thylakoid membrane
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P51275 | MGKEIVESAILSSVLVLVGLAVGFLLLKVQGE | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3313
Sequence Length: 32
Subcellular Location: Plastid
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A2BXL5 | MAKEIFSIAAVFWILIPIGLVGGALLLKFQGD | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3432
Sequence Length: 32
Subcellular Location: Cellular thylakoid membrane
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Q3AY07 | MLFTVAWASLAAMFSFSIAMVVWGRNGDGTLKF | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3626
Sequence Length: 33
Subcellular Location: Cellular thylakoid membrane
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Q3AJN5 | MLFTLGWASLAAMFSFSIAMVVWGRNGDGTLNF | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3612
Sequence Length: 33
Subcellular Location: Cellular thylakoid membrane
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Q8DKN2 | MDIITLGWVGVLSVFTLSIAFVVWGRHGM | Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3206
Sequence Length: 29
Subcellular Location: Cellular thylakoid membrane
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Q9LLC6 | MALRCKTPAATCAARSRRSVRVSAHKGAFEQAQVAAAAFVAAAVIAAPANAGVVLQQPVLKKAFQDDTPAAPPPKREFRGLAPPALPQSDAPNVAAEKPKKAEVVESTSGGLDPRSVALPGALALTIGGFVAASKIDGSFNDWFMEAVVRDSNNYAGYEATLKSENGVTFPKVAAGGTKKVKAATGSKKGGFPFGGKK | Function: The cytochrome b6-f complex functions in the linear cross-membrane transport of electrons between photosystem II and I, as well as in cyclic electron flow around photosystem I.
PTM: Phosphorylated.
Sequence Mass (Da): 20247
Sequence Length: 198
Subcellular Location: Plastid
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Q9SZD6 | MATITPSSISNAWLIPGASFTVKKSDCSIKCSFSRKAGKQILSSTQRLVLPLSTSLRLFPTHGRQFVLHPHRRATGTDVVAAVEEQDSTPVVAEDKETVASEKSDAPAPTSQSRGTARPGRKSEMPAVKNEELVPGATFTGKVRAIQPFGAFVDFGAFTDGLVHVSQLSDNFVKDVSSVVTIGQEVKVRLVEADIESKRISLTMRENDDPPKRQSGGSDKPRSGGKRDGSKGGGQRKGEGFNSKFAKGQMLDGVVKNLTRSGAFITIGEGEEGFLPTAEEADDGIGSMMMGGSSLQAGQEVKVRVLRIARGRVTLTMKEEDDGKFDETTTQGVVHTATNPFMLAFRKNEEIAAFLDKREEEAEKPPVETPVEPEAEASVTSAEVEESVCVPAEVTSEEVPSSETPKVVEEEVIATKAEDDSPEKEEQTETLAAAAEAEEVVPPIPETKSEEEIVENSIPPNSATDEVSSPEALASEEVEKEQVVAETPVDEVKTPAPVVTEASSEESGNTATAESIKGISPALVKQLREETGAGMMDCKNALSESEGDMVKAQEYLRKKGLASADKKASRATSEGRIGAYIHDSRIGVLLEVNCETDFVSRGDIFKELVDDLAMQVAACPQVEYLVTEDVSEEIVKKEKEIEMQKEDLLSKPEQIREKIVDGRIKKRLDSLALLEQPYIKDDKVIVKDLVKQRIATIGENIKVKRFVRYTLGEGLEKKSQDFAAEVAAQTAAKPKAKEEPKAEEAKEAVASPPTTVVSAALVKQLREETGAGMMDCKKALAATGGDLEKAQEFLRKKGLSSADKKSSRLASEGRIGSYIHDSRIGVLIEVNCETDFVGRSEKFKELVDDLAMQAVANPQVQYVSIEDIPEEIKQKEKEIEMQREDLLSKPENIREKIVEGRISKRLGEWALLEQPYIKDDSVLVKDLVKQTVATLGENIKVRRFVKFTLGEDN | Function: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP (By similarity). It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity).
PTM: Probable substrate for the chloroplast protease ClpP6.
Sequence Mass (Da): 103782
Sequence Length: 953
Subcellular Location: Plastid
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O13764 | MENRICTLAKPLPKLDESKQAWVSYLWLKKALPGFEEHSAYVYMTTNPTIAGRIFLPINNEDLEDGTVEISGYDNLLADALYISTIAPVKLDFVQLIVIDDNSQDQDAIIERIKGRNAILMESDFINQNILVQVCQPVRHGVVDSETKFVIERKDSFTFLASNEKNISSFKRGKTETDAELVIRPSKVHTEIQWCLQNCSLIHVPFELLFNVGKKNGCPISLRLSDGKNVYGIASIKSDTEHDSVQLSPSLHYFDEFNESVISEEGTEAFLVARGPSVGIASRISLRTIPTQSCFSEKLLKAANLCVVQQVKQKVFLQSKQIFCVPINSLMANSDSVDILELTRNTDAYIWYSVEEIDPLNTYNIYYTNEDTSIVLDTQLSHRLLPSLRKPLLNFVKVHPPSQKLLRFCRAFFDPQQVPGFNPFFLLHGNPFTGKTKAVEEVASLFSAPVFTISSYEFADATADHLEAKLDMFVQNVVKSPCAIIFVKDLDVLSISSDEGNIVPGSKSIQILLSKIDLVKSPQGRYIVIGTCHSIEKIPYEILSESFFELKFSELEMDERLELLKIYANNVIIDKRISLKDVALKTNSMSFGELECLPDHMTKAAVDRIKRTGYDNDSIILSGPIITEQDVDVSINRIRKEKSNTIFTVPKVNWDDIGGLEEAKTVLRDTLQLPLQFPELFSQGLKPRSGVLLYGPPGTGKTLLAKAVATELSLEFVSIKGPELLNMYVGESEANVRNVFEKARNSSPCVIFFDELDSIAPHRGNSSDSGNVMDRVVSQLLAELDSISKDNNKYVFVIGATNRPDLLDPSLLRPGRFDKLVYLGINKSEESKASMLRALTKTFKLDETIDLNEIAKNCHPNFTGADMYALCSDAVLSAIKRKTNEIDLLIQASGTDLSTEEFFKRNENQDSLELRITKEDFLTSLKKLRPSISEQELHRYEMVRHQFS | Function: Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 106506
Sequence Length: 948
Subcellular Location: Cytoplasm
EC: 3.6.4.-
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Q9XF57 | MPVFKAPFNGYSVKFSPFYESRLAVATAQNFGILGNGRIHVLELAPGAPGVTESVSYDTADAVYDVCWSESHDSVLIAAIGDGSVKIYDTALPPPSNPIRSFQEHAREVQSVDYNPTRRDSFLTSSWDDTVKLWAMDRPASVRTFKEHAYCVYQAVWNPKHGDVFASASGDCTLRIWDVREPGSTMIIPAHDFEILSCDWNKYDDCILATSSVDKTVKVWDVRSYRVPLAVLNGHGYAVRKVKFSPHRRSLIASCSYDMSVCLWDYMVEDALVGRYDHHTEFAVGIDMSVLVEGLMASTGWDELVYVWQQGMDPRAS | Function: Receptor required for the peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal . Specifically binds to cargo proteins containing a PTS2 peroxisomal targeting signal in the cytosol . Cargo protein-binding triggers interaction with PEX5 and formation of a ternary complex composed of PEX5 and PEX7 along with PTS2-containing cargo proteins, which is tranlocated into peroxisomes by passing through the PEX13-PEX14 docking complex .
Sequence Mass (Da): 35473
Sequence Length: 317
Domain: The WD40 repeats are involved in the binding of PTS2-containing proteins.
Subcellular Location: Cytoplasm
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O59894 | MFKFQTNGFSGYAVRYSPFYDNKIAVATSANYGLVGNGRLYVLSIMDDGNIITDISYDTQDGLFGVAWSETNENHVLTSSGDGCVSLFDTTLKDYPVMKFTEHQREVFSVDWSNIDKNLFCSASWDGSVKVWSPGSNRNTSLLTLRSLASREEKTGRIEKPIPVVQPSQVPMSKTRPNIRNDNNDCVYDAKFSFHDPNIIMSCNSDSHLQLWDTRLPNPLFMDFVAHNGLEALSCDFNRYRPFVVASAGVDKLAKVWDTRMIQPNVHSRPPRALNKFMGHEFAIRKLAWSPHGPTQLLTCSYDMTVRVWNDSPSPTSRVGLLDGASQPHAPPCSKIFSAHTEFVMGCDWSLWGEPGWVVTTGWDEMVYVWNTQRLQ | Function: Receptor required for the peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal, such as 3-oxoacyl-CoA thiolase (By similarity). Specifically binds to cargo proteins containing a PTS2 peroxisomal targeting signal in the cytosol (By similarity). Cargo protein-binding triggers interaction with PEX20 and formation of a ternary complex composed of PEX20 and PEX7 along with PTS2-containing cargo proteins, which is tranlocated into peroxisomes by passing through the PEX13-PEX14 docking complex (By similarity). PEX7 receptor is then retrotranslocated into the cytosol, where it is ubiquitinated and degraded .
PTM: Polyubiquitinated, leading to its degradation by the proteasome . Ubiquitination is dependent of PEX5 and PEX20 and takes place following recycling into the cytosol .
Sequence Mass (Da): 42422
Sequence Length: 376
Subcellular Location: Cytoplasm
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P45817 | MTMSARVRKMALPSNCDLSDVEMICDNVLGCLEDLDSSRVVSRVTSREDVDESTIGDLISLDCVSLETPLFSFLFLGVTLFLFLSLLQQSLVFLLGVFLRLVQLVGHFLLLLMGEQIGVIDKAMSHIPLPEVGQHSQQVQIQHLVERRFGLDVVTAIVVIGDNELFQVVGHQFRVGIMSDGQRSQQSQNSGMNVASSSRGRHQLVPDRPGSQLSSQKLSSLVPLARIAAAEIPCAVQQSLSRLFARSVQNRQVQRPHLDPQRQRNIVGVFGVQHGRAVLLCALGGDLIEKRPNQLVRVVKVLVDKFPRRLPKRLVHLVHLGRGSLVHCRCDRVCQQRGCCHLWHCGGHFFVGLVSWIVDETAACVVFCLFKVVSETQRISSLPRYMHRELNTAGVVWGCGGKHM | Function: Essential for the import of peroxisomal matrix proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44914
Sequence Length: 404
Subcellular Location: Peroxisome membrane
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Q04364 | MNEVTCSITGDNPIHKINNGLGLKWNNLGKFSDFQTNDSAARDARTIDYIFTNCQTGSSIGKIDFRAALPADKSQHSGVSEKEFSRLENQWSKEFSCFPKNKNADVTKPSRNKHEKRSANLHNRYFAQYYSTAYQQNRIYPCRISYNEHSSVSNGWEFQFKSIENQLLNELKIENNVEEKTVGYEYVAEYEETIDFMHMLSSVPQTYQFLKSNIYITERDPYKIGCVLMDNGSNLNEVVMAFEAAISQDPSHINAWLKLGIVNFENESESNGELALRNCLNLDPNNTIALENLAIHHINQQNESESLKLFHKWILSKFSKVFQPSAGENKDSINKIPKKAHLAHILESLLNMGIEKKDQYDIYSVLSILYYSDQKIKQSQKCLEFLLLEKPNNGTIWNRYGAILANTKSYHSAINAYNKCKQLRPNFTRVRYNLAIAYMNKGDYVKASKMLIEVILLRSKGYEHNKAKMQNKFMQNLKNALIASKNFDSLDLINGSHNTESLISTLKAIYNKMD | Function: Peroxisomal import receptor that mediates the peroxisomal import of both malate synthases MLS1 and MLS2 in oleate-grown cells . Recognizes the C-terminal peroxisomal targeting signal PTS1 sequence SKL of MLS1 and MLS2, probably via its TPR domains . Interacts with the PTS1-receptor docking protein PEX14 but not with peroxins PEX1, PEX3 through to PEX8, PEX10, PEX11, PEX12, PEX13, PEX15, PEX17, PEX18, PEX19 and PEX21 .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59065
Sequence Length: 514
Domain: The WxxxF motif is involved in the interaction with the PTS1-receptor docking protein PEX14.
Subcellular Location: Cytoplasm
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P21777 | MKRIGVFTSGGDAPGMNAAIRAVVRQAHALGVEVIGIRRGYAGMIQGEMVPLGVRDVANIIQRGGTILLTARSQEFLTEEGRAKAYAKLQAAGIEGLVAIGGDGTFRGALCLVEEHGMPVVGVPGTIDNDLYGTDYTIGFDTAVNTALEAIDRIRDTAASHERVFFIEVMGRHAGFIALDVGLAGGAEVIAVPEEPVDPKAVAEVLEASQRRGKKSSIVVVAEGAYPGGAAGLLAAIREHLQVEARVTVLGHIQRGGSPTAKDRILASRLGAAAVEALVGGASGVMVGEVEGEVDLTPLKEAVERRKDINRALLRLSQVLAL | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 33537
Sequence Length: 322
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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P16861 | MQSQDSCYGVAFRSIITNDEALFKKTIHFYHTLGFATVKDFNKFKHGENSLLSSGTSQDSLREVWLESFKLSEVDASGFRIPQQEATNKAQSQGALLKIRLVMSAPIDETFDTNETATITYFSTDLNKIVEKFPKQAEKLSDTLVFLKDPMGNNITFSGLANATDSAPTSKDAFLEATSEDEIISRASSDASDLLRQTLGSSQKKKKIAVMTSGGDSPGMNAAVRAVVRTGIHFGCDVFAVYEGYEGLLRGGKYLKKMAWEDVRGWLSEGGTLIGTARSMEFRKREGRRQAAGNLISQGIDALVVCGGDGSLTGADLFRHEWPSLVDELVAEGRFTKEEVAPYKNLSIVGLVGSIDNDMSGTDSTIGAYSALERICEMVDYIDATAKSHSRAFVVEVMGRHCGWLALMAGIATGADYIFIPERAVPHGKWQDELKEVCQRHRSKGRRNNTIIVAEGALDDQLNPVTANDVKDALIELGLDTKVTILGHVQRGGTAVAHDRWLATLQGVDAVKAVLEFTPETPSPLIGILENKIIRMPLVESVKLTKSVATAIENKDFDKAISLRDTEFIELYENFLSTTVKDDGSELLPVSDRLNIGIVHVGAPSAALNAATRAATLYCLSHGHKPYAIMNGFSGLIQTGEVKELSWIDVENWHNLGGSEIGTNRSVASEDLGTIAYYFQKNKLDGLIILGGFEGFRSLKQLRDGRTQHPIFNIPMCLIPATVSNNVPGTEYSLGVDTCLNALVNYTDDIKQSASATRRRVFVCEVQGGHSGYIASFTGLITGAVSVYTPEKKIDLASIREDITLLKENFRHDKGENRNGKLLVRNEQASSVYSTQLLADIISEASKGKFGVRTAIPGHVQQGGVPSSKDRVTASRFAVKCIKFIEQWNKKNEASPNTDAKVLRFKFDTHGEKVPTVEHEDDSAAVICVNGSHVSFKPIANLWENETNVELRKGFEVHWAEYNKIGDILSGRLKLRAEVAALAAENK | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 107970
Sequence Length: 987
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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Q9FIK0 | MAAETSIRKLPSLSGLRHRRNPLEDNPYFHPSNGFYITPSDVILAQVAYDHSAHSQSRVAYHRAGPRREIMYEPSAVKAAIVTCGGLCPGMNTVIRELVVGLWELYGVREIYGIPAGYRGFYSMKAVKLDPKAVHDWHKKGGTVLATSRGGFHLQKIVDAIHLNGYNQVYIIGGDGTMRGAVEIFKEISLRKLEVGITVIPKTVDNDVGIIDRSFGFQTAVEMAQEAISAAHVEAESAVNGIGLVKLMGRSTGHIALHATLSSRDVDCCLIPEMDFYLEGKGGLFEFLEKRLKERGHAVLVVAEGAGQEMIPRNESQKQERDESGNAVFLDVGVWFKSVLKAWWEREHPDELFTVKYIDPTYMIRAVPANATDNLYCTLLAHSAIHGVMAGYTGFVPGPINGNYAYIPLEEVAQTKNQVNTRDHKWAWVRSVTNQPDFETNVKG | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 49182
Sequence Length: 444
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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Q9HGZ0 | MTNTILDTYSSRRKPRRIGILTSGGDAPGMNGAIRAVVRTAIQNGCEAWAIHEGYEGLIQGGAMMHPLYWEDVRGFLSRGGTLIGSVRCDRFREREGRLQAARNMVLFGIDALVVCGGDGSLTGADLFRSEWPELLNELVSTGVLTVAQVAPHQNLNIVGLLGSIDNDFSGTDATIGCYSALTRICEAVDAVFDTASSHRRGFVVEVMGRHCGWLALMAAIATGADWLFIPERPPRDGWEDDMCSIITKNRNRGKRRTIVILAEGAQDSNLDRISSSAVKDVLSKRLGLDTRVTVLGHIQRGGSPCAYDRWLSTLQGIHAVKAVLSMTPESPSPVVIIQENRIRTSSLAETVALTKEANASMHAKEFEKAATLRDPEFMEYHSAYRHLNTSDHPKMVLPEDKRMRVAIIHVGAPAAGMNPATRAVVAYCLTRGHTPIAIHNGFPGLCRHHDDTPGSVREMHWLESGDWINDGGSDIGTNAGLPLDDIETTAQCFERYKFDALFVIGGFEAFTAVSQLRKARKQYLAFRIPLVLLPASMSNNVPGTEYSLGSDTSLNTLVYFCDVVRQSASSSGHSVFVVEAQGAEYQATAAALAAGAMTVYTPERGITLQSLSNDIEYLRQQFSKDHGANRSGKLIIRNDQTSTIYSTTEIANIIKHEAKNRFDAQGVVPGHFQQGGKVSPIDRIRAFRLAVKCMEHLETFAGQSPEEIMNDENSATVISIKQSRILLLPMGGPTGVEATDTDWKRQRPKTQNWLEIQEAVDSLSGRSSLYAIPN | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 84727
Sequence Length: 775
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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Q8A624 | MGTVKCIGILTSGGDAPGMNAAIRAVTRAAIYNGLQVKGIYRGYKGLVTGEIKEFKSQNVSNIIQLGGTILKTARCKEFTTPEGRQLAYDNMKREGIDALVIIGGDGSLTGARIFAQEFDVPCIGLPGTIDNDLYGTDTTIGYDTALNTILDAVDKIRDTATSHERLFFVEVMGRDAGFLALNGAIASGAEAAIIPEFSTEVDQLEEFIKNGFRKSKNSSIVLVAESELTGGAMHYAERVKNEYPQYDVRVTILGHLQRGGSPTAHDRILASRLGAAAIDAIMEDQRNVMIGIEHDEIVYVPFSKAIKNDKPVKRDLVNVLKELSI | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 35257
Sequence Length: 326
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
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Q27483 | MEQKFKKGKDHGVGVLTSGGDSQGMNAAVRSVVRETIRQGHRCYLIREGYNGLINGNIELAKWAHVANVTHLGGSMIGTSRCDEFRTTDGRKKAAAIMFDKRIFHLIVIGGDGSLMGAQKLKEEWGRFGEELFAEGKITEEVANEGRELHLAGIVGSIDNDCIESDKSIGSDTALHRICEAIDGLVMTAQSHQRVFVVEVMGRHCGYLALTAAIAVEADYVFYPEIPPDEKWPEQLCHQLGSVRKMGKRQNVIILGEGVTNSKGQRIDVRQVKEEIETRLQLEVRIATLGHLQRGGAPSFLDRLIGLRMGYEAVQEVLKGKEEKEGAVVTGQKTIAKVMCLRGHNIQRNELSRVIRQTETANEEIMQRHSDLACRLRGFGFLDKQTYLNFVSIPLSTTMPSRTKTFAVVHIGSPCAGMNAATYSFTRMANHSGIQVIGIKHGWDGLKNKDVKLLTWANVQGWAQFGGSMLGTKRQLPSEMDLIAEGLNSNNVDGLVIIGGFMAFESALILQQNRSEYTCLSIPIVVIPATISNNCPGTCMSLGVDTALNEICRQVDNISQNAIGSKNKVMIIETMGSRSGFLATMTALSTGSQFALIRQVETNEKDLEKLAIETKERLDSGNLEKFLLIRSEGASDEIYSPDVKKIFDKVMKNKYGVRITNLGYSQLGGHPSCFDRQMGIRMGVRAFEGIVNPVKMGDRDCCVIGLRGSSLRYVPVQGLGKKVCFEHGVPHNMWWLDLHPLVEAMTKKPQEAVLSS | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 83301
Sequence Length: 756
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
|
O94200 | MISIVNGTSTLSLVAGSVETLNQAINFYTNILGLSVHSEQNDWTYLSNDDNKMIVKIQLDTKSGLSLDQVNDRRTEIIAKLNVTDWRSLDTTSVLKVQNLVALIETLTTFNYTLQITPNELYPNEVYCVGPIGYIIGFTACDEPLTLVPPLQKSHPKPGLVSNLMSKSGSQSRNIEETKAVRRNIAVMTSGGDSQGMNAAVRAVVRATIFHGSKAFAVQEGYAGLVKGGPEYIKEMKWQDVRGFLSEGGTNIGTARCMEFKERWGRLKGCKNLIDAGIDGLIVCGGDGSLTGADLFRHEWPSLIQELKDKGEITNEQFERHKHLYICGMVGSIDNDMAMTDATIGGYSALERICRAIDYIDATANSHSRAFVVEVMGRHCGWLALMAGIATSADYIFIPEKPASSKDWQDQMCDIVGKHRAQGKRKTIVIVAEGAITSDLKPITSDEVKDVLVDRLGLDTRITVLGHVQRGGTAVAFDRTLATLQGVEAVKAILELTPDVPSPLIAIDENKICRRPLVEAVRITKSVASAIEAKDFEKAMSLRDHEFKEHLANFMAMNTANHEKPTLPREKRKKIAIINIGAPAGGMNSAVYAMATYCMSRGHTPYAIHNGFAGLSRHESVKSIEWIDIEGWNSIGGSEIGTNRQTPEETDIGMIAHYFEKYQFDGLIIVGGFEAFVSLEQLERSRAMYPSFRIPMVLIPATISNNVPGTEYSLGADTCLNSLMEYCDIVKQSASATRGTAFIIDVQGGNSGYIATFASLISGAQASYVPEEGISLQQLEMDINSLREAFAVEQGMTKSGKLIIKSSNASKVLTPHTLADIFNDECHGDFDTKTAIPGHVQQGGLPSPIDRSRGDRFAIRAVQFIEDHCDVLAPYRYELDFPIDDKKILNTAAVLGIKSSRLRFTSIRHLFDFETELGRRMPKTIYWNTIRDISDQLVGRTRLDKP | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 104046
Sequence Length: 946
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
|
Q8XL57 | MMQPIKKIAILTGGGDCPGLNAVIRAVTRTAILKYGYEVIGYKFGYRGLYNNDFVKLDLDSVSGILHRGGTILHSSNKDNLFDYQVEDENGKIVKKDVSDVGVENLKKEGVDALVVIGGDGTLTSARDFSRKGVNVIGVPKTIDNDLLATDVTFGFNTATEIATEALDRLHTTAESHHRIMLLEVMGRNAGWIALESGIAGSADVILLPEIPYDINKIVEKVKEREEAGKQFTIIVVAEGAKPKDGEVVVSKIVDDSPDPIRLGGIANKLAIDLEGLIKNHEIRSTVLGHIQRGGNTSTYDRILSTKYGVKAVELINSNLFGNMVALKGNKVSYESLENVIGHTKNVDPEGELVNTAKSIGISFAD | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 39514
Sequence Length: 366
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
|
Q8YVR1 | MRKRIGILTSGGDCPGLNCVIRAVVSHATLTYDWEVLGIPYATQGLRERQAIALNMHGWDLRGIDPLLNMGGTILGTINKGDTLAHVDEMLASYQALALDALIVIGGDGSLGILHELASRGNWNLVAIPKTIDNDVALTERAVGFDTAVNTIVDALNRLTFTAASHDRVMIVEVMGRSAGHLALHAGIAGGADVILIPEISYTISGLCQHIAELRDRWQRKFAIVVVAEGAKLCLEDVQENIASSCAPSKCGRGQYIADQIAQCSKNLIDTRVSVLGHIQRGGIPSALDRLTATVFGKTAVDLIAQGKFGQMVAWQNGEAIPVPIQDVVAQSPLHVNPQGSLVQSARCLGIYVGEKT | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 38007
Sequence Length: 357
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
|
Q9L1L8 | MRIGVLTAGGDCPGLNAVIRSVVHRAVDNYGDEVIGFEDGYAGLLDGRYRALDLNAVSGILARGGTILGSSRLERDRLREACENAGDMIQNFGIDALIPIGGEGTLTAARMLSDAGLPVVGVPKTIDNDISSTDRTFGFDTAVGVATEAMDRLKTTAESHQRVMVVEVMGRHAGWIALESGMAAGAHGICLPERPFDPADLVKMVEERFSRGKKFAVVCVAEGAHPAEGSMDYGKGAIDKFGHERFQGIGTALAFELERRLGKEAKPVILGHVQRGGVPTAYDRVLATRFGWHAVEAAHRGDFGRMTALRGTDVVMVPLAEAVTELKTVPKDRMDEAESVF | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 36434
Sequence Length: 341
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
|
Q55988 | MGTKRIGILTSGGDCPGLNAVIRAVVKASALKGWEVYGIPYGTDGFVEVAHGKYQAEDLLLTKHGYALPGMLKGLDVLQFLSGSVLGSLSKGHPEQPAIAEAILKGYAILDLEALIVIGGDGSLDIIYDLAQKGNWHIIAIPKTIDNDVPFTDLAVGFSTAVDIVTQALYDLTFTAASHERIIIVQVMGRDAGHLTLHAGIAGGADIILIPEITPCLTSEIIRNCCYQLMNLRKSGRHFALIVISEGVHDQNNKKNKHIADYLAEEISETSQHLCDIKDPAFCDLISLDIRATTLGHLQRSGTPLSFDRLLATVFGIRAVELIEQEIYDQVVIWRSGKVEHADLKPIISIIKECHQENRCPFPVDRDGFMVKTAKSLGIYLGED | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 41759
Sequence Length: 384
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
|
P16862 | MTVTTPFVNGTSYCTVTAYSVQSYKAAIDFYTKFLSLENRSSPDENSTLLSNDSISLKILLRPDEKINKNVEAHLKELNSITKTQDWRSHATQSLVFNTSDILAVKDTLNAMNAPLQGYPTELFPMQLYTLDPLGNVVGVTSTKNAVSTKPTPPPAPEASAESGLSSKVHSYTDLAYRMKTTDTYPSLPKPLNRPQKAIAVMTSGGDAPGMNSNVRAIVRSAIFKGCRAFVVMEGYEGLVRGGPEYIKEFHWEDVRGWSAEGGTNIGTARCMEFKKREGRLLGAQHLIEAGVDALIVCGGDGSLTGADLFRSEWPSLIEELLKTNRISNEQYERMKHLNICGTVGSIDNDMSTTDATIGAYSALDRICKAIDYVEATANSHSRAFVVEVMGRNCGWLALLAGIATSADYIFIPEKPATSSEWQDQMCDIVSKHRSRGKRTTIVVVAEGAIAADLTPISPSDVHKVLVDRLGLDTRITTLGHVQRGGTAVAYDRILATLQGLEAVNAVLESTPDTPSPLIAVNENKIVRKPLMESVKLTKAVAEAIQAKDFKRAMSLRDTEFIEHLNNFMAINSADHNEPKLPKDKRLKIAIVNVGAPAGGINSAVYSMATYCMSQGHRPYAIYNGWSGLARHESVRSLNWKDMLGWQSRGGSEIGTNRVTPEEADLGMIAYYFQKYEFDGLIIVGGFEAFESLHQLERARESYPAFRIPMVLIPATLSNNVPGTEYSLGSDTALNALMEYCDVVKQSASSTRGRAFVVDCQGGNSGYLATYASLAVGAQVSYVPEEGISLEQLSEDIEYLAQSFEKAEGRGRFGKLILKSTNASKALSATKLAEVITAEADGRFDAKPAYPGHVQQGGLPSPIDRTRATRMAIKAVGFIKDNQAAIAEARAAEENFNADDKTISDTAAVVGVKGSHVVYNSIRQLYDYETEVSMRMPKVIHWQATRLIADHLVGRKRVD | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 104618
Sequence Length: 959
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
|
Q94AA4 | MSTVESSKPKIINGSCGYVLEDVPHLSDYLPGLPTYPNPLQDNPAYSVVKQYFVDADDSVPQKIVVHKDGPRGIHFRRAGPRQKVYFESDEVHACIVTCGGLCPGLNTVIREIVSSLSYMYGVKRILGIDGGYRGFYAKNTVSLDSKVVNDIHKRGGTILGTSRGGHDTTKIVDSIQDRGINQVYIIGGDGTQRGASVIFEEIRRRGLKVAVIGIPKTIDNDIPVIDKSFGFDTAVEEAQRAINAAHVEAESIENGIGVVKLMGRYSGFIAMYATLASRDVDCCLIPESPFYLEGEGGLFEYIEKRLKESGHMVLVIAEGAGQDLMSKSMESMTLKDASGNKLLKDVGLWLSQSIKDHFNQKKMVMNLKYIDPTYMIRAVPSNASDNVYCTLLAQSAVHGAMAGYTGYISGLVNGRQTYIPFYRITEKQNHVVITDRMWARLLSSTNQPSFLGPKDVFDNKEKPMSALLDDGNCNGVVDVPPVTKEITK | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 53666
Sequence Length: 489
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
|
Q8A2E9 | MRIGILTSGGDCPGINATIRGVCKTAINHYGMEVIGIHSGFQGLLTKDIESFTDKSLSGLLNQGGTMLGTSREKPFKKGGVVSDVDKPALILQNIQEMGLDCVVCIGGNGTQKTAAKFAAMGVNIVSVPKTIDNDIWGTDISFGFDSAVSIATDAIDRLHSTASSHKRVMVIEVMGHKAGWIALYSGMAGGGDVILVPEIPYNIKNIGNTILERLKKGKPYSIVVVAEGILTDGRKRAAEYIAQEIEYETGIETRETVLGYIQRGGSPTPFDRNLSTRMGGHATELIANGQFGRMIALKGDDISSIPLEEVAGKLKLVTEDHDLVIQGRRMGICFG | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 35853
Sequence Length: 336
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
|
Q30T53 | MKNIAILSSGGDVSGMNPAIKHFVEYALHNGLTPYFVYNGFEGLIDNKITKASHSDVAGIINRGGTILGSSRSKRFMLKNYREVAKKNLDALDIDMLIVLGGDGSFRGMDIFYKEHGVKFCGIPSTIDNDINGTIYCLGVDTALNVIKDSIDNIRDTASSFSRAFVIETMGRDCGYLALVSSLCSGAELCLIPEVEYNLSSYEDSFKEQIKNGRKYFIVIVSEGIKDNSKEIAEWLEQKVGIESRVTVLGHTQRGGTPSIYDRLMAYKFVNHAIDALLGDINSSVVCYSKTGFIHKDIDEITSQKYMLDPELLSYLKKF | Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 35330
Sequence Length: 319
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
|
Q9WY52 | MKKIAVLTSGGDAPGMNAAVRAVVRYGVRQGLEVIGVRRGYSGLIDGDFVKLEYKDVAGITEKGGTILRTSRCEEFKTEEGRELAAKQIKKHGIEGLVVIGGEGSLTGAHLLYEEHKIPVVGIPATIDNDIGLTDMCIGVDTCLNTVMDAVQKLKDTASSHERAFIVEVMGRHSGYIALMAGLVTGAEAIIVPEIPVDYSQLADRILEERRRGKINSIIIVAEGAASAYTVARHLEYRIGYETRITILGHVQRGGSPTAFDRRLALSMGVEAVDALLDGEVDVMIALQGNKFVRVPIMEALSTKKTIDKKLYEIAHMLS | Cofactor: Mg(2+). Mg(2+) can partially be replaced by Mn(2+) and Fe(2+).
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 34487
Sequence Length: 319
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Subcellular Location: Cytoplasm
EC: 2.7.1.11
|
P32207 | MENPVRINTLYNVFVERYIENLSIYSIPINSTCGIHIGEIKGTFKRCFLKILNMCINDKELSFNILIKTLKDVTSTLSQKEKEELSKEIGIDILNNDPKYVPEIIRNCSSSADVTNIIDIQTLDVGKCIAPYDKQILLQIVNSGTAEANCVMNSIMNSMNRRYIDNANIYNYLNLTNRPWFIFSIIIIAIIFVIGICSIKRRIGIKYKYGTFLYV | Function: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.
PTM: Disulfid bonds are oxidized in the cytoplasm by OPG088 protein.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24641
Sequence Length: 215
Subcellular Location: Virion membrane
|
P24361 | MAETKEFKTLYNLFIDSYLQKLAQHSIPTNVTCAIHIGEVIGQFKNCALRITNKCMSNSRLSFTLMVESFIEVISLLPEKDRRRIAEEIGIDLDDVPSAVSKLEKNCNAYAEVNNIIDIQKLDIGECSAPPGQHMLLQIVNTGSAERNCGLQTIVKSLNKIYVPPIIENRLPYYDPWFLVGVAIILVIFTVAICSIRRNLALKYRYGTFLYV | Function: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.
PTM: Disulfid bonds are oxidized in the cytoplasm by OPG088 protein.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23962
Sequence Length: 212
Subcellular Location: Virion membrane
|
P07613 | MEVITDRLDDIVKQNIADEKFVDFVIHGLEHQCPAILRPLIRLFIDILLFVIVIYIFTVRLVSRNYQMLLALVALVITLTIFYYFIL | Function: Early protein involved in virion morphogenesis. Participates in the formation and elongation of crescent-shaped membrane precursors of immature virions in cytoplasmic factories.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10255
Sequence Length: 87
Subcellular Location: Virion membrane
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P0DOU1 | MENVPNVYFNPVFIEPTFKHSLLSVYKHRLIVLFEVFVVFILIYVFFRSELNMFFMHKRKIPDPIDRLRRANLACEDDKLMIYGLPWITTQTSALSINSKPIVYKDCAKLLRSINGSQPVSLNDVLRR | Function: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.
PTM: Most cysteines are linked by disulfide bonds. They are created by the viral disulfide bond formation pathway, a poxvirus-specific redox pathway that operates on the cytoplasmic side of the MV membranes.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 15066
Sequence Length: 128
Subcellular Location: Virion membrane
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P0DSX7 | MNSLSIFFIVVATAAVCLLFIQGYSIYENYGNIKEFNATHAAFEYSKSIGGTPALDRRVQDVNDTISDVKQKWRCVAYPGNGFVSASIFGFQAEVGPNNTRSIRKFNTMAQCIDFTFSDVINIDIYNPCVAPNINNVECQFLKSVL | Function: Envelope protein required for virus entry into host cell and for cell-cell fusion (syncytium formation).
PTM: Contains two intramolecular disulfide bonds. They are created by the viral disulfide bond formation pathway, a poxvirus-specific pathway that operates on the cytoplasmic side of the MV membranes.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 16244
Sequence Length: 146
Subcellular Location: Virion membrane
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Q5A343 | MRSPSLAVAATTVLGLFSSSALAYYGNTTTVALTTTEFVTTCPYPTTFTVSTCTNDVCQPTVVTVTEETTITIPGTVVCPVVSTPSGSASASASAGASSEEEGSVVTTQVTVTDFTTYCPYPTTLTITKCENNECHPTTIPVETATTVTVTGEVICPTTTSTSPKESSSEAASSEVITTQVTVTDYTTYCPLPTTIVVSTCDEEKCHPTTIEVSTPTTVVVPGTVVCPTTSVATPSQSEVATKPTTINSVVTTGVTTTDYTTYCPSPTTIVVSTCDEEKCHPTTIEVSTPTTVVVPGTVVHPSTSATIITTTAEQPPASPEVSTIESVVTTPATLTGYTTYCPEPTTIVLTTCSDDQCKPHTVSATGGETVSIPATIVVPSSHTTQVEITVSSASVPASEKPTTPVTVAAVSSSPAVSTETPSLVTPAISIAGAAAVNVVPTTAFGLFAIILASIF | Function: Cell wall protein which contributes to cell wall synthesis and is important for acquiring normal surface properties. Required for virulence in a mouse infection model.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Location Topology: Lipid-anchor
Sequence Mass (Da): 46501
Sequence Length: 456
Subcellular Location: Secreted
|
Q5A4X8 | MKFTTVATVFAISSLAAAKGGEKDHGKASTVTKYVTETTHRYGRFDKTSRSKKPKETGTHRYGKFNKTPRPVTTTVLVKESDLPKKRDAVVARDSKNASSNSTTSSGNNGVATGVSLGLAGVLAVGAALVI | Function: Hydrophilin which is essential to overcome the simple stress of the desiccation-rehydration process.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 13744
Sequence Length: 131
Subcellular Location: Secreted
|
P53872 | MKFSSVTAITLATVATVATAKKGEHDFTTTLTLSSDGSLTTTTSTHTTHKYGKFNKTSKSKTPNHTGTHKYGKFNKTSKSKTPNHTGTHKYGKFNKTSKSKTPNHTGTHKYGKFNKTSKSKTPNHTGTHKYGKFNKTSKSKTPNHTGTHKYGKFNKTKHDTTTYGPGEKARKNNAAPGPSNFNSIKLFGVTAGSAAVAGALLLL | Function: Hydrophilin which is essential to overcome the simple stress of the desiccation-rehydration process.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Location Topology: Lipid-anchor
Sequence Mass (Da): 21966
Sequence Length: 204
Subcellular Location: Secreted
|
Q5A1E1 | MKFIIILFTLISIVTAAQRIYNKDYSYYGCNSYCDKASDQEDACGYYDDDVSYQDYYGCLCGNEIFLSNLKSCDCFTSIIASVSKSVCSKATEDSDWGYYDDSTSSIMDFFTADNTPASNTGMTTQTDGAINDNQNTGSKTSSGAANYLTSFSIGTFFVFVLGLI | Function: Probable GPI-anchored cell wall protein that may be involved in cell wall organization, hyphal growth, as well as in virulence.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 18105
Sequence Length: 165
Subcellular Location: Secreted
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P96740 | MNTLANWKKFLLVAVIICFLVPIMTKAEIAEADTSSELIVSEAKNLLGYQYKYGGETPKEGFDPSGLIQYVFSKADIHLPRSVNDQYKIGTAVKPENLKPGDILFFKKEGSTGTVPTHDALYIGDGQMVHSTQSKGVIITNYKKSSYWSGTYIGARRIAADPATADVPVVQEAEKYIGVPYVFGGSTPSEGFDCSGLVQYVFQQALGIYLPRSAEQQWAVGEKVAPQNIKPGDVVYFSNTYKTGISHAGIYAGAGRFIQASRSEKVTISYLSEDYWKSKMTGIRRFDNLTIPKENPIVSEATLYVGEVPYKQGGVTPETGFDTAGFVQYVYQKAAGISLPRYATSQYNAGTKIEKADLKPGDIVFFQSTSLNPSIYIGNGQVVHVTLSNGVTITNMNTSTYWKDKYAGSIRVQ | Function: Cleaves, in an endo-type manner, the gamma-glutamyl bond between D-glutamate and L-glutamate of poly-gamma-glutamate (PGA).
Sequence Mass (Da): 45247
Sequence Length: 413
Subcellular Location: Secreted
EC: 3.4.19.-
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Q7ZUC7 | MAAACTRTLGKVGRLVLDTPTCRFTNTAAFVPRTSMRCQGRAYGTGSSGFKSRLLLAAPVRGSGRVLGCAFLLGGGFGLYQTIKLTLQHHLAEKESDASDLDTDLKLTLYQYKTCPFCSKVRAFLDYHRLPYEIVEVNPVMRQEIKWSTYRKVPILMVNGTVQLNDSSVIISALKTYISSKDKKISEILACYPEMKSKNDRGKDVIEFGNKYWVMVHDADADQLYPGKDSRKEEIKWRTWADDWLVHLISPNVYRTPTEALASFDYIVREGKFGSFEGFFAKYFGAAAMWIISKRLKYKHNLQADVRQDLYKAVNDWVAAIGKNKQFMGGDEPNLADLAVFGVLRVMEGLQSFDDMMEHTKVKKWYSRMQKATQHVS | Function: Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2) (in vitro). The biological function and the GSH-dependent property of PTGES2 is still under debate (By similarity). In vivo, PTGES2 could form a complex with GSH and heme and would not participate in PGE2 synthesis but would catalyze the degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA) (By similarity).
Catalytic Activity: prostaglandin H2 = prostaglandin E2
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 42792
Sequence Length: 377
Pathway: Lipid metabolism; prostaglandin biosynthesis.
Subcellular Location: Golgi apparatus membrane
EC: 5.3.99.3
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Q9H7Z7 | MDPAARVVRALWPGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGPSPVAAARKGSPRLLGAAALALGGALGLYHTARWHLRAQDLHAERSAAQLSLSSRLQLTLYQYKTCPFCSKVRAFLDFHALPYQVVEVNPVRRAEIKFSSYRKVPILVAQEGESSQQLNDSSVIISALKTYLVSGQPLEEIITYYPAMKAVNEQGKEVTEFGNKYWLMLNEKEAQQVYGGKEARTEEMKWRQWADDWLVHLISPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQDNVREDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQPWYLRVERAITEASPAH | Function: Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2) (in vitro) . The biological function and the GSH-dependent property of PTGES2 is still under debate . In vivo, PTGES2 could form a complex with GSH and heme and would not participate in PGE2 synthesis but would catalyze the degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA) (By similarity).
PTM: Synthesized as a Golgi membrane-associated protein, and the proteolytic removal of the N-terminal hydrophobic domain leads to the formation of a mature cytosolic enzyme.
Location Topology: Single-pass membrane protein
Catalytic Activity: prostaglandin H2 = prostaglandin E2
Sequence Mass (Da): 41943
Sequence Length: 377
Pathway: Lipid metabolism; prostaglandin biosynthesis.
Subcellular Location: Golgi apparatus membrane
EC: 5.3.99.3
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Q8BWM0 | MAQAARLSWVLVSSRCALTEGLLTRPWQPLSAQSRAGFTRVAAGSRGAAVRKGSPRLLGAAALALGGALGLYHTVRWHQRSQDLRAERSAAQLPLSNSLQLTLYQYKTCPFCSKVRAFLDFHSLPYQVVEVNPVRRTEIKFSSYRKVPILVAQEGDSLQQLNDSSVIISALKTYLVSGQPLEEVITYYPPMKAMNDQGKEVTEFCNKYWLMLDEKEAQQMYGGKEARTEEMKWRQWADDWLVHLISPNVYRTPAEALASFDYIVREGKFGAVEAAMAKYVGAAAMYLISKRLKSRHHLQDDVRVDLYEAANKWVTAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLEAFDDLMRHSHIQPWYLRMERAIEEAPSVHHVNPSCKD | Function: Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2) (in vitro). The biological function and the GSH-dependent property of PTGES2 is still under debate (By similarity). In vivo, PTGES2 could form a complex with GSH and heme and would not participate in PGE2 synthesis but would catalyze the degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA) (By similarity). May also have transactivation activity toward IFN-gamma (IFNG), possibly via an interaction with CEBPB; however, the relevance of transcription activation activity remains unclear .
PTM: Synthesized as a Golgi membrane-associated protein, and the proteolytic removal of the N-terminal hydrophobic domain leads to the formation of a mature cytosolic enzyme.
Location Topology: Single-pass membrane protein
Catalytic Activity: prostaglandin H2 = prostaglandin E2
Sequence Mass (Da): 43324
Sequence Length: 384
Pathway: Lipid metabolism; prostaglandin biosynthesis.
Subcellular Location: Golgi apparatus membrane
EC: 5.3.99.3
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B1XWA3 | MKILRLQDLIAAGQVAGQRVFIRADLNVPQDDAGHITEDTRIRASIPCIEMALKAGAAVMVTSHLGRPTEGEFKPEDSLAPVAARMGELMGREIPVIANWTDGVEVAPGQLVMLENCRLNKGEKKNNEALAQKMAALCDIFVHDAFGTAHRAEASTYGIAQFAKIACAGPLLAAEIDAISLALANPKRPLVAIVAGSKVSTKLTILKALSANVDGLIVGGGIANTFLLAAGLSIGKSLAEPDLVGEARAVIDAMKARGAAVPIPVDVVCAKTFSPTAEATVKAATDVADDDLILDIGPQTAAILAAQLKAAGTIVWNGPVGVFEFDAFAHGTETLARAIAESDAFSIAGGGDTLAAIAKYGIEKDVGYISTGGGAFLEVLEGKTLPAFEILTKRAAG | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 40939
Sequence Length: 397
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
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Q8F5H8 | MELPRLENVDLSGKRVFLRVDFNVPVENGKVTDKTRIEKTLPTIELLIKKGARIIIASHLGRPKGQVNPEFSLAPVVETFQSLVKSKVYFSKTVIGEDAIKLSKELKNGEILVIENVRFHKEEEENDPGFSKKLSALADIYVNDAFGAAHRAHSSTEGIARLLPAYAGLLMHKEILELSALLHKPARPFVAIIGGSKVSTKIKVLTNLFDKVNHLLIGGGMAYTFLKSRAIPIGNSLVEKEFEVQAFQLIEKAGVAGIDLQLPVDHIIGDQFNEKAKTKSVDKMGILDGWMGMDIGSKTVSNYEKIIKNAGTIFWNGPMGVFEMDKFASGTMAIAKAVAKSKAKTVVGGGDSIAAINKAGVADKITHISTGGGASLEFMEGRKLPGVEALKKKTSE | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 42919
Sequence Length: 396
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
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Q03UX8 | MAKLTVSDLELSGKKVLMRVDFNVPIKAGVIGNDNRIVAALPTIKYVLENNGRAILFSHLGRIKSEDDKKELSLAPVAARLGELLGKDVKFVPQTRGEELESAINALQDGEVLMVENTRFEDVVDGEVVKNESKNNPELGKYWASLGDDLFINDAFGTAHRAHASNVGIASNVSQAAAGFLMEKEIKFLGDAVANPVRPFVAIIGGAKVSDKIEIVKSLLNKADKVIVGGGMAYTFDAAKGNKIGNSLFEADKVELAKELMAEAGDKLVLPIDSIAADAFSNDAKTEVVDAEDGIPDGYMGLDIGPKSVKLLQDTLSDAKTVVWNGPMGVFEMSNFAKGTLAIGEELVKVTENGGTTIVGGGDSTAAVQQLGVADKLTHISTGGGASLEYLEGKELPGIASISEK | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 42728
Sequence Length: 405
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
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O60101 | MSLSTKLAITDVDLKGKNVLIRVDFNVPLDGDRITNNARIVGALPTIKYALEQQPKAVILMSHLGRPNGARVAKYSLKPVAAELSKLLGKPVKFLDDCVGPEVEKACKEAKGGEVILLENLRFHIEEEGSAKVDGKKVKADASAVEAFRKSLTSLGDIFVNDAFGTAHRAHSSMVGVDLPRVSGFLMKKELDYFSKALENPARPFLAILGGAKVADKIQLIDNLLDKVNRLIICGGMAFTFLKVLNGMKIGDSLFDEAGSKNVESMMAKAKKNNVEVFLPVDFVTADKFDKDAKVGSATAEEGIPDGWMGLDCGPKSSAKFAEVITTSKTIVWNGPAGVFEFDNFAKGTKSMLDACVKTCEAGNVVIVGGGDTATVAKKYGKEDALSHVSTGGGASLELLEGKALPGVVALSSK | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 43964
Sequence Length: 414
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
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A8H0N0 | MTILNMKDLDLQGKRVLIREDLNVPVSDGVVTSDARLRASLPTIKLALEKGAAVMVMSHLGRPTEGEFNAEFSMQPVVDYLTKALDCPVRLAADYLDGIEVAVGEVVVFENVRFNLGEKKNDEALAKKMAALCDVYVMDAFGTAHRAQASTHGVGLHAPIACAGPLLAGELEALGKALDNPARPMVAIVGGSKVSTKLTVLESLSTKVDQLVVGGGIANTFVAAAGHKVGKSLYEADLIEEAQRLVANAQSRGGDIPVPTDVVVAGEFSPTATATLKDVSDVSDTDMIFDIGPDSAEALAEIIKNAGTVVWNGPVGVFEFDQFGEGTKRIAQAIAESNAFSIAGGGDTLAAVDKYGIADKVSYISTGGGAFLEFLEGKELPAVAMLESRGQ | Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Mass (Da): 40876
Sequence Length: 391
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Subcellular Location: Cytoplasm
EC: 2.7.2.3
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Q0P9C5 | MMKISFIIATLNSGGAERALVTLANALCKEHEVSIIKFHAGESFYKLENEVKVTSLEQFRFDTLYHKIASRFKKFFALRKALKESKSDVFISFLDTTNIACIAAKIGLKTPLIISEHSNEAYLKPKIWRFLRRVSYPFCDALSVLGSSDKVYYERFVKRVKLLLNPCHFSDEISFDSSFEKENLVLFIGRLDHNKNPVMFLKAIAHLDKNLQENYKFVIAGDGQLRQELEYKVKSLGIKVDFLGRVENVKALYEKAKVLCLCSFVEGLPTVLIESLYFEVCRISSSYYNGAKDLIKDNHDGLLVGCDDEIALAKKLELVLNDENFRKELVNNAKQRCKDFEISHIKEEWLKLIAEVKNA | Function: Processive glycosyltransferase that is part of the biosynthetic pathway of the lipid-linked oligosaccharide (LLO) that serves as the glycan donor in bacterial protein N-glycosylation. Catalyzes the transfer of exactly three alpha-(1->4)-N-acetylgalactosamine (GalNAc) units to the growing LLO precursor, GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenyl . Cannot accept UDP-GlcNAc as substrate .
Catalytic Activity: N-acetyl-alpha-D-galactosaminyl-(1->4)-N-acetyl-alpha-D-galactosaminyl-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-tri-trans,heptacis-undecaprenyl diphosphate + 3 UDP-N-acetyl-alpha-D-galactosamine = [alpha-D-GalNAc-(1->4)]4-alpha-D-GalNAc-(1->3)-alpha-D-diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate + 3 H(+) + 3 UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 41163
Sequence Length: 359
Domain: Contains an amphipathic helix (''ruler helix'') that has a dual role of facilitating membrane attachment and glycan counting. The ruler helix contains three positively charged side chains (Lys-67, Arg-71 and Lys-74) that can bind the pyrophosphate group of the LLO substrate and thus limit the addition of GalNAc units to three.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Cell inner membrane
EC: 2.4.1.292
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Q0P9C6 | MPKLSVIVPTFNRQVLLEKAIKSIQNQDFKDLEIIVSDDNSSDDTKSVVQNLQKDDDRIKYFLNQNYKQGPNGNKNNGLDQASGEFVTFLDDDDELLSGALSTLMQKANEGYAHVFGNCLIEKEGNLSKEFSGKGLEKDSEISKKDFLMAKFSGEFFSVFKKSLLENKRFNEEFYGNEATLWVNLYKEKSFYIHKAFRIYRIFRQDSVTLGASKNAYRVYLGYLELAKILENELRMSKDKDYKKTCASYYKMAAYYAKLAKNYKALYKCLFKSLSIKINAPALILLILSIIPNNMIEKLSKIRVALCKN | Function: Glucosyltransferase that adds he final branching glucose to complete the final heptasaccharide structure in the N-linked protein glycosylation pathway.
Catalytic Activity: [alpha-D-GalNAc-(1->4)]4-alpha-D-GalNAc-(1->3)-alpha-D-diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate + UDP-alpha-D-glucose = [alpha-D-GalNAc-(1->4)]2-[beta-D-Glc-(1->3)]-[alpha-D-GalNAc-(1->4)]2-alpha-D-GalNAc-(1->3)-alpha-D-diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 35511
Sequence Length: 309
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
EC: 2.4.1.293
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Q0P9C7 | MQKLGIFIYSLGSGGAERVVATLLPILSLKFEVHLILMNDKISYEIPECQIHFLECSKPSENPILKFLKLPFLALKYKKLCRNLGIDTEFVFLNRPNYIALMARMFGNKTRLVINECTTPSVMYMKNNFNSLVNKFLISLLYPKADLILPNSKGNLEDLVQNFSISPKKCEILYNAIDLENIGQKALEDIALKDKFILSVGRLDKGKNHALLIRAYARLKTDLKLVILGEGVLKDELLALIKELNLEEKVLLLGFDNNPYKYMAKCEFFAFASVFEGFSNVLIESLACSCAVVCTDHKSGARELFGDDEFGLLVEVDNENSMFQGLKTMLEDDKLRKAYKNKAKTRAKAFDKVKIARDALKYLLG | Function: Adds a GalNAc residue on to the Und-PP-Bac2,4diNAc-GalNAc disaccharide in the N-linked protein glycosylation pathway. Transfers the third sugar in the heptasaccharide biosynthesis.
Catalytic Activity: N-acetyl-alpha-D-galactosaminyl-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-tri-trans,hepta-cis-undecaprenyl diphosphate + UDP-N-acetyl-alpha-D-galactosamine = H(+) + N-acetyl-alpha-D-galactosaminyl-(1->4)-N-acetyl-alpha-D-galactosaminyl-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-tri-trans,heptacis-undecaprenyl diphosphate + UDP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 41308
Sequence Length: 365
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Cell inner membrane
EC: 2.4.1.291
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Q0P9C4 | MLKKLFFILSKEDKNFLFFLLVFSVFISFIETFAISLVMPFITLASDFSYFDRNKYLISLKEYLNIPVFEIIVYFGVGLIVFYVFRALLNAYYFHLLARFSKGRYHAIAYKVFSKFLNINYEKFTQKNQSEILKSITGEVYNLSTMISSFLLLMSEIFVVLLLYALMLLINYKITLFLSIFMVLNAFILVKILSPIIKKAGVRREEAMKNFFEILNTNLNNFKFIKLKTKEDGVLSLFKAQSEAFSKANITNESVAAVPRIYLEGIGFCVLVFIVVFLVLKNESDISGILSTISIFVLALYRLMPSANRIITSYHDLLYYHSSLDIIYQNLRQEEENLGEEKLSFNQELKICNLSFGYEGKKYLFKNLNLNIKKGEKIAFIGESGCGKSTLVDLIIGLLKPKEGQILIDEQELNANNTKNYRQKIGYIPQNIYLFNDSIAKNITFGDAVDEEKLNRVIKQANLEHFIKNLPQGVQTKVGDGGSNLSGGQKQRIAIARALYLEPEMLVLDEATSALDTQSEAKIMDEIYKISKDKTMIIIAHRLSTITQCDKVYRLEHGKLKEEK | Function: Mediates the ATP-dependent translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate across the cell membrane; this is an essential step during the N-linked protein glycosylation pathway. Transport across the membrane is effected via ATP-driven conformation changes. Most likely, only the polar and charged part of the glycolipid enter the substrate-binding cavity, and the lipid tail remains exposed to the membrane lipids during the transmembrane flipping process.
Catalytic Activity: ATP + H2O + lipopolysaccharideSide 1 = ADP + phosphate + lipopolysaccharideSide 2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64739
Sequence Length: 564
Domain: In the absence of ligand, the homodimer has a V-shaped structure with a large cavity that is accessible from the cytoplasmic side.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Cell inner membrane
EC: 7.5.2.5
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Q6FFS6 | MAGSPRVYNSQHCGFSVAVMRFLLLLLTAVLISLAWLSPDHSYPWLTFASEMLSFAAFLSLLALFLNRPLELPRVQLLALPVVFIPMIQWGFGLVVDFSSALLSSAYLLGFWLTMLLGYNLSRSSADRERMFTLSSYLLFAVALLTSLIACIQWLNLESHVPGVMNLYSHRPYANFAQPNNMSTFLILGLLGCLYLAEKQKLKQYYIWPVAALIVFAITLSQSRTAWVFGLFFIIYWTYKSWRYPTHLKRYAVLLWAIGFFAVGLLFPRFTRLIQKLKEGNVVQTSSVVERASAGHERLGIWQQMLDAIHQKPWTGYGWNQTSIAELSSMSSNTIHVWFTSAHNVVLDLLVWNGWLLGGLITICILIWICWLNVHAKTTESIIACLMVSAVWIHTLLEYPLQYAYFLLPVGFLMGLIQAQTPDQTARSVPVSVIRSIWVIGIMLLALIWRDYNLYKVNSLRILKNQPANIEIWGSSKILVLTEFDQRLYWLKLSPVAPLTSTELDQIEKMVQNKATPYNLQKYAQLLLANHQFEKAQQQIAYLNRLHKKDYTLQDLQQANASAVESSK | Function: Catalyzes the O-glycosylation of multiple protein targets. Is responsible for general protein glycosylation within A.baylyi ADP1. Does not act as an O-antigen ligase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64866
Sequence Length: 568
Subcellular Location: Cell membrane
EC: 2.4.-.-
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Q6F7F9 | MNSIFKKIKNYTIVSGVFFLGSAFIIPNTSNLSSTLYKELIAVLGLLILLTVKSFDYKKILIPKNFYWFLFVIFIIFIQLIVGEIYFFQDFFFSISFLVILFLSFLLGFNERLNGDDLIVKKIAWIFIIVVQISFLIAINQKIEIVQNFFLFSSSYNGRSTANLGQPNQFSTLILITLFLLCYLREKNSLNNMVFNILSFCLIFANVMTQSRSAWISVILISLLYLLKFQKKIELRRVIFFNIVFWTLVYCVPLLFNLIFFQKNSYSTFDRLTMGSSRFEIWPQLLKAVFHKPFIGYGWGQTGVAQLETINKSSTKGEWFTYSHNLFLDLMLWNGFFIGLIISILILCFLIELYSSIKNKSDLFLFFCVVAFFVHCLLEYPFAYTYFLIPVGFLCGYISTQNIKNSISYFNLSKRKLTLFLGCCWLGYVAFWVEVLDISKKNEIYARQFLFSNHVKFYNIENYILDGFSKQLDFQYLDYCELKDKYQLLDFKKVAYRYPNASIVYKYYSISAEMKMDQKSANQIIRAYSVIKNQKIIKPKLKFCSIEY | Function: Specifically catalyzes the glycosylation of the pilin-like competence factor ComP.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64444
Sequence Length: 548
Subcellular Location: Cell membrane
EC: 2.4.-.-
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P49062 | MANARSLVAKANNINVGSLILMALVFGSCVANGEYLGGRRGLAANSGNPTVYDITKFGAVGDGSTNTFKAFLNTWIQVCDSPVPATLLVPKGTFLAGPVIFAGPCKSKVTVNVIGTIIATTSGYATPEWFLFERVDNLVLTGTGTFHGKGEAVWKADGCGKKVQCNLPPTSLKFRNMKNVEINGISSVNAKAFHMFLVKTENVNIQNIKLTAPAESPNTDGIHLSNADNVSILDSTIATGDDCVSVGRGSNNVTVERVICGPGHGLSVGSLGKYKNEEDVSGIHVNNCTMIETDNGLRIKTWGGSDPSKAVDIKFENIIMQSVKNPIIIDQNYGSRGGDSQVAISDILFKNIRGTTITKDVVQIMCSKSVPCQGVNVVDVNLDYVGKTGGEKKSSSGGLVGALCDNANVIFGGKLSFPMCPK | Function: May function in depolymerizing pectin during pollen development, germination, and tube growth. Acts as an exo-polygalacturonase.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-galacturonosyl](n-1) + alpha-D-galacturonate
Sequence Mass (Da): 44430
Sequence Length: 422
Subcellular Location: Secreted
EC: 3.2.1.67
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P26213 | MHSYQLLGLAAVGSLVSAAPAPSRVSEFAKKASTCTFTSASEASESISSCSDVVLSSIEVPAGETLDLSDAADGSTITFEGTTSFGYKEWKGPLIRFGGKDLTVTMADGAVIDGDGSRWWDSKGTNGGKTKPKFMYIHDVEDSTFKGINIKNTPVQAISVQATNVHLNDFTIDNSDGDDNGGHNTDGFDISESTGVYISGATVKNQDDCIAINSGESISFTGGTCSGGHGLSIGSVGGRDDNTVKNVTISDSTVSNSANGVRIKTIYKETGDVSEITYSNIQLSGITDYGIVIEQDYENGSPTGTPSTGIPITDVTVDGVTGTLEDDATQVYILCGDGSCSDWTWSGVDLSGGKTSDKCENVPSGASC | Function: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.
Catalytic Activity: (1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.
Sequence Mass (Da): 38108
Sequence Length: 368
Subcellular Location: Secreted
EC: 3.2.1.15
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Q2UHL4 | MHFQLLGLAALGSLAAAAPAPSRTSELVERGSSCTFTSAAQASASAKSCSNIVLKNIAVPAGETLDLSKAKDGATITFEGTTTFGYKEWKGPLIRFGGNKITVTQAAGAVIDGQGSRWWDGKGTNGGKTKPKFIYAHKLQSSTIKGLHVKNSPVQVFSVQGNDVHLTDITIDNSDGDNNGGHNTDAFDVSESNGVYITGANVKNQDDCLAINSGENIEFTGATCSGGHGISIGSIGNRDSNTVKNVKVADSTVVDSDNGIRIKTISGATGSVSGVTYENITLKNIKKNGIVIEQDYKNGGPTGKPTTGVPITDLTVNGVTGSVASKATPVYILCGKGSCSDWTWKGVSISGGKKSDKCQNIPSGASC | Function: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.
Catalytic Activity: (1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.
Sequence Mass (Da): 37798
Sequence Length: 367
Subcellular Location: Secreted
EC: 3.2.1.15
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Q00446 | MVSYLFVLGALASVAIASPVPELKARASCTFTDAASAIKGKASCTTIVLNNIAVPAGTTLDMTGLKSGTHVSFSGKTTFGYKEWEGPLISFSGSNVVIDGASGHSIDCQGSRWWDSKGGNGGKTKPKFFYAHSLKDSTIRGLHTLNTPVQAFSINGAANLGVYDVSVDNSAGDSAGGHNTDAFDVGSSTGVYISGADVKNQDDCLAVNSGTNITFTGGTCSGGHGLSIGSVGGRKDNVVKSVSITNSKIINSDNGVRIKTVAGATGPVSDITYSGITLSNIAKYGIVIEQDYENGSPTGKPTSGVPISGLTLSKISGSVSSSATPVYILCASCTNWKWSGVSVTGGKKSSKCTGIPSGSGAAC | Function: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.
Catalytic Activity: (1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.
Sequence Mass (Da): 36712
Sequence Length: 363
Subcellular Location: Secreted
EC: 3.2.1.15
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P26216 | MACTNNAMRALFLLVLFCIVHGEKEESKGIDAKASGPGGSFDITKLGASGNGKTDSTKAVQEAWASACGGTGKQTILIPKGDFLVGQLNFTGPCKGDVTIQVDGNLLATTDLSQYKDHGNWIEILRVDNLVITGKGNLDGQGPAVWSKNSCTKKYDCKILPNSLVMDFVNNGEVSGVTLLNSKFFHMNMYRCKDMLIKDVTVTAPGDSPNTDGIHMGDSSGITITNTVIGVGDDCISIGPGTSKVNITGVTCGPGHGISIGSLGRYKDEKDVTDINVKDCTLKKTMFGVRIKAYEDAASVLTVSKIHYENIKMEDSANPIFIDMKYCPNKLCTANGASKVTVKDVTFKNITGTSSTPEAVSLLCTAKVPCTGVTMDDVNVEYSGTNNKTMAICTNAKGSTKGCLKELACF | Function: May function in depolymerizing pectin during pollen development, germination, and tube growth. Acts as an exo-polygalacturonase.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-galacturonosyl](n-1) + alpha-D-galacturonate
Sequence Mass (Da): 43444
Sequence Length: 410
Subcellular Location: Secreted
EC: 3.2.1.67
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Q9P931 | MSVQTVSIQPFGDQKPGTSGLRKKVKIFQQENYTESFLTSIFLSIPEGAQDAFLVIGGDGRYYNSDVIQKIAKIGAAYGVKKLIVGQNGILSTPAASNLIRKRKATGGILLTASHNPGGPDNDFGIKYNLTNGAPAPEQVTNKIYEVSKSLTSYKYIDLPEVDTTTVGTRSYGPLEVEVVHSTEDYVSMMKEIFDFDLIRSFLKKHPDFKVLFDGMHGVTGPYGIDIFVNELGLPSSSTMNCIPKPDFGGGHPDPNLVYAHELVEAVDKNGIHFGAASDGDGDRNMIYGANTFVSPGDSLAIIAHHAKLIPWFQKHGVDGLARSMPTSGAVDRVAKAQGLQSYEVPTGWKFFCNLFDNKKMSICGEESFGTGSNHIREKDGVWAIVAWLNVIAGVAEQKPNETPSIASIQAEFWETYGRTFFTRYDYENVDSDGANKLIAALSEKAVDNKSSFVGSTISGRKVVDSGNFAYTDLDGSVTKNQGLYVKFDDGSRLVVRLSGTGSSGATIRLYVEKYEGDKSKYQMATQDYLKDNVGLALELLKFKEFVGREEPDVKT | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible interconversion of glucose 1-phosphate and glucose 6-phosphate . Key enzyme in hexose metabolism. The reverse reaction is an essential step for biosynthesis because glucose 1-phosphate is the starting point for the synthesis of UDP-glucose, which acts as a precursor for the synthesis of oligosaccharides and trehalose (By similarity).
Catalytic Activity: alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate
Sequence Mass (Da): 60684
Sequence Length: 556
Subcellular Location: Cytoplasm
EC: 5.4.2.2
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O15820 | MQATIKRYPTSPISGQTLGTSGLRKRASEVENTPNYLENFVNAMFNAASNLQKPGKIIIGGDGRYLNLKALDIIIRVALSRGFTDIVVGKSGFMSTPAESATIIRRKAEAGFIMTASHNPAGKEHGDFGLKLNMSNGGPAPIEVTSKIEESARNIKEIVIAELNKPLNIDSVGDIEIECEGKKAVVHVIDPLEDYIAYLHECFDFENLKQFVSKYHLKVQVDGFNAVTGIYNKKVFCELLGLPESSLKNAIPMPDFGGKHPDPNLTYAAELVHAVIPEDSPYDIGFAFDGDGDRNLIVGRGAFVSPSDSLAILSTKYNDIPFFVKNGFKGVARSMPTSAAVDHVTSITETPTGWKFFGNLMDSGKISLCGEESFGTGCCGIREKDGIWAALCWVSILAAESERAQRLVGVKEILESHWAKYGRNYYQRYDFDEVDKKAAEDMMQMMRDNAKTVKCDLNGVPLKFCDDFEYHDSVDGSVTSKQGIRFVFEDGSRIIFRLSGTGSVGATIRVYFDKYSKDYKADQTKVLADMVTVAYAVSQITKFTGREKPSVVT | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible conversion of glucose 1-phosphate into glucose 6-phosphate . This enzyme participates in both the breakdown and synthesis of glucose .
Catalytic Activity: alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate
Sequence Mass (Da): 60788
Sequence Length: 553
Subcellular Location: Cytoplasm
EC: 5.4.2.2
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P40391 | MASIARDIFKAYDIRGIVGKTLTDEAAYLIGKAIAAKAAEKGITRIALGRDGRLSGPELMEHIRRGFTDSGINVLNVGMVATPMLYFAAVNECGGSGVMITGSHNPPDYNGFKMMLGGDTLAGEAIQELLSIIEKDGFAAAGKQGSVTEKDISGEYLKHITGHIRLKRPMNIAIDAGNGVGGAFAGKLYKGLGNKVTELFCDVDGTFPNHHPDPSKPKNLQDLIAALKNGDAEIGLAFDGDADRLGVVTKDGNIIYPDRQLMLFAQDVLNRNPGAKVIFDVKSTRLLAPWIKEHGGKAIMEKTGHSFIKSAMKETGAPVAGEMSGHIFFKERWFGFDDGLYAGARLLEILSASDNPSEVLNNLPQSISTPELNIALPEGSNGHQVIDELAAKAEFEGATEIITIDGLRVEFPDGFGLMRASNTTPILVLRFEADTQEAIERIQNQFKAVIESNPNLIWPL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: This enzyme participates in both the breakdown and synthesis of glucose.
Catalytic Activity: alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate
Sequence Mass (Da): 49476
Sequence Length: 460
Subcellular Location: Cytoplasm
EC: 5.4.2.2
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O74374 | MIETIPTKPYEGQRPGTSGLRKKVTVFEQPNYVENFVQATMDVVEPSAKGAHLVVGGDGRYFNFHAIQVIAAIAAGNGVEKIIVGTNGYLSTPAASHIIRKYKLTGGIILTASHNAGGPKNDFGIKYNLGNGGPAPESVTEKIYSITKTISEYKMVKIPPLDLTTTGVRRYGPLTVEVIDPVKDYVQLMKEIFDFDLIRSFLSKNPDFTFVFDALHGITGPYGEALFCKELGMPSSVCQNCKPLPDFGGGHPDPNLTYAKSLVARVDRDNIVMGAASDGDGDRNMIYGANAFVTPSDSVAIIAHHAELIPYFRDGGVHGFARSMPTSGAIDRVGKYKGKNVYEVPTGWKFFCNLFDAKRLSICGEESFGTGSDHIREKDGVWGILCWLNILAGLNAQNPKIKTLIDVKKDFYNIYGRTFYSRYDYEELENEAAGKVMDRMRAIADDKSKVGEAVLPGFVVSEAGDFEYHDPIDGSESKHQGLYIKFENGSRIVTRLSGTGSSGATLRLYMEKHESDSSKFDLDAQVALKPVVHAALEILALEELTGRKEPTVIT | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible interconversion of glucose 1-phosphate and glucose 6-phosphate. Key enzyme in hexose metabolism. The reverse reaction is an essential step for biosynthesis because glucose 1-phosphate is the starting point for the synthesis of UDP-glucose, which acts as a precursor for the synthesis of oligosaccharides and trehalose.
Catalytic Activity: alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate
Sequence Mass (Da): 60599
Sequence Length: 554
Subcellular Location: Cytoplasm
EC: 5.4.2.2
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P56601 | MHHMPRTTGMNVAVVGGGISGLAVAHHLRSRGTDAVLLESSARLGGAVGTHALAGYLVEQGPNSFLDREPATRALAAALNLEGRIRAADPAAKRRYVYTRGRLRSVPASPPAFLASDILPLGARLRVAGELFSRRAPEGVDESLAAFGRRHLGHRATQVLLDAVQTGIYAGDVEQLSVAATFPMLVKMEREHRSLILGAIRAQKAQRQAALPAGTAPKLSGALSTFDGGLQVLIDALAASLGDAAHVGARVEGLAREDGGWRLIIEEHGRRAELSVAQVVLAAPAHATAKLLRPLDDALAALVAGIAYAPIAVVHLGFDAGTLPAPDGFGFLVPAEEQRRMLGAIHASTTFPFRAEGGRVLYSCMVGGARQPGLVEQDEDALAALAREELKALAGVTARPSFTRVFRWPLGIPQYNLGHLERVAAIDAALQRLPGLHLIGNAYKGVGLNDCIRNAAQLADALVAGNTSHAP | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX . Does not oxidize coproporphyrinogen III . Involved in the classical protoporphyrin-dependent (PPD) heme b biosynthesis .
Catalytic Activity: 3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX
Sequence Mass (Da): 49388
Sequence Length: 471
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.3.4
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P0DKC3 | MLSRSVASAVTPVSSSSLLPNSKPIFCLKTLSGYRSSSFCGGCIRKINHKPLRMTSSNITPRAMATQQLENADQLIDSVETFIFDCDGVIWKGDKLIEGVPETLDMLRAKGKRLVFVTNNSTKSRKQYGKKFETLGLNVNEEEIFASSFAAAAYLQSINFPKDKKVYVIGEEGILKELELAGFQYLGGPDDGKRQIELKPGFLMEHDHDVGAVVVGFDRYFNYYKIQYGTLCIRENPGCLFIATNRDAVTHLTDAQEWAGGGSMVGALVGSTQREPLVVGKPSTFMMDYLADKFGIQKSQICMVGDRLDTDILFGQNGGCKTLLVLSGVTSISMLESPENKIQPDFYTSKISDFLSPKAATV | Function: Photorespiratory enzyme that dephosphorylates the 2-phosphoglycolate produced by the RuBisCO oxygenation reaction.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 39762
Sequence Length: 362
Subcellular Location: Plastid
EC: 3.1.3.18
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P95967 | MIKLVLVDLDGTLTEDRESTRIDLDAIYAIRLLQKSGIKVSLVSGNSYPILRGLYTYLYLDGGFVAENGCIVFYKEKYRMCRQMEQSLVDEFKSLFKLRDTWQNEYRECDFGFVPAKITDEMINWAKERNLYIKSSGYAVHIAYNPAGKRIGVEKLLQLLGLKKEDVAAIGDSSTDIELFQQVGFKVAVGNADDELKDIADYITSNKSGKGVREFVDKLLKGEFDGIK | Function: Catalyzes the dephosphorylation of 2-phosphoglycolate.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 25843
Sequence Length: 228
EC: 3.1.3.18
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Q8GWU0 | MAPQLLSSSNFKSLFDSVDTFLFDCDGVIWKGETLIDGVSQTLDLIRSKGKNVVFVTNNSVKSRRQYAEKFRSLGVTSITQDEIFSSSFAAAMYLKVNNFPKDKKVYVIGGEGVLEELQIAGFTGLGGPEDGEKKAQWKSNSLFEHDKSVGAVVVGLDPNINYYKLQYGTLCVRENPGCLFIATNRDAVGHMTDLQEWPGAGCMVAAMCGSTEREPIVVGKPSTFMMDFLLQKFGTETSRMCMVGDRLDTDILFGQNAGCKTLLVLTGVTSESNLLDKGNKIEPDYYTSTVSDIIKLMESP | Function: Dephosphorylates 2-phosphoglycolate, but does not contribute to photorespiratory metabolism.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 33012
Sequence Length: 301
EC: 3.1.3.18
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P95931 | MDIGSNEILVASDYDRTLASEENNFVISPIVSQKVNEFSKKYKFVVVTGREKKFIDKLAVGLKPTAWILENGSLILFNDREFVLCEKSWFERDRKKIIEILDNLKVRYSIGRIILYVDGYGSKLDMLSEIEKYGRIEVNRNDAMILPKGVDKGVGVLKFKELTGFKGKIIALGDSENDYALFRVADIKVAVANAIPQIKEIADIVTENPNGLGVVEILDKILSGNFGKEVDIY | Function: Catalyzes the dephosphorylation of 2-phosphoglycolate.
Catalytic Activity: 2-phosphoglycolate + H2O = glycolate + phosphate
Sequence Mass (Da): 26215
Sequence Length: 233
EC: 3.1.3.18
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P18200 | MTILPRHKDVAKSRLKMSNPWHLLAVGFGSGLSPIVPGTMGSLAAIPFWYLMTFLPWQLYSLVVMLGICIGVYLCHQTAKDMGVHDHGSIVWDEFIGMWITLMALPTNDWQWVAAGFVIFRILDMWKPWPIRWFDRNVHGGMGIMIDDIVAGVISAGILYFIGHHWPLGILS | Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19418
Sequence Length: 172
Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell inner membrane
EC: 3.1.3.27
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P44157 | MTENNPLKKISLLNPIHLLAVGFGSGLIHPAPGTWGSLAGTILGVILLSLLGVKIFLIFTALCFLLGCYLCQKTTADMGVHDHGSIVWDEFVGVFIVLAAIPSLSWQWILAAFALFRFFDILKPFPIRYFDEKLENGFGIMIDDVLAAIYAVIVVFAIQYWML | Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18035
Sequence Length: 163
Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell inner membrane
EC: 3.1.3.27
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Q5HGE8 | MNIPNQITVFRVVLIPVFILFALVDFGFGNVSFLGGYEIRIELLISGFIFILASLSDFVDGYLARKWNLVTNMGKFLDPLADKLLVASALIVLVQLGLTNSVVAIIIIAREFAVTGLRLLQIEQGFVSAAGQLGKIKTAVTMVAITWLLLGDPLATLIGLSLGQILLYIGVIFTILSGIEYFYKGRDVFKQK | Function: This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21014
Sequence Length: 192
Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Subcellular Location: Cell membrane
EC: 2.7.8.5
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Q5HPQ8 | MNIPNQITVFRVILIPFFILFALVDFGFGQISILGGNHIRIEILISAIIFVVASLSDFADGYLARKWQLVTNMGKFLDPLADKLLVASALIVMVQLGFTNSVVAIIIIAREFAVTGLRLLQIEQGFVSAAGQLGKIKTAVTMVAIIWILLGDPFVHYLRFPIGVWLLYIGVFFTILSGIEYFYKGRDVFKHSK | Function: This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21497
Sequence Length: 193
Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Subcellular Location: Cell membrane
EC: 2.7.8.5
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O66076 | MRLSDFYTALRLALVLPFFALYHMSRWVVMYFPAANVGRVVSIASVLLFLFIACTDFLDGYYARKSGKYSSFGKVFDPFADVIANVTVMLCLVADNFMPVFLFLCILYREFGMMFLRMLACGEGHVVGAQRMGKLKTASYMGAVLFSLLLKALYAFELAGADWYERMRAVGRLVYVVPVVLALASFFSYLKTFFPILKRVCGRTRYPVCKTCREWD | Function: This protein catalyzes the committed step to the synthesis of the acidic phospholipids.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24639
Sequence Length: 216
Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Subcellular Location: Cell membrane
EC: 2.7.8.5
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P73390 | MFLLFFIVHWLKIMLPFFAQVGLEENLHETLDFTEKFLSGLENLQGLNEDDIQVGFTPKEAVYQEDKVILYRFQPVVENPLPIPVLIVYALVNRPYMVDLQEGRSLVANLLKLGLDVYLIDWGYPSRGDRWLTLEDYLSGYLNNCVDIICQRSQQEKITLLGVCQGGTFSLCYASLFPDKVKNLVVMVAPVDFEQPGTLLNARGGCTLGAEAVDIDLMVDAMGNIPGDYLNLEFLMLKPLQLGYQKYLDVPDIMGDEAKLLNFLRMEKWIFDSPDQAGETYRQFLKDFYQQNKLIKGEVMIGDRLVDLHNLTMPILNLYAEKDHLVAPASSLALGDYLPENCDYTVQSFPVGHIGMYVSGKVQRDLPPAIAHWLSERQ | Function: When expressed in E.coli with Synechocystis PhaE and C.necator PhaA and PhaB, confers the ability to synthesize up to 13% (w/w) poly(3-hydroxybutyrate) (PHB) depending on the carbon source; all 4 genes are necessary for PHB production . Cell-free in vitro coexpression with PhaE gives a heterodimer able to polymerize 3-hydroxybutyrate-CoA .
Catalytic Activity: (3R)-3-hydroxybutanoyl-CoA + [(3R)-hydroxybutanoate](n) = [(3R)-hydroxybutanoate](n+1) + CoA
Sequence Mass (Da): 42961
Sequence Length: 378
Pathway: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.3.1.-
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Q52981 | MTDWLDHLLILPILLPLAVAAVLIPINERDRTLKGAIGFASTLVVFILSMILMRLAAAGTGSLPGSGVYQLGNWPAPFGIVLVLDRLSALMLCLTSGLALAAQAYSMARWHTAGHHFHSLFQLLVAGLNGAFLTGDLFNLFVFFEMMLAASYGLLLHGSGPLRVKAGLHYIAVNLAASALFLIGVSLIYGAAGTLNMADLATKLAALEPRSRTLVEMGSAILGVAFLVKAGMWPLSFWLPTAYAAATPPVAGVFAVLTKVGIYVIIRLHLLVFGTAAGASSGFGQEWLVTGGMLTIAFGGIGVLASQAMGRLAGYSVLVSSGTLLAAVGLGHDGMLAGALFYLVSSTLTIGAFFLLIELVERGRDAGADVLAVTMEAYGDFDEDEEEEEVGAAIPGTMAVLGLCFCLCALLLAGLPPLSGFIAKFALISGLFDMPAAELATAMSAADWTYVTLLILSGLAAMIAMNRIGIRTFWASIEGTIPRVVVIEITPVVVLLGACIFLSLQAGPAMRYMQATADDLLAPLTHSERVLSAPRAGSQ | Function: Part of a K(+) efflux system which is required for the adaptation of R.meliloti to alkaline pH as well as for the infection process during symbiotic nodule development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56303
Sequence Length: 539
Subcellular Location: Cell membrane
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P45372 | MSNTNFFNDDWLELQRKYWDNWTDMSRKAMGLDSASSSATTPWEAAIDQWWKAMAPAAPDLSRSFMEKMMEQGKNFFRLADTFAKRADEGNAGNGLELWTKTLEDMQKRFSGSLDDGGNTMQRLMSFWELPLDNWQRMMSSMSPMPGDMLRNMPHEQFKDSLDRALSAPGLGYTREEQSQYQELMRSAMEYQAALQEYTNVYTKLGMKSVEHMGSYIQGVIDSGKTIDSARALYDNWVACCEGAYADEVATPEYARIHGRLVNAQMALKKRMSILVDENLGALNMPTRSELRTLQDRLQETRRENKALRHSLHSLERRVAALAGEEPATKPATALRSPAPAAKAPARRRTTKTNPAD | Function: Polymerizes D(-)-3-hydroxybutyryl-CoA to create polyhydroxybutyrate (PHB) which consists of thousands of hydroxybutyrate molecules linked end to end . This subunit has no catalytic activity but enhances the activity of PhaC, the catalytic subunit, 100-fold .
Sequence Mass (Da): 40524
Sequence Length: 357
Pathway: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate biosynthesis.
Subcellular Location: Cytoplasm
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G0HQZ5 | MSNTNNIQEEWTEMVEEMNNAVADSMEQNMKAQAAFVESWADAVEDTIPKEEDLADGMDGYNRAYEEWIDAAEQMVERSTDAAQGEDVDPAEFRDIWLQSANEAFKHVMGTSAFAAANGQLVESMMEMQQEADDLSQDALEQMGFPTRNDVDEVAERLIELERRQHAVEQKLDRVLEHLEE | Function: Involved in the production of polyhydroxyalkonic acids (PHAs), which are water-insoluble biopolymers used as intracellular energy reserve material when cells grow under conditions of nutrient limitation. PHAs are composed primarily of 3-hydroxybutyric acid (3HB) and 3-hydroxyvaleric acid (3HV). Required for the production of poly-beta-hydroxybutyrate (PHB) and poly(beta-hydroxybutyrate-co-beta-hydroxyvalerate) (PHBV).
Sequence Mass (Da): 20610
Sequence Length: 181
Pathway: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate biosynthesis.
EC: 2.3.1.-
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Q52982 | MRTWFPYPLLSIALLLMWLLLSQSVTPGSIVLGLVVSTVLAWVTLNLQPARSRLHRWSRIAGFILRVVGDVIRSNIAVTLIILRAGRRPVNAGFMTVSLDLDDENALALLACVVTATPGTAWLEYDRRQKILLFHVLDIENEDLWRKTITRYAADLKEIFE | Function: Part of a K(+) efflux system which is required for the adaptation of R.meliloti to alkaline pH as well as for the infection process during symbiotic nodule development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18240
Sequence Length: 161
Subcellular Location: Cell membrane
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P73389 | MESTNKTWTELMTPLSQFWLESSSQAWKNWFDLMAKGGAGAMMGSAPQSFESLPQQFLQSQQFYGELLKLSFEAWQSLWPKLDNGSAPGAVQGYLKQLQTQIEQYTATTQALQGDMDGLWQCYIKEVQRFSQLWLSTWQSSVAPLGKLPTGDIHAWLDLNNLYGDALYNKNLSSFMRSPLLGPSREMNGKLLRAFDDWVKLSQAMADYQLLEADIQYRGFAALMEDLLARAKEDKPVKTWKEFQQRWAIAADQVFEEAFCEEKNLKVRGKFINALNRYRIQQQEILEAWLKMLNLPTRSEVDEIHQTIYQLRKEVKSLKKRLGETEANPG | Function: When expressed in E.coli with Synechocystis PhaC and C.necator PhaA and PhaB, confers the ability to synthesize up to 13% (w/w) poly(3-hydroxybutyrate) (PHB) depending on the carbon source; all 4 genes are necessary for PHB production . Cell-free in vitro coexpression with PhaE gives a heterodimer able to polymerize 3-hydroxybutyrate-CoA . This subunit has no catalytic activity but enhances the activity of PhaC, the catalytic subunit (By similarity).
Sequence Mass (Da): 38047
Sequence Length: 330
Pathway: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate biosynthesis.
Subcellular Location: Cytoplasm
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P45367 | MSNDSFFNNDWLELQRKYWDSWSEMGRKAMGLENQQTLTTPWEGALDHWWKAMSPATPDFSKTFMEKMMEQGKNFFRMAETFANTPEDTTATNGLTWWTKALEDMQKQFSGSLDDGGNSMQRMMSFWELPIDNWQRMMSSMSPMPGDMLRNMPHEQLKDRSGRALSAPGLGYTREEQSQYHQLTRTAMDYQAALQEYTGFYSQLGMKSVERMGDFIQGVIDSGKSIDSARTLYDNWISCCETVYAAEVATPEYAQIHGRLVNAQMALKRRMAIMVDENLGAMNMPTRSELRTLQDRLQETRRDNKQLHRALHALEKQVAALSGKTPTTALKAPAPATKATEKPATRATTRRKTAAKPTGGTADD | Function: Polymerizes D(-)-3-hydroxybutyryl-CoA to create polyhydroxybutyrate (PHB) which consists of thousands of hydroxybutyrate molecules linked end to end. This subunit has no catalytic activity but enhances the activity of PhaC, the catalytic subunit.
Sequence Mass (Da): 41387
Sequence Length: 364
Pathway: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate biosynthesis.
Subcellular Location: Cytoplasm
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A0A1S4H2E2 | MHSPGAAAYVFLQCLVALVAAVIAQSGADQPPTTVVEVTAHGSVSMTPPTPRSPLLNETELVELNQPGSTAVFVALPTNPPTVSVDSSSTTTVASTQEPTSTTERTMSPEEIQKLLLPPATVEADILHVNATDDNRPDAKSSGKDSECPTLEGADHLSQTQLLTRLTHVCRYDRLERPKRESINGTNGPVKVYARAYIYFMQNLEAHDLQFKIHALLQFRYVDPRLVFREVAPNRTKPIMGEQSLRDLLWVPHVFLANERSSDILGTAEKDILTSISPDGTVIVSTRISATLYCWMNLQKFPFDEQHCSTVLESWMYNEDDLVLLWEHKSPVTLAPELHLTEYVLLEMFTNETVINADLSDLRHGAFAGNYSSLSFTVHLAREMGFYMMDYFIPSIMLVAISWVTFWLQADQSAPRITLGTSTMLTFITLASAQGKTLPKVSYIKASEIWFLGCTGFIFGSLVEFAFVNTIWRRKRNVEVKKVNSKHVLKQAITPRPARKDMSGLHKSHSCTSLADSATTVSANSFNNYLTVHSIPQKSPSSATLPIISTTDVDRAMTEASNVTIQIEGQTSNVNGNGWTTMTPQEVAIWIDKRSRFVFPIAFVIFNIFYWTFVYYV | Function: Ligand and pH-gated channel that mediates chloride transport in the mid-gut and thereby may function in larval metabolism and fluid homeostasis. Channel opening is triggered by zinc binding or, to a lesser extent, an increase in extracellular pH.
Catalytic Activity: chloride(in) = chloride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68733
Sequence Length: 617
Subcellular Location: Cell membrane
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Q9V9Y4 | MDTLGIFVLISYLGLSSAAGVHLGDLQQNLAANGSVVVSPLNTTDAFSVSINLSQSTVNNCPSLKNAESMALMELLTRLTAPCRYDRMVPPVVHNKDGEEVPMDIYARFYIYVMKNLDSSDLQFTVQGLLQLRYLDPRLAFSSYLPNRRQPIMGESELKKMLWVPHIFLTNEQASTVLGTSAKDELTSIYPNGTVLTSTRLQATLYCWMNFQKFPFDEQKCKTTLESWMYNTTLVQLHWETDNPVSFDKQLQLTEYNLIGSLYNESIRVSNESYMSHGSLEGNYSIISFTVLLTREVGYYVIDYFLPSIMIVTISWVSFWLQADQTPARTTLGCTTLLSFITLSLSQENNLMKVSYVTMSEVWFLVCTIFIFGSLVEFAFVNTIWRRNNDLQLKKRTTKYIVKSTFVPHLKKHRRHGYRRTDSTMSTMSTTSMDKTCGPNNTVITIETPIIIGGSLSREDSAISLDEQDETSTSESSDSSKEKPAQTFATMTPKEVSLWIDRKMRFVFPLSFIVFNALFWTLVYCL | Function: Ligand and pH-gated channel that mediates chloride transport primarily in the mid-gut and thereby functions in larval metabolism and fluid homeostasis . Channel opening is triggered by zinc binding or, to a lesser extent, an increase in extracellular pH . Zinc-dependent activity in the mid-gut is required for modulating Tor-dependent metabolic programs that promote larval feeding and systematic growth . It may therefore act as an intestinal zinc sensor that mediates larval growth and metabolism in response to micronutrient availability . Activates Tor signaling via its activity in maintaining lysosome homeostasis in interstitial cells and/or by its role in activating the release of insulin-like peptides in the brain after feeding, via an unknown mechanism . Functions in lysosome homeostasis by regulating chloride transport into enterocyte lysosomes to sustain V-ATPase function which maintains lysosomal acidification and consequently promotes Tor activation at the lysosome membrane . Also appears to play a role in regulating fluid secretion and osmotic homeostasis in Malpighian tubules in response to the pH of extracellular urine . This function is important for proper urine production during diuresis .
Catalytic Activity: chloride(in) = chloride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59826
Sequence Length: 526
Subcellular Location: Apical cell membrane
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O24721 | MNSSNTGAPEAAQAATLEAFDRRAAEQYLRGQWIAEEHLMRAIGGPRPAGIPYRWEWKSVEVALDEATIALGPVDTARRHLTFVNPGLMDRGSATTHTISAGFQLVKPGEVCWSHRHTMSAVRFVTKGHPDAFTAVDGERLPMEDFDLLITPRFSWHDHHNSGDADVVWLDGLDIGLLQSLGAVFYEPYGDDSQNVRPSSSEGIGTRSHWLRPTWERGRESRLPIRYPWKEVNARLDVYDLDAGTPYDGLALRYANPVTGGPTMATMDCWVQRLAPGFDGKSHRRSSSAITYVISGSGTMVTEDETITFNRGDVISLPNWTNFRWTNDSEIEPVLLFSMHDIPALEAFGLLYEEPEAILNATPAPINPTPSLNPIYRPGAFYDQDEL | Function: Dioxygenase involved in phenanthrene catabolism by mediating cleavage of 1-hydroxy-2-naphthoate.
Catalytic Activity: 1-hydroxy-2-naphthoate + O2 = (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate + H(+)
Sequence Mass (Da): 43082
Sequence Length: 387
EC: 1.13.11.38
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Q79EM8 | MTSPAVTSADITGLVGIVPTPSKPGSEAPDAVDTVDLDETARMVELIVASGVDVLLTNGTFGEVATLTYEELLAFNDTVIRTVANRIPVFCGASTLNTRDTIARSLALMGLGANGLFVGRPMWLPLDDEQLVSYYAAVCDAVPAAAVVVYDNTGVFKGKISSAAYAALAEIPQIVASKHLGVLSGSDAYASDLAAVKGRFPLLPTADNWLPSLEAFPGEVPAAWSGDVACGPEPVMALRRAIAEGLWDDARAVHEDIAWATEPLFPGGDISKFMPYSIQIDRAEFEAAGYIVPGPSRHPYGTAPAAYLEGGAEVGRRWAGIRQKYVATLAEP | Function: Plays a role in phenanthrene catabolism. Catalyzes the transformation of trans-2'-carboxbenzalpyruvate to 2-formylbenzoate and pyruvate.
Catalytic Activity: (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate + H2O = 2-formylbenzoate + pyruvate
Sequence Mass (Da): 34881
Sequence Length: 332
EC: 4.1.2.34
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Q79EM7 | MTTPRKFDEYRWNVLVDGVPLNVESRYPISDPSTGRYLTQVPDCAEADVDRAVQASRQAQAEWGALPPRARAAKLRELITLLREHREEFAMLDAIDGGFPISMMRNDVDAALELMDIFADMALDLGGKTIPVSTNLHFTTHEPFGVVARIGAFNHPFFFAASKVAAPLMAGNSVILKAPDQTPLSSLRLAEVAAEVLPQNLLITISGRGRVAGRAIVRHPQIKRIGFIGSTDTGRSIQRDAAEVAVKHISLELGGKNAQIVFADADLEQAALGAVNGMNFTWTAGQSCGSTSRLLVHESVADQVIARVVELVSAIAVGPPLDENAQMGPLVSQAQYDKSVHAIGEGIREGAKVVAGGGRPEGVGEGGWYLAPTVLADVRPGSFIEQNEIFGPVLSVIIFATDDEAVAIANGVEYGLTASVWTSDITRAHLIARRVEAGYVLVNGGSRHYWGLPFGGVKSSGVGSEESMEELISYTETKTTTVVLG | Function: Plays a role in phenanthrene catabolism by catalyzing the oxidation of 2-carboxybenzaldehyde to phthalic acid. Not active with 3-carboxybenzaldehyde, 4-carboxybenzaldehyde, benzaldehyde, salicylaldehyde, 2-methylbenzaldehyde, 2-chlorobenzaldehyde, 2-fluorobenzaldehyde, 2-benzaldehydesulfonate, 2-methoxybenzaldehyde, 1-hydroxy-2-naphthoaldehyde or n-hexylaldehyde.
Catalytic Activity: 2-formylbenzoate + H2O + NAD(+) = 2 H(+) + NADH + phthalate
Sequence Mass (Da): 51806
Sequence Length: 485
EC: 1.2.1.78
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Q8IWS0 | MSSSVEQKKGPTRQRKCGFCKSNRDKECGQLLISENQKVAAHHKCMLFSSALVSSHSDNESLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYHCALHDKAQIREKPSQGIYMVYCRKHKKTAHNSEADLEESFNEHELEPSSPKSKKKSRKGRPRKTNFKGLSEDTRSTSSHGTDEMESSSYRDRSPHRSSPSDTRPKCGFCHVGEEENEARGKLHIFNAKKAAAHYKCMLFSSGTVQLTTTSRAEFGDFDIKTVLQEIKRGKRMKCTLCSQPGATIGCEIKACVKTYHYHCGVQDKAKYIENMSRGIYKLYCKNHSGNDERDEEDEERESKSRGKVEIDQQQLTQQQLNGN | Function: Transcriptional regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription.
Sequence Mass (Da): 41290
Sequence Length: 365
Domain: The PHD-type zinc finger 1 mediates both nucleolar localization and interaction with UBTF.
Subcellular Location: Nucleus
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Q4L9P7 | MSQIEFKDVNKVYPNGHVGLKDINLNIEKGDFAVIVGLSGAGKSTLLRSVNRLHDITSGDILIEGKSITKAKGNDLLMMRRNIGMIFQHFNLVKRSSVLRNVLSGRVGYHPTWKMVLGLFPKEDKVKAMDALERVNILDKYDQRSDELSGGQQQRISIARALAQEPAIILADEPVASLDPLTTKQVMDDLKKINEELGITILINLHFVDLALEYGTRIIGLRAGELVFDGPASEATEEVFNDIYGRKLKDDEKLGVE | Function: Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphonate(out) = ADP + H(+) + phosphate + phosphonate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28568
Sequence Length: 257
Subcellular Location: Cell membrane
EC: 7.3.2.2
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Q49XC6 | MSQIEFKDVRKVYSNGHVGLDRINLNIEKGDFAVIVGLSGSGKSTLLRSINRLHDITEGEILIDGKSMTKASGNQLLEMRRNIGMIFQNFNLVKRSSVMRNVLSGRVGYHPTWKMVLGLFPKEDKIKALEALDRVNILDKYKSRSDELSGGQQQRISIARALCQEPAIILADEPVASLDPLTTKQVMDDLKRINQELGITIIINLHFVDLAREYGTRIIGLRDGQLVFDGPVERATDEAFNEIYGRSIQDEEKLGVN | Function: Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphonate(out) = ADP + H(+) + phosphate + phosphonate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28823
Sequence Length: 257
Subcellular Location: Cell membrane
EC: 7.3.2.2
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Q3SGJ8 | MSAISIQSVTKRFPNGFEALKGIDTEIQTGSFTVVLGPSGAGKSTLLRLMNGLETPTTGAVRIDGETVDGHRLRHIRSKVAMVFQQFNLVERLSVVTNVLTGRLAQRSWVGSVFYLFRQEDLGIAREALARVGLTDKAWSRADKLSGGQQQRVGIARALAQRPKVILADEPVASLDPVSSEEIMALLREICDRDGITVVVNLHQVDLAKRFADRIIGMNAGRVVFDGTPAELSAQALRTIYQREGIEDDTSLDLALAYA | Function: Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphonate(out) = ADP + H(+) + phosphate + phosphonate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28231
Sequence Length: 259
Subcellular Location: Cell inner membrane
EC: 7.3.2.2
|
Q73P71 | MILELKNISKTYPSGRRALQSISFKIEEGEILAIIGLSGAGKSTMLRCINRLVEPDEGEVIFLGEKINKLKGKKLRQYRSKIGMIFQNYNLVERLNAVENVLHGCLGSIPSYRGALGLYTEEEKEKAFALLQTVGMEEFAFQRCSELSGGQKQRIGIARALMQSPKLLLCDEPIASLDPQSSETVLNYIKEFAVNKNIACLISLHQMEAAKKYADRIIALNNGKIVFDGIPDSLNDEVLHKEIFTNVSIDSGEKSL | Function: Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphonate(out) = ADP + H(+) + phosphate + phosphonate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28468
Sequence Length: 256
Subcellular Location: Cell inner membrane
EC: 7.3.2.2
|
Q1C9L0 | MGQALRKLTAADYPVVVQEPRKKVLAVKGLVKAYKSQHRVLDNINFELHAGEFVAIIGRSGAGKSTLLHILNGTIPTSAGEIINYHENGDTQNIAALTTKQMRKWRAKCGMIFQDFCLVPRLDVITNVLLGRLSYTSTLKSFFKLFSEQDQARAIELLQWLNMLPHALQRAENLSGGQMQRVAICRAMMQNPKILLADEPVASLDPKNTTRIMNTLQKISENDIAVIVNLHSVDLVKDYCTRVIGIAHGRIIFDGPPSMLNDSIIQDIYSDESAELLH | Function: Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + phosphonate(out) = ADP + H(+) + phosphate + phosphonate(in)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30989
Sequence Length: 278
Subcellular Location: Cell inner membrane
EC: 7.3.2.2
|
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