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A0A6S7FF74 | MTQNKLYTLAFVLDAGRILLGMKKRGFGAGRWNGFGGKVDPGESIEAAAKRELFEECNLTAKNLGHVGILKFEFVGEPRIMEVHVFKTSSYEGSVQESEEMRPQWFQTDQIPFPDMWPDDDLWFPMLLNNEKFEGYFKFEGHDKILDYTLKKL | Catalytic Activity: 2-oxo-ATP + H2O = 2-oxo-AMP + diphosphate + H(+)
EC: 3.6.1.56
Subcellular Location: Nucleus
Sequence Length: 153
Sequence Mass (Da): 17677
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A0A6G2K0D4 | MEIAVFAVCAVIVIGGALGVIVARHPVYAALSLVATLFGVAVLFLTLDAPFLAAVQVIVYAGAIVVLFLFVIMLLGVDRAENLRTEPLGGQRPLAVGLGVATLVLALLFAIAVGTGGFGDGSVATGAPAAVAPERDSCTGLSKALEDSSPLVAACDGTEPISNIRQVARWVFTDYVWAFQLTGLLLTVAVVGAVVLARGRRGADGDDEAAGPAPDTAPEAV | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 221
Sequence Mass (Da): 22394
Location Topology: Multi-pass membrane protein
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A0A6S7JVE1 | MQAQIGYDIMAEDTITDLVHNNRKLLEKHITATEIETFVSLVRLKRECRFLVYLSDLCVSNNTAIPATQELIYKSVLESSSNSDLLIKTRVIDDVVHVEWCTDNGTVQKSQHELADGFKRGDRQDVEIMNFYRHQLDLFAYMCFDRQYLAINRLSEQLDVDLVQRCMADEELPCELRAAFCRLMLHMHIDRDPQEPITPVRYARLWSEIPLQLSIDDYDKQDIFGKKNRAKFTKTVDFVEAYLRQISSNIWAFNNKEQNKLTYEVVQIARHLIYFGFYGLNDLIKLTMKLLAILDGEQRAYDRANAVKKKTAMTSKRDVSRSVSTIGTLMTRMVLPGAKDPWGLIMSSDKMSNLKCSDIEKDRIVMETKVKIIEILEFILNVRLDYRISSLLTIFKREFDVKNGSAVGSEGIDLERVGIQAEQLFGGSGTSIVGAKITHDLDFDGTGGCTFLRVLLSLIIHDYPQLVVGALKLLLKHFSQRQEVLHAFKQVQLLVTAKDVENYKTIKDSLDELRLLVEKSELWVFKAKKKSDGKKGESNRKKSNAKDQSKMDGKSLESFSESVDLQTYRSRLASEESQNEDNANEDTSLLTNYQTIKKILEHLCELCVTVTHGKKKNNKHEQRLLRNMGAHTVVVELLQIPYEKKKDIYMKDVMTLAHEFLQLFCLTNKHNQAILYKHLDLFLVPGLQEAHTLQHIFQDNLSLCNEVPDKVIHHLVRAIETEGRQVQYLKTLQTLVKAENQAVRKCQDFIMVEFLNAGEEVLLFFNERKMQEPFFELMRSETDNLSESSSIAYHIHLVKLLATCTEGKNANTEIKCHSLLSLDDILRVVTHPDCMSEVKDAYIYFLIHCYVDTEVEMKEVYTSHHIWALFDNFLLDMARVR | Function: Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 881
Domain: The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has the ligand-binding site in the N-terminus and modulatory sites in the middle portion immediately upstream of the channel region.
Sequence Mass (Da): 101648
Location Topology: Multi-pass membrane protein
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A0A7D9HPR0 | MPALYRDPLVDNVGVWGIPTSTLDWCEENYAVTRYVAEFWNTITNYFMVVPPLLAALRCHQLGLDTRFLLSFLSFMGIGVGSTLFHATLQYKMQLLDELPMIYCTYIMLYCVLACDNEPRKKNVGLKLFLTVCNILVTVVYVVFVNPLIFQWVYGLSVAVLIISTVHSARYHRFIYISFLDLYCTPNLVLMHTSYFLIFVKSNNKNEKKEVHFSSRKHNVSQGLSFSAFVCYGIGFILWNIDNAFCTHVRYFRGLIPWPFNALGQLHGWWHCFAAFGGYFQILYTIDLRVKCMKNKRKSEQNGSHQNGGTDIRPLGKKNISSRMFRDLWCWIPVRSRRKYDPEYGVNNNTIISNGSSKHMRT | Function: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid.
EC: 3.5.1.-
Subcellular Location: Membrane
Sequence Length: 362
Sequence Mass (Da): 41976
Location Topology: Multi-pass membrane protein
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A0A353SU12 | MKGISAIILAAGQGRRMKSILPKVAHLVLGKPMIWHVAHAARAAGIREIVFVLGYGRDKVLPVVEAYGGKVAIQESQFGTGDAARCGLAELSPAAKEVVVLCGDAPLLRPATIRALLAARRRQGTPASVLTGVLDDPTGYGRIVRGDDGTVARIVEEKDANAALRKVREVNSGTYAFDRVFLERGLPRLSDVNAQREYYLTDVVLEALAEGKRVFPVAAAEPDEVRGINSRRELADATRILLEKKLEELMASGVTLVDPRRTYAETEVSVGQDTVIDPGVTLLGATRIGRGVRIRTGCVVEDSVLSDGVELRPYTVVSGSRVGKGAILGPFSHLRPESDIGEGAHIGNFVEVKKSRIGKGSKANHLAYLGDATIGKKVNVGAGTITCNYDGINKHPTVLGDGVFVGSDTMLVAPLTVGKGALIGAGSTITENVPAFALALCRAEQKVVEGWVARKRPELLKKAGLSAPAAKKGKK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Subcellular Location: Cytoplasm
Sequence Length: 475
Sequence Mass (Da): 50249
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A0A815Q2A6 | MTDPQLTETSSDVDKTNKSKYDKTKILLYIAMGFSAWGDRMWNFSVGIYFISLNPTNLLSVALNGIALNLAVILFATAIGDWIDRNPRLSTLRKSLYFQNLSVAVMAVLVVIALYYQSSLPQYWMIIIQGFLIGIGMIATLSSVACKVSISKDWVVALYGSNRQNLANTNATLRRIDLISNVLAPILTGAIMAFTSRWLSAVLIAGWNVVSLGFELFLYTRVYHLAEDVLANKVSVNKSNEELTEKKKGPLRQFFTSLQGLETYASLSVFLPGLSLALLYMTVLSFDSVTRAYVIEQGLSEAFLGLLNGLGSILGIIGTIAYPFFVKCTGLVRTGIIGFWSEFSMIILCLISLFVYGTSFGPFQHLTIGSCQYYEILTKNNSTTTLIPYQCSNSKLSVLLLVIGITLNRFGLWIADLTVNQLQQERVPEKIRGRIGGTQHSLNQFFDLLRYVLIIFLPRMQQFGYHVCLSVLSVFTASLIYTIWSCSSASHLVPPAADIEMTETNVDLAQHYEVQLGEKLDYVDEDDNKI | Function: May be involved in iron transport and iron homeostasis.
Subcellular Location: Membrane
Sequence Length: 530
Sequence Mass (Da): 59031
Location Topology: Multi-pass membrane protein
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A0A827QFJ5 | MTLVGLLPTMVLMMTCFTRFIIVLSLLRQALGLWFPFVRIMAFLRYMPVLDNSALTARVRIILSLALAIIITPLIPHPVPHDLLSLNSLILTVEQILWGMLFGLMFQFLFLALQLAGQILSFNMGMSMAVMNDPSSGASTTVLAELINVYAILLFFAMDGHLLLVSVLYKGFTYWPIGNALHPQTLRTIALAFSWVLASASLLALPTTFIMLIVQGCFGLLNRIAPPLNLFSLGFPINMLAGLVCFATLLYNLPDHYLHLANFVLQQLDALKGHYGG | Function: Role in flagellar biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 277
Sequence Mass (Da): 30642
Location Topology: Multi-pass membrane protein
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A0A7Y1XSQ7 | MTTPPPQEPSSELYEDAHDVVQRLRRGVKDDKDREQAHRSFWRELPILILIALVAAVIIKTFFIQAFFIPSGSMLETLQIDDRVMVNKLSFTFSDVGRGDVVVFDQFCGATDPNAGENVAEKVFRNIAEAIGLSTPQSDFIKRVVAVGGETLEIADGAVTIDGLAIDEPYLPAELSLPSSLNYGPITVPEDHVFVMGDNRDNSKDSRSCGPIHQDQIVGRAFVIIWPPSHWSGL | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 234
Sequence Mass (Da): 25806
Location Topology: Single-pass type II membrane protein
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A0A7C8ADN6 | MAGVFEVYVKSHFSAAHSLRGYAGDCARVHGHNWMVEVFVRCAELDELGIGIDFRDIKAAVKDVLVGLDHCDLNGLPVFTEQNPTSENIARFLYKELSRRLNTRKIHISRVKVSETPGAGAFYWEE | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.-.-.-
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 126
Sequence Mass (Da): 14195
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A0A0A9XTR6 | MHRAITGCKLWNVSVLTILILTACNVLLMLRLLHTECTSISVEPAPKPHPPLPPLISDSAVTSNASPVFNVDPHLGRWDNKHMYKMIDHALVGSLFSELSVKYSVCLATQTSLEKLHSLVQVAHHWNGPISAALFAAGDEEFTILQGYIDFLRRCYAPVRERISFQLAFPKEKVPTTSSYAEKSSQLDCLRPEASLGKLLKLRSADIVRWRLRNPYPQNHMRNLARKNCQSPHVFLTDVDIVPSTDLAEGLNKFFKTELCNGLCAYVIPTYELDDRVPFPKNKTELVRLTGRGLARPFHHKVFIYNQFATNFSRWEQDKFVNSVHVSHKVTNFEFLYEPFYVAPDTVPPHDERFVGYGFTRNTQVYEMYVAGYEFFVLSPVFTIHWGLQHRKGRPSWRERQNTNNRKNFDQFKREVFVRYHKDPLNMVAHQPKDNKLK | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-[beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + UDP-alpha-D-glucuronate = 3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + H(+) + UDP
Subcellular Location: Golgi apparatus membrane
Sequence Length: 438
Sequence Mass (Da): 50587
Location Topology: Single-pass type II membrane protein
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K0A052 | IGTLYFIFGASGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNLVPLMLGAPDMAFPRMNNMSFLLPPALTLLLVSSMVENGAGTGTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFFF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 218
Sequence Mass (Da): 23068
Location Topology: Multi-pass membrane protein
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A0A507DMQ5 | MRFITHGSAKSSSRTGIFERIVNSNRNIILLSGGVILTAAGFTGHQGPTPYPSVTSSNDRTDLLLSEPQRPYSSKSMTDILRSLLVFKLCQLTPLVSLTPYILKYSEALNIDQPIHAIIRHTFFSHFCGGEDINEVVKTMSAFHHMGIRCILDYAIEADTDAPLASPDEAGLYAANIADTLMQSIDVAKLFPGSLIAVKVTALLPPRTLADWSGILCKVDSCISSSSTGDGVITKEQLIYGLQAAGATLDEASTIYNAASELSDNRVDRISLSQVLSVWHPQGKIVLSRLAKLGDYSTVVDNALEEMKSVCFYARDCHVGILIDAEQTYFQPAVSEQAFL | Function: Converts proline to delta-1-pyrroline-5-carboxylate.
EC: 1.5.5.2
Catalytic Activity: a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)
Sequence Length: 340
Sequence Mass (Da): 36936
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A0A2R2WVM0 | GSPDMAFPRMNNMSFWMLPPSLTLLISSSIVETGAGTGWTVYPPLSSNIAHQGSSVDLAIFSLHLAGISSILGAINFITTIINMRISNLSFDQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 152
Sequence Mass (Da): 16391
Location Topology: Multi-pass membrane protein
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A0A288MLG5 | MVGSSLSLIIRLELAKPGLLLSDGQLYNSIITAHAILMIFFMVMPTMIGGFGNWMLPLLLGAPDMSFPRLNNLSFWLLPTAMILILGSTLVDSGCGTSWTVYPPLSTSGHPGSSVDLAIFSLHCAGISSILGGINFMTTTKNLRSSSISLEHMSLFVWTVFVTVFLLILSLPVLAGAITMLLTDRNLNTSFFDPSSGGNPLIYQHLFWFFGHPEVYILILPAFGIISHSSLYLTGKKEVFGSLGMVYAILSIALIGCVVWAHHMYTVGMDLDTRAYFTAATMVIAVPTGVKVFSWLATLFGTKMVFQPLLLWVMGFIFLFTIGGLTGVMLSNSSLDIILHDTYYVVSHFHYVLSMGAVFGIFTGITLWWSFMTGFAYDKMQMNI | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 384
Sequence Mass (Da): 42137
Location Topology: Multi-pass membrane protein
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A0A853SXT0 | MPVPTSPPKMSAPIDAVQVRDFFSRPARVAPSDFLRREVSARMHERLELVKITPHRVLDAGCGPGADLAQLHKDYPAAQIIGLDAAQAMMQAARAPASKLASLNQFLSKLLPAKTGVDLLCGDLGDLPLAQGSIDLVWSNLALHWHAQPDRVFAEWRRALRLDGLLMFSCFGPDTFREVRDAFAEADLYPHALPFVDMHDFGDMLVETGFSTPVLDMEIITVTYDTAEKLLADVRAFGGNPLTTRRRGLMGKAAWQRMLAALEKTRRPDGKLGLSFEVIYGHAFRPAPRVTRNGEAIIRFDLPRKPK | Pathway: Cofactor biosynthesis; biotin biosynthesis.
Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
EC: 2.1.1.197
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Length: 307
Sequence Mass (Da): 34018
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A0A815SPL8 | TYNGRQDFVQLLIQEIKIDSYGFCLMNRQGFTTRMTDNIDAYKKYKFVVAIENSNCIDYVTAKLIKAVESGSIPIVASLNGRPDYRRFMPEHSYTG | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 96
Sequence Mass (Da): 11041
Location Topology: Single-pass type II membrane protein
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A0A0A9Z0F4 | MAHRIDQGTLYRPPPLAKFFHALPHVNISLHLVNSTFAPDSDVYLESLGILGSIPALWLILTLFMLLIYLCTRCCDRKPRPKHSIVILKWTLSFFTMLCCGAVGVGLYGNDDVHNGMLELLSAGRAMDETISSVKNQTSAIDSTLKLKVEYLLTQLGDVFDEPVTNQTARAGLLALLEAMTSNTSIALASLQDISRPLRPVTLAPTLDNLHLAEAIRWPVTMAILSILLVFCVILLFGVARHSRCALITFSVFGLFAVIFSWLMASIYLTASVALGDLCMSPGQLMEREAPAPLQREILEYYTSCDQISQNPFFVVVRKATSAVDAVSYSMGSMTKIARQLYKPQQLHPKLDMLSKEVKLATSLIQSLATKLDCTQIHNQYMSALHAVCEMALFGLTFMLAASIGAGFLFAILVWLDSHTWIYIRKKQRTYGNIFNPERRPSNLVFWVQTESERRYSQTGRLRWF | Function: Probable chloride channel.
Subcellular Location: Cell membrane
Sequence Length: 465
Sequence Mass (Da): 52023
Location Topology: Multi-pass membrane protein
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Q953N1 | MSVVPVFGASFVGLGLVGLFLWKVSFVFVVLVCILLLIVVFLYDGLSCMIHHYESAFWLFVLSEVIIFGSFLTCCLFFDCWCYDSLSSSLEIPFVGCFVLLGSSITVTGFHHLFGWRYCDLFLFMTIVLGLSFVVLQVLEMEEISFNIVDGSFYSSSFCTVGLHFSHVVLGVIGLITLFLVGSDSFGVYRCTVLTWYWHFVDYIWLLVYTVVYVC | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular Location: Membrane
Sequence Length: 215
Sequence Mass (Da): 24370
Location Topology: Multi-pass membrane protein
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A0A6I8Q647 | MREHSKSGAMWRILKSVNIQTVIIVFLLILLIGSWKPSSSPYSTKKEGQHCPELPSVPVKNDPELLILIWTWPFGETFPLDTCHSLHGISGCKLTTDRNLYSQANALIIHHFDIMEDKGLLPKEPRPHHQRWVWFNLEPPLIIKNLNMMGNHINMTMTYRTDSDIPLPYGWLKTLKEPPRVDIPKKSKLVAWVVSKWYPGIRRTQYYEELKKHIHIDVYGKMHKKLSWEEFYSTIGQYKFYLAFENVNHKDYITEKLWENSFNTGAVPIVLGAPRENYEKFIPPDSFIHVDDFSSPQDLAAFLLELDKDDHRYRQYFNWRSSYEVVRNVGWDSHYCKACKVLHQSQGYQVIPDLAKWFK | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 359
Sequence Mass (Da): 42291
Location Topology: Single-pass type II membrane protein
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A0A0A9ZFG7 | MENHVNLNKPPLHTLPPAGGNMNSYEFHRVELEGLVDSTGSQLVGPRAIPSYKGAANTDESRGGFLVLSPFELAGSQEHVMVNRGWVPIDAGKNPVMLAQYIG | Function: Probably involved in the biogenesis of the COX complex.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 103
Sequence Mass (Da): 11097
Location Topology: Multi-pass membrane protein
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A0A536AR06 | MPDRGRGRMPCRDRCDARPRRRRAAARWRASRHGLRGRGMRDALARKHHRQQALLRVVSQQRLSTQADVVRALRRAGFAATQATVSRDVVELGLVKVARDGTHAYAPPSAAAPGGGMERLRRFCEDYPVEGALATNLVVLRSLPGTANALAAALDASRLDEAVGTLAGDDTVFIAATNERHARALLGRLTTFGIARKGTK | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 200
Sequence Mass (Da): 21721
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U5LTP5 | MTNIFFMIPVFLFLVGFWIYVSKRKHLMNMLISLEYIVLSIFLLVVLVSFTLGLETYVSLMFLIASVCEGSLGVGIMVGMVRSHGSDYVSSFSVLKC | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Membrane
Sequence Length: 97
Sequence Mass (Da): 10914
Location Topology: Multi-pass membrane protein
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A0A5B0P050 | MELLHRSNTGESCRPPNYPVHCPQSSGTNSNTTLNTTAQTRHILMIRSEGDMESKTNDDKYSVILPTYNERRNLPIMIWLLARTFDQHQIDWEVIVVDDNSPDGTLEVAQQLQRLYGPHRIILRPRAGKLGLGTAYMHGLSTCTGTFTIIMDADFSHHPKYLPTFIALQRAHGLDIVTGSRYRPGGGVHGWDFKRKLVSRGANMLTYILLDPGVSDVTGSFRLYRTSILRELIQKTTSRGYVFQMEIIVRARSMGCRMGEVPITFIDRLYGDSKLGKDEILGFVKGLWKLFWTI | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins.
Catalytic Activity: a dolichyl phosphate + GDP-alpha-D-mannose = a dolichyl beta-D-mannosyl phosphate + GDP
EC: 2.4.1.83
Subcellular Location: Endoplasmic reticulum
Sequence Length: 294
Sequence Mass (Da): 33376
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A0A497B3Q9 | MRGRLICLTGIDGSGKTTLAHRLSVSLSQQGTEYRYVYARFLPMLVRPGWMLTRQLFLRGHDMNSDYVGYSSVKKSFLHKRSLAKLHETSVLTDYLIQVTFKVTIPVLLGANLICDRYVYDTVVSDLAPDLDYSPQRVQEVINLCFRVMPRPDLVFLLDVPETVTLQRKSDVAAREYLSERRRIYSTIAADGHHMVTLDGTVPMDQILNQAVAVATRRFSPKFYGHEITDN | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 231
Sequence Mass (Da): 26346
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A0A0A0N0J9 | MTHLQKTHPLLKIANNTLVDLPAPISISAWWNFGSLLGLCLIIQILTGLFLAMHYTSDISTAFSSVAHISRDVSHGWLIHNMHANGASFFFICVYLHVGRGLYYGSYLYKETWYIGVILLLLLMMTAFVGYVLPWGQMSFWGATVITNLLSAVPYAGNTLVQWIWGGFSVDNATLTRFFAFHFLLPFIIAATTLVHLIFL | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 200
Sequence Mass (Da): 22448
Location Topology: Multi-pass membrane protein
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A0A6N6L375 | MSTERFEEIKAKLQGTLIVSCQAEEGFPLNKPEHIVALASSAVMGGASAIRASGPHNIRAVRKATDVPIIGIYKKVYPDSEILITPTINEVEAIVDAGSDIVALDATNRLRPDGDTFPQLYREVRNRWDVPIMADVSTFDEGYAAWELGVDIVSTTLSGYRAYSPQQEAPDLDLVRKLSEQLSIPVIAEGRIAGPDDVRAALDYGAFAVVVGSMITRPHLITKHFAGGLEKPEPSGRVLALDIGGTKIAGGVVDQDGSILVKKKIPTPSGGGPEILEQSAQLLKELRNQHTGNLIASIGISTGGQIDRRGEIVGATDMLPNWVGFGLRKGIEEQFDLPTVVLNDGHAAAFAEHKLGAGRGVQSMLCVVIGTGLGGGLILDGEIQHGSHGLAGSIGQMKASIDGEEYISLEKIVSGPGLLNLYNNSIDKDKSATSPEDVAERAIKGEALAHEAIERIGTYLGLGLSHALHTYDVDCIVVGGSVAQIGEPLFDSTRGALSKYGYSTIADTPIRVAELGPNAGMIGAALWAIKIQNTVN | Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 3/5.
Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
EC: 5.1.3.9
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Length: 536
Sequence Mass (Da): 56611
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A0A6B1E038 | MAVAKQISALRGMRDVFAAEYAHSRGLLEALEQHLRLHAYAAIDPPLLENTELYLRKSGEDIAARLYEFDFKSRRLALRPELTASVLRAYVEELHGEPLPLRLRYSGLVFRYEKPQLHRYRQFTLAGAELLGAPADYADAELLAMACGGLESVGIHNYRLVIGTSALLENFLSSLGLRKQLHNFLLRNMENLRKQGMDYVVDSLRAVLPGFQLTSPDRAEAKEQDSQQLIHVLREMTDAEAHSAISQFLRSLNIHIDANRAESQVIDRLLHKIREDEQAPKLRTALEFMTRLSEIVGEPDYALAAAAQLCQEVALDDSPLKQLEITLRRLAESGGLSGEIQLDFGLSRGLHYYTGMIFEIHGQTRAGEAIQLCGGGRYDNLVSILGGEPTPAAGFAWGIERVASASPAPAASAQERFVCVIPVAEADYATCQAIAADLRAQQLVAEVSMGGRSLRRSLKQADRRGASLVIIIGEAEREENSAVLRDMRGGEERRVAIAALPAAAADMLRQQERDHAS | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 517
Sequence Mass (Da): 57084
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A0A0A9XDD6 | LQWFEAETAMKPEMRIRDYYAGKHILVSGATGLMGKALVEKLLRSCPGVSKIYVIVRPKKGVAPEERWKKTMDGPLFTYLRETHPESLEKCQVLPGESSADNFGLSKEHIQMIEENVNIIYHVAASISFEDDLVAAIKFNLKPTHTLLELARRTKKLECFVHVSTAFSNMNRKGLVEEKVYKSHLGWRELLDLAEDPNNFELLCALQPKVLNGHLSTYTLTKGLAEDAVYEYRDHFPIVINRPAIVLGAFKDPRPGWMDVDNILSLFGKGWRMGVLRVMLYEDTHELQQVPLDLPIKALIVAPWKKYVQAQRDVEVHCCRLDY | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 323
Sequence Mass (Da): 36935
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A0A816H474 | FFFIGYAIAKKIIKLINDVALVINNDTHIGNRLKLLFVKNYRVTAAEYIIPAADLSEQISLAGTEASGTGNMKFMLNGALTIGTLDGANIEMCEECGAENMYTFGFTVEEVQQRRQQGYDPYESLKNEELRLAVDQIRDGYFSPDDRSRFHDIISTLLTGGDHWMVLGDYQAYIDKQCEVSRDFLNHQIWYSKCIYNIAAAAKFSSDRTIEEYAKDIWHCTMHKNGRPDNIKEECSTMNHEELSHHKSNDSLT | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate
Sequence Length: 253
Sequence Mass (Da): 28846
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A0A6N8YR54 | MSAVDDQRYIALVDLDAFYASVEVIEEPSLAGKPLLIGGSPTSRGVVAAASYEARKYGCHSAMPMSRAVRLCPEAIVLRPRFHLYREYSGRVMDILQQESGVIQQMSIDEAYVDLTPVSKDMQEAAGRAHRMQGRVRVDLGLPCSVGIASNKMVAKVACETGKPGGFVVVESGTESAFLADLGVRSLPGIGPRSTERLRAHGFHTLGQVAAASPEALVTVLGPWGAALKRRAQGEDSSPVETDRETKSVSAEETFAEDVNVRESLAEELRRMAERVARSLEQHGLVGRTVTLKLRLSDFTTLTRSSSRDNATAHADAILADALHLLDANWEPRTNVRLIGVGVSNLRPVQAPGQLALDMDAAEEEN | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Subcellular Location: Cytoplasm
Sequence Length: 366
Sequence Mass (Da): 39485
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A0A814EIR2 | MILPASKEEGKRIKKRYCVFNMDGSIAELKGFEVKRNGELQLIKIFQTSVFEAFLKGTTLEECYNHVATIADYWLDMLYSHAKDISDKELFELISERRTMPRILAEFLGEDVIKDKGLCYRFDIANVPRDVPITARAIPLAIFQSQQSIRNHYLRKWLHLSTVDNLDIREILDWNYYIDRFNSCIQKIIIIPAALQNIRNPVPRVSHPDWLHKRLVEKNSLYKQKRITDVFNSIDKQTYIDNNEPQFIITNDIEDIGEQTKSSINLIKKLQQ | Function: DNA polymerase II participates in chromosomal DNA replication.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Nucleus
Sequence Length: 272
Sequence Mass (Da): 31921
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A0A146KKZ4 | MCTAHLHAVWATRRLWILCSFPWNLFAQLWNFHRTTTFYALTSSKSCFGTFGGGDPCWGTTHTHTHTLQIIAIFGGFMYMSSAFTSMLTYLRSRKQDQAQVLFMGLFPLRASYLPFLLLLLSYLEGNIAQDIIGILLGHTYYFLTDIYPRMTCREYVCLAGSMLMLGTGYTENCTSHRLRLLQTPPILCYIFRQPVVPPSSFYNYIKITQGFRGYTITGCVPTTFVPLQPPVKSATATFPTSSAPSVAGS | Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 250
Sequence Mass (Da): 28149
Location Topology: Multi-pass membrane protein
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A0A815UYD9 | MNILKTCYTELDSLITYLPNLNSNQKEYFREIYLTKKMTTKQEIQWKEILQRKNSIINNNELFLYNLLINCYMKNRSNILLINIDIKNKNLTKNTFQYNDYIYKNSLITYICLSNIWIKRRKYLIDDALIYLLSEFQLIECLTRKRQLFIQLSGIGETFFNVPYYITRNLKEKQQNNFKLNKFNTRKRTVQFHLHTTKQGQQAHLTDLYETLIARNMIQYRISKYERFDIHHPIEKLFNEQLFVDAFFQSDFSKKFFNHRPKEEMEQIRENLIPIFEKFQLNHHQFYLRRRSRLPLSFTNHHVPEPTATLDQLVPLTTPISSIKNFICIWLKNILPIELFGSKYNYKLFIYKMCFLIELPRIQEYSLGDAIRKLKLKHFQWSNIQMLNSSSLICQLYICHLIYFLIQYVLILVRSYFYVTEPSTPSHQLELIFYRHKIWYAIQQKSRKELFSKSCCPNVEQENVNNYDCIRYLWKIRFVPKITNVRYLACAQIEFNTRENINHLKYTNEILKYLRRHNRHLIGISTFNRVEMHRRWQDYCRIAPKIDNDSMTYFLRSDISNFYDSVNLDYLDK | Function: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.49
Subcellular Location: Nucleus
Sequence Length: 573
Sequence Mass (Da): 69834
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A0A2R4FZZ0 | SPSNISAWWNFGSLLGLCLIVQILTGLFLAMHYTADISSAFSSVAHICRDVQYGWLIRNLHANGASMFFICIYLHIGRGLYYGSYMHKETWNIGVILLLLVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGVNLVEWIWGGFSVDSATLTRFFTFHFLLPFIIAGASMIHLLFLHETGSNNPTGLNSNT | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 193
Sequence Mass (Da): 21463
Location Topology: Multi-pass membrane protein
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A0A815M8Y8 | MESFGLTLINKLNKNSTNAKTQIDYCFTNGNGLKSDYFESLTSFHKPIWIRKREILTGIHVDEIKQIRTDIPFNLKDLRSYDQSDTMEVDEEFSSDRYKIVDENEQTDIDKTFNLKDRHTNDQSDMMEIDEQSSFANYENIDSNSRKILDHFLLVLDFNSTTDTDQISNQVQIINDLIGKSPFITMHNKDQSVRLKSKTEYSVQAFVSVYTRTRTTADGNCLYSSLSIINIASEKLTHSMRLLAVNAMINNSDYFQTLCKVLDYSFEEQLQRTATNTIWGGEVQIQALSIALSHPIYSYIQFDNNPKNRHYIPLNISVQELIDRFNKGTAGSHLKHIEYKSDMNKLGFCIYYNGTHYDALLPFQANPQQFVPHFDKINMSL | Function: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
EC: 3.4.19.12
Subcellular Location: Cytoplasm
Sequence Length: 381
Sequence Mass (Da): 44089
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A0A0A9WU53 | MDKKSVKVKSTSASSGISESYEWSPSPWLLLLCIITVLSLATRFYKVTEPEHVCWDEVHFGKMGSWYINRTFFFDVHPPLGKMLIALSGYLSGYDGSFAFDKPGDKYGDVNYVGMRVFCTFLGSCIAPLAYLIVLELTNSPSAAFMSSMMIICDVGILTLTQYILLDPILLFFIMMSTYGIVKFNNCKKSCIWLHNYSEKS | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Location: Membrane
Sequence Length: 201
Sequence Mass (Da): 22670
Location Topology: Multi-pass membrane protein
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F6U3Q0 | MGKRQHQKDKMYITCTEYTNFYGGKRPDIPKSNFRRLSFDHCSLSLQPFEYPVCTPDGIVFDLLSIIPWIKKYGTNPITGEKLEAKSLIKLNFAKNQDGKYHCPVLFSVFTNNSHIVAVNKTGNVFSYEAVEQLNIKSKSYKDLLTDEPFTRQDIITLQDPNQLDKFNVSNFHHVKNNLKVTDPDEEKARQDPSYYLKNANMETRETLSELYRDFKGDEMLAATMKGPEKKTTDKLNAAHYSTGAVSASFTSTAMTPETTHEAAAIAEDTVRYQYVKKKGYVRLHTNKGDLNLELYCDKTPKTCENFVKLCKKNYYDGTIFHRSIRNFVIQGGDPTGTGTGGESFWGKPFKDELKPNLSHTGRGVLSMANTGPNTNKSQFFITFRSCTYLDRKHTVFGRVVGGFDTLTAMENVDTDTKTDRPKEEIRIESSTVFVDPYDEADAQVAAEREKTRKAEEEEKMKAKALLPKKEQSQEPKAYRKGVGKYINMAATKRSAEDDETGPSTSKKERLTRDFKDFSSW | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 521
Sequence Mass (Da): 59275
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A0A2S8MSX2 | AHVIAARYPITVALHTDHCPKDKLDTYVRPLLEISSERVRAGGNPLFQSHMWDGSAVPIDENLAIAQELLKQAAAAKIVLEIEIGVVGGEEDGVEAEINEKLYTTPEDFEKTVEALGVGEH | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Length: 121
Sequence Mass (Da): 13171
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A0A0U3HSK0 | MAGTGGREGDAALLDGARVVVTRTPERALALARLLRREGAEVTAAPLLEATLPARTAPLAQLLDRAARAGHGDWLAVTSVNTVRALQALAGEDLGGRLAAARRAGLRVAAVGDATASALAAAGLGPDLVPAGAHSADGLLAGWPEEPDPGLALLPQSARARPVLADGLAARGYRVRAVTAYETVPWPAAAPLAPGAAQDGPDAPGVLDRGQLLARLSGPGVDAVVLTAPSHLDELVGEDPSVLAGPALVAIGEPTRRAAAAHGLHAVAAGRPTPEGVRDALVRALAARRGAPPGRSAPPGTPPGTDPNRPTQETTP | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Length: 316
Sequence Mass (Da): 31550
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A0A7W0TC26 | MDVRIAESAEEAAGFAGAWLADRLREAIALRGEVSLAVSGGSTAPGLFAALAGEPDVAWPAVSLWQVDERVAPDGDPDRNAGQLDALPSAATVHLMPVTAPDLSIACDEYASTLPEQFDVVHLGVGPDGHTASWPPGDPVAYDSHPVAMSAEYQGRRRMTLTPGVVNAATWRLVYVLGASKSDVVASWLRGDDSLPIGLVEERSTVVVLDPGASSGLPQ | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequence Length: 219
Sequence Mass (Da): 22819
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A0A0N5CPN2 | MPHQLRRVNQNNQNRIDNENGTDIKTKTTYLGISQPISISGPDETDIVLSKKLDEYLQANGYFETEEEMNLRLKVLCKINAYVKKWVQLVSRRRQMPESEIQQVGGKLFTFGSYRLNVHTRGADIDSLCVAPRHVNRNDFFTSFYEMLAEDPNVAELRQVQEAFVPVIKLKYYGIEMDMLFARLALPRVPEEQQLNDDFILKNLDEKSVRSLNGCRVADEILKLVPNVSTFTYALRAIKLWARNHGIYSNVLGYLGGVSWAILVARTCQLYPNAGPATLVQKFFLLYTQWEWPNPVVLKDTEVLYAREMPSLQELVFDPRSRPGDRFHLMPIVTPAFPQQNSTFNVTKSSLKIITNEIEEGLLITDSIFNGKADWSALFEEVNFFTRYRHYLALLCVSASEQDELVWCGLVESKIRLLVASLDRRKSVKVCHVHTKHYQPRNDPFPVHIPLSNPRCRVWFVGLDFNKAVSRKIDIQHEIQSFLDLLNNLATTQNIYVEGMSLIPHYLRKVELGRWLNVDDLTRGRNAMKRKCLAVSDNQNIAVALANKARSEPSSFSSLHSLESASPSTSSSGTETKKVENLSVASSSGNLLLSGDEQIRVASFQLGEDQIHHRKRRAEMSVDDECESAHIKLSPSPSSNVLSSDTKEVESERGSQNTSASFSI | Cofactor: Binds 2 magnesium ions. Also active with manganese.
Function: Polymerase that creates the 3'-poly(A) tail of mRNA's.
EC: 2.7.7.19
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Subcellular Location: Nucleus
Sequence Length: 664
Sequence Mass (Da): 75435
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A0A183U8Q2 | MCGSSLEMYGSRLQVAASKNVRMWLTKVRKIKSIYHTLNLFNLDVTQKCLIAECWCPVADLDRIQLALKRGTVGPSSRFFLSYFSDLRNYLRELITKSIVRKRCFYWDKDRYSSLLYLYSMSR | Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Location: Membrane
Sequence Length: 123
Sequence Mass (Da): 14541
Location Topology: Multi-pass membrane protein
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A0A2H4UKL3 | MSGMSGKDSPSSALSAVPADAAAKLSALEAENARLRDVLSSRQGKEPTYSGYLYKYRPFTSAFTKYQWDQRWFTLNGTALQYYKTEKDAVYHPRGHVNVEGCIVEWEGLKKGAYWTFQVLDPRTGASLLRLSTQDKGRAEVWVQHLVDAGCHKRILNASYRNRSPPRSADIRWNQSATSSPACSTGRHPPPSVPGSVNRRLDLAQRWVASAGASAGGADSVSTTGYTSESGLSEAGTEQPPARQASNLRPPAQPADKAKRGPILGSTPMHTEVRSSLLDHRRMATTQHSGIFNLMTVVLFAANLRLVIENILKYGILANPAGWVSAVVTPKGNVWLTLCWLWLAFAVFTAYAIELVGCARLEAERKAGIAKRKKEISPSDAKRRAAAMGRLTERLMWLLNFANISAALLFPCYMVFATNADPAPGGVLMLLTVILWMKLISYAHCNQDYRMARREGVLRPGERGSDAPIPREGPGALAYPENITLTNLAYFVVAPTLVYQPAYPRSSRIRMRWIMRRVLELLFTIGLMLFVVEQYTAPTISNSLAPIQQLDWPRLVERVLKLALPTLYGWLGIFYSLFHLWLNILGELTAFGDREFYKEWWNSTTTDDYWRTWNMPVHKWMLRHVYSPVVRAGAPRMTAMLLVFFVSAVFHELVVGLPLHVGMWSPVQWARFWSNPGLPSWSSIQWPHAFFGIMFQVPMIFATRYLQAKIQNAQVGNIIFWVVFCIIGQPVSIIMYYHDWCVLNR | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 745
Sequence Mass (Da): 83800
Location Topology: Multi-pass membrane protein
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A0A7Y5NLK4 | MHLALPGALVALLAGIGVYGVLARRNAVLVLIGVELILNAANLLLVTAGSRQGAPFSAGAVLTLFVITIAAAEITVALAIILVLFRRAGHIDLTAVPDLTDDPDDPDDPEDPDEPSDVGATPDPARSGEGAP | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 132
Sequence Mass (Da): 13405
Location Topology: Multi-pass membrane protein
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M9VCW2 | ASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVVGEDNQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKAQAETGEIKGHYLNA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 234
Sequence Mass (Da): 26107
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A0A0A9WLB0 | MIQGGDFTHGTGVGGESIYGKRFDDENFSIKHTRAGLLSMANAGPDTNGSQFFITTVQTRTFFLLLLLWCLYLLSLLCVLVYSFQSMALPSPHTAWLDNRHVVFGEVLDGMDLVRRIEAVGTQSGRPSKRVMIADSGEL | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 139
Sequence Mass (Da): 15331
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A0A146LU03 | MSLLRSGTDLEMRLIWMAMLVLVTASTQHVHKPARILAVVPMPWKSHHFVFQTIIKALAARGHQIDYLTPFPIENAPPNVRHLMIKDTFAETIGSVELEDMDLFWSPQEHLMWRSMNVKYLEEVYRNEPAIRTLLSSNEQYAIVMSECNINQEITAVWAHRFNATPVSVLAVPDMFFANEMTGLPGNPSYMLDSTSHLSDRMDFLERLWNSVQYVVSLPLHYYKLREFQRVADDVLRYPGWETRPSVSRLASDQALVLVNSHVSVGSVYPRSPHVKEIGGMTLTGSTLLPKDLQSFMDSAAEGVVYFSLGSSVDMNVMTRGNKMDGFLRAFQALKHRVVLKWMGDNMPNISDPRILIRTWFPQLGILAHKNTRVFVTHGGLQSLMETVNYGVPVVAIPIFGDQFKNVKIAVSRGLGIELAKQNLTETSLRWAIEEVAKNTKYKEAVRKRSNILKDVPMKHVDEAVYWIEYVLRHGRVLQPASLHMPFYQIYLLDVAAFIIAVLGVFYFLIKAAKANYCR | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 519
Sequence Mass (Da): 59142
Location Topology: Single-pass membrane protein
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A0A0A9XRR9 | MDPHTLLPFLHDVPPHTVQLERRVEFTWVPRTLPISLRNVASAQSKQFLRLGCGNLWRQLRLGWALHCDVGLVPTAKLPQQATSMLRPRTLELLLADAALWNKHSLIVPAHAGRSHVPTSHNSIELDPWCRTRQPMFVGASWSSVLLACRATVRRTSLQQTIKGILTAGPVKSLRYLLHKLLR | Pathway: Lipid metabolism.
EC: 2.7.7.41
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 183
Sequence Mass (Da): 20673
Location Topology: Peripheral membrane protein
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A0A6L7JJ72 | MISNRAIAAHLERIAQAIDLADPDSGRSRTYGAAARRIESSKQDFAALAQARELTGVPGIGPSLARTIGEFVSSGSSRRLDELLQQIPPGAWQLLSVRGLGARTVGRIVRDLGVSDLDSLRAAGSDGRLSQLPGIGSRKVAQILAEIERIAATRGLFSLGHALATAHLEAARLGNIDGVSAVRLAGAARRACETMSGVDLVVAVRDPSRPALAALGGESLVQLDPDELQEPIPVRIRVSAEESLGSALVLATGSDEHIARLTDLARRRGIELDSPQTTFGTEAELYRAVGLDLIPPELREGREEIELARRGQLPRLLEHRDLGCDLHAHSDWSDGQDSIAAMAEAAHRAGLRQLVISDHSQSLAVANGLSPERVAAQRDEIAAQARQWGELSLLHGTESEIRVDGSLDFEPEVLASLDWVVASVHAGLGQSRSAMTERILTAISNPATCAIGHPTGRIVLGREGFDFDHDVVFAAAAETGVALEINSQPGRLDLSADLARRAARAGAVLTVNSDAHAAAQLANTQLGAMIARRAGLTCAQVINAWEWEQIAERRARRLAGA | Function: Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Cytoplasm
Sequence Length: 561
Sequence Mass (Da): 59500
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A0A7T0KBB1 | MNHQSKRLWIESIQGSRRKSNFLFASVLFAGALGFFLVGFSSYLGRNLIPLLFFEKILFIPQGIIMCFYGIAGLFFSFYFWCTIFFDVGSGYNQIDEKKGIICLFRWGFPGRTRRVYLRFSIENVQMITMQVQKSLFSSHHVLYMKVRGLPDIPLARTGEKIHQKEMEQKAVELARFLRVSIEGV | Function: Seems to be required for the assembly of the photosystem I complex.
Subcellular Location: Membrane
Sequence Length: 185
Sequence Mass (Da): 21518
Location Topology: Multi-pass membrane protein
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A0A0A9WM37 | MYRGYGPSVAGIVVYRAGYFGLYDFSKVYLMPHAGLQDGTILCLLTKFSLALSIDIFSALAAYPLDTVRRSMMMMSGRKDKLYTNSLQCAKYILTHNGASGFYKGALTNCIRAIGSA | Function: Catalyzes the exchange of ADP and ATP across the membrane.
Subcellular Location: Membrane
Sequence Length: 117
Sequence Mass (Da): 12815
Location Topology: Multi-pass membrane protein
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A0A183UR28 | MHHPVSSASGLNNGMNRETRPMERCTMQLGKQKVNEVRNNKIDDVETEFIMGQVQLLEPSTNRQVLVLAWTRFFEYDMAELLKMKGLTNCKYMCTITTDRRKFSAADAVVFHVRDMNLTDLPQSRSDNQTFVFFIQESPYHTGYVLDQIPSNYFNITMTYRLDSDVRAGYGWMSPIDNTTSRDEVWRWNEVEDIVEGKSKSVLQMVSNCATESKRELYVSALAQHIEVTEYGRCGHGSCDKQCEQQAIAQHYFYLAFENSVCRDYVTEKLFRRMEMIIVPVVLKRSIASSFLPNGSFIAADDFDSPRNLADYLKYLQNNKREYLRQNLARLRPISLAHKFSKQNRLYFSYLFFEISLSLSRYFEWTKAYKKKLDDDYGCSLCEFLHTNLTKPRVISEIKDWWFSGGACVNDYALTLISVLEIMGKFLG | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 428
Sequence Mass (Da): 49822
Location Topology: Single-pass type II membrane protein
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A0A7Y3I1D9 | MPTLPHDPHAHTMTFGDHLEELRKRLLFALAAPLPLFIVLFFFSDTLIEWILLPVYDVLAVHGLPPDLQVLSPPEFLITKLKVALIGALTITTPWLIWQAWLFIAPGLYQHERRFVRLLIPGSAVLTVAGVALMYFVMLPLMLHVLIMFAADMRVPVPPPSVPAAVTELVESTPVVEIRTRPPAPLQPGMVWLQAPEMELRAAVAGDDDGTVAVHVVPPPRDGRIDQTFRVSFVVNFTLVLMLGIIVAFQMPLVILLLGWLGFVNADWLRRQRKSALAVCGVVAAIITPADAVSMVLMLLPLYGLYELGIVLLVVAPAHAVVEGRVFRWRPKRADNPPATADQPRKPVQSEKSVSRETGPADAGNETDRSDRS | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Location: Cell membrane
Sequence Length: 373
Sequence Mass (Da): 41128
Location Topology: Multi-pass membrane protein
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A0A8T3S3W5 | MELIPAIDLRDGMVVRLRQGDFERESVHGLDPVAVAQRWAGEGASRLHLVDLDGARAGQPVQAALVERIVSSVSIPCQVGGGIRSLDDARRMLLLGADRVILGTALLRDVQLGRELVGEHGAQRIVAAVDVRGDVAVGSAWATGADGVDHRAVIEGLSAGGLEWFAVTSVERDGMLSGPDLETLGALREAFPAARLIASGGISRLADLCALTDAGMAAAILGRSLYDGQIDLTEALAAMRPTSRRSSSDITGGDGKQDPAGFSRGRVL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
EC: 5.3.1.16
Subcellular Location: Cytoplasm
Sequence Length: 268
Sequence Mass (Da): 27946
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A0A5B0QAN5 | MRRLQKRKIALTIIFGFALINHTVQIALGQYMITMKRGKTNSARKQGTLNACSFLTIAAVIFRLELVALLAPIVLLSLISKRVTFWQLVSRGFLVTFAGLEMTLPIDSYFWQKLTWPEGASLIFNVLEGKSAEWGVMPWHFYLTSSLPKLLGITYPLALLGFVLNRKVFLLGACTLVFVVAMSCLGHKETRFIIYIVPVWNLSTSICVHRITSPFRHSRWIKLGLMSLIGVVAALNMAFTTYLSMHNYPGGAAMMALHSLEDLRPIQELNIHLDNLVSQTGGSRFLQLNDLDGAQNYPLTTKGRLWRYDKLANITESSHQFDVILSEQPELHNFQALEHVTAFDGVRRRHFKAPLSDRLFDFVQSCWAKKACFSFHSMWDILSPIEIVFNHKQITIFLQTNPT | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 403
Sequence Mass (Da): 45822
Location Topology: Multi-pass membrane protein
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A0A5J4YNR1 | MGPDRLCDAMAFAGQLDSVKATLRSRPRKGAFCSTLAQLRRDNAVRARRTVAPGWLQRSAQEPGSSRLRMGASGSESIPQVGVAVTREAGKNDTMRELLVSKHRDNRTLDSAQPFHIQVHEIPCITHTQVPEGLQKLDDALRQDGGLGHEFEWVVITSPEAAHNFLFAVEAAAQSTESSNSDAYAALANVKVAAVGKATCDALEEGGVSVDFVPSVAYADALGTELPKSDLSLSSQTGCKVLYPASARAQRTLQTTLEQRGFQVTRLNIYDTVAAVFSERERHLAGHSVDIACFASPSAVSAWHKEMQGVLPACAVCIGKSSALRCVELGMAEHTVFFPQNPGVGSWAEMVFVAAASLLEMNSFTTFSGKPSEALEAGPQN | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Length: 381
Sequence Mass (Da): 40744
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A0A2E6NW01 | MLEEITIFSDGSSLGNPGPGGYGVIMRWKDKEIKISEGFRKTTNNRMELLGPITALKKLKQPQNVLITTDSRYVIDGIEKGWAKKWKQNNWMRDKKNKALNSDLWELLINQCDYHLSVKFKWVKGHKGHAENEECDLLAKEAAMSSDLKIDEIFELKELE | Cofactor: Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence Length: 160
Sequence Mass (Da): 18439
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A0A816GF91 | LLPRHLQIIYEINARHLKNVRDRFPFDEDRIRRMSIIEEGSIQLINMAYLSIIGSHTVNGVAQLHSKLLRESMFKDFYELTPEKFQNKTNGVTFRRWLALCNPDLFSLIVECIGEQFIRNNYQSLQLFRHYALNKNILSRIQQIKIKNKLRLARMLEDEYNIEINVESIFDVQIKRIHEYKRALL | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate
Sequence Length: 185
Sequence Mass (Da): 22162
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A0A3B9RUV9 | MTMYHPRVKMCGMTRECDIRHAIECQTDAIGLILYPHSPRGLTLEQAVNILPKLPAFITLTVVMVNPNAIDVWQVLEYLPAHVIQFHGEEDADFCAQFKVPYIKALPAISRDFILKKSSEYYSAQALLLDTPSLDKKGGTGQTFDWSIIPPLAQPLVLAGGINEANVTGAIQRVKPYALDLSSSIEISPGIKDKTKMLKIMSKIKPTAVM | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 210
Sequence Mass (Da): 23222
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H2EHC7 | SWLATLHGCQLNYSPSLLWSLGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFINWYPLFTGLNMNSLLLKVQFFMMFLGVNITFFPQHFLGLAGMPRRYSDYPDSYTTWNIVSSMGSTLSFISIIFFLLIIWESMISNKTNIFANHLNSSIEWLQ | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 175
Sequence Mass (Da): 19881
Location Topology: Multi-pass membrane protein
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A0A183V7G8 | MTVTYTLEVSQARFWGFPKLLARWRGSIYRLMYREMCAFLAAYYIVAFIYRYAASTNMQRRFERFAVYCKEFTAVVPITFVLGFYVAFVVGRWWQQYISIPWPDRIAMQISVFVQGADERGRLIRRALVRYLNLLAVLTFQSTSTVIKKRFPTIEHLVDAGLLTANERADLEATVAPHGIWWIPAQWFAQLAMVARKEGRIFDDMHLKSLIDVVTIAVYSFFASCLFGRQYLLYGTKLNERHEVDYYVPVFTILQFFFYVGWLKVAESMICPFGEDDDDFDMNWLVDRNVQVGYVIVDQMHSKYPKLSRDIFWDNLESEMPYTQAAANYKREPFFGSTTAMKLALVFLACFHLASAICALINS | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 363
Sequence Mass (Da): 42339
Location Topology: Multi-pass membrane protein
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A0A183U0H7 | MAEYLRMSGIYWCLTAMDLMGQLSQMGTDAIVDYIKKCHQPNGGFSSAIGHDAHLLHTLSAVQVLIMLGRLEEIDVSAVTNYVVARQNADGSFGGDESNEIDTRFSFCAIATLYLINHLDAADIDKAIEFVLKCYNFDGGFGTRPGSESHAGQVYCCLGSLAITGRLEQINIDGTGRWLAERQCRSGGLNGRPEKLPDVCYSWWVLASLATIKRIHWIDRDLMRKFILACQDEDGGFADRPGDVVSLLFVHGSIAKKLI | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX.
EC: 2.5.1.60
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Length: 259
Sequence Mass (Da): 28529
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A0A5B0RM31 | MNSLYSLALRQTSSIQAELTELEKSITSSTTRNNTAGLHGQIAASLSSLQRTLDDYQAMSKAEVVDSKRAKAAARIEKFKDDFLALKKQFDQIKTLERTLKEESQRQELFQSNSTSYRTNAATHSSPTTAESPYQTGYHRTNAAINSRAGGGGGAGYRTNSALDENHFLQQTNSTLDIYIAQGQAILGNLGDQRDMLKGTQKKLRSAANVLGLSRETIQFIERRSKADFILFGIGATFTLVSFYFILKLFG | Function: SNARE required for protein transport between the ER and the Golgi complex.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 251
Sequence Mass (Da): 27711
Location Topology: Single-pass type IV membrane protein
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A0A0K8TJ45 | MMTGVLRIFRFSLVQRPKNLFDSTKSVGQNVSKRFLSETTTPPNPKGSRMRVLILAGAVGGSIGAAYTFYKREGLKKAILNPDGEGLPVIWKELPNVRVSREVVGPDRSLDITLFQYPTCPFCCKVRAFLDFHGLSYKVVEVNPIRKTELKWSEYRKVPILVVKVDDGYIQLNDSSVIISILQSYLLDPDYKLRNVVKFYPNIAYMGDDGNVKKEVLNKYHVMYHTSVPEGQTNDRIANERNWRKWADNNLVHMLSPNVYRTRSEAVESFEWFSKVGEWDKNFSPWEVSSIIQLGSGVMWMLGKRLQKKYNLKQDVRLSLYDSCNNWLKLLKTRGTQFHGGSKPDLADLAVYGVLSSIEGCAAFADLRKNTKISGWYESMKASVGRHDGFLGR | Pathway: Lipid metabolism; prostaglandin biosynthesis.
Catalytic Activity: prostaglandin H2 = (12S)-hydroxy-(5Z,8E,10E)-heptadecatrienoate + malonaldehyde
EC: 5.3.99.3
Subcellular Location: Membrane
Sequence Length: 393
Sequence Mass (Da): 44816
Location Topology: Single-pass membrane protein
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A0A0A9XS04 | MSSADGVASFFENKTVFVTGATGFLGAVLVEKLLRSCPGVERVYLLIRKKKDEEADKRLARILSMPLFSSVPAELKAKVSAVEGDVALEDAGLSKNDKAKVVGETQVVFHVAAYINFNAGLGRAVRINVQGTSYILDLAKSMPNIRVFVYTSTAYCNCTQSDVILEKVYPSKWAPRDFIKHIESMSTDEIAIQQPSILGSFPNAYVFSKLLAENLITSERGNIPVAIVRPTIVMGALKSPMPGWVDNVNNGAAGFIAGAGRGVFRSIHGDGSKVADIVPCDQFANLLVACAWDVAMNGDLRVYHHSSGRDNPIKWSDYVGLSVEGARKYPCTGLVFLPKAKLRSSKVWHDVYSLFAHFLPAIFLDFIGPLKGIKPGLMDIQNRYFKGMQYTSFFTFRQWVFDTKNTDELAAKLTDAEREEFDFDTRHIDWPSYMESCVHGIRKYYHREPDRNLPLARMIYQIWCVIDFGYHTLMLLIISAVFFFLSNDLVLSVLLGIIFLLLYIWF | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 506
Sequence Mass (Da): 56619
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A0A6D2JQQ3 | MVERLEKVGLSFAAQDESDKRMEIIEFPSHPFFIGAQFHPELKSRPGKASPLFLGLIEASCGELETVMSPASAHQNVISNGTKNVFVNGSSKKATNGLADTDDEFTTMMTLPNRHHKPGTEPHTIHSITHHSNLQYVNDVRNVLSSTEFAVLENSYLSTVIKLAKMGNRFSAKLFHFFMQRRILTRGQVLWFSFADQPIRLQRDGGRMNSLEKVSLGAAIISEGIIVGRSSGKRIPQERLLKYRHYEVFSKLPWGKIGYEALSESILKMNAHSWSKERYDVQGFVWAIIFWSFAAVPDLGITIATPCETSASSDPLCFQWKSVKYGSMSKVILVEKRENVLVKTIIGESKAFEHLVQQTHPDDRDFDSVVCLVTQGYNMTREDWVRGEIDILVASGQIGNQQRRQRCANP | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate
Sequence Length: 410
Sequence Mass (Da): 46195
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A0A383S357 | MAENRFAALDAAAGGLTPDATLVDDLFQVVEALRANPQLRRALTDTSLAAAARGRLAERLFGQRIGSVAVDLLATAAAMDWRFGLELADALERQGVRSAVRSGDPATVRDELGACARLIGELPQIEQALSAHGSGPEQRSAFVTRLFGPRISAATLLLVQHAARRGGRVGRTIAGYEEIASAVLGRLLARVTVARALPADQAERLSEQLARVYATPVDLSISIDPEVLGGVLVRVGDEVIDGTIATTLDQARRQLA | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Cell membrane
Sequence Length: 256
Sequence Mass (Da): 27047
Location Topology: Peripheral membrane protein
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A0A1S5RSB0 | INSISLLLQPVAFILVILSTAAEFGGGTGWTLYPPLSTSLMSLSPVAVDVIVIGLLVSGVASIMSSINFITTVVHLRAKGLTLGILSVSTWSLVITSFMLLMTLPVLTGGVLMLLSDLHFNTL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 123
Sequence Mass (Da): 12885
Location Topology: Multi-pass membrane protein
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A0A183U776 | MEMAGIVCHTGANIITEARKLVEQIGRPLELDTDGIWCLIPASFPENVSFSLNNPKRKSVTVSYPGAMLNALVRDNFTNDQYHHLESDGSYTVTSENSIFFEVDGPYLAMILPASKEEGKKLKKRNSYNERCPELTILTASALK | Function: DNA polymerase II participates in chromosomal DNA replication.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Nucleus
Sequence Length: 144
Sequence Mass (Da): 16024
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A0A0N5CX91 | MQILDWEARVDDYGRIFYIDHINKRTTWEAPANSCVTTHSKLAQKLICLQIFKTSEALQFYNSSRYLKHILHRIRRDGNTFERFKQNRELVKFLNLFADNTLPLPEGWQLSGHLNEQQLQTVEQINFRFQLRRSQLLLDAYNQMLSVDASELRKSQLSVVFDEEDGLDYGGPSRELFFLLSRELFNPYNGLFEYSANDTYTVQISPMSVYVDHYTDWFAKVKFELFFYQKLSPSIDDLKAMDPQFYNSLVWIKENEITEDLGLTFSVTENVTGKIVDRELLRDGKNLMVTEVNKYEFITLMIKWRIERGVSEQSKALLRGLYQVIDRDLLRIFDNKQLKLMLSGTMEIDIEDWRRHTEYKNGYHADHICITWFWNIVYGMTNEDRLKLLQFVTGTSSVPYDGFQALRGSDGPKKFTIEKWGSEKSLPRAHTCFNRLDLPAYLTQHILGAKLRTAIHESATYEIE | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.26
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 464
Sequence Mass (Da): 54608
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E7N8H2 | MTYFTVNGDIPSIRSSSQISTLGPSGTSSEHAARYFLKSFGTKSFGTKSFGTDNCRILLYPSYRDAARSVSVGESEYLVVANAFHGINDFYMDPVLSVHSVFLMLTPQYGLAKRPGDFLRSQFEVISHPAPVPLIAELMPPRHKCAGIVAANSTAAAASAVENGDYDVALTTHSAAEKHNLVFFSNQRPIEMVWTVFTHG | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 200
Sequence Mass (Da): 21771
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D7LEJ2 | MAGRSERRSRFRDLRRCSFPVIVAFLCFLASSTFLSQLHIYFTSTHRLICTAENSCLCWLPEHYQMRLTLEYYLLPAPMRNFPRRENLENPNHYHYALFSDNVLAYPNYKSMLNLLRFYISIIFPKLEKILLLDDDDVVVQKDLTPLWSIDLKGKVNGAVETCGVTFHRLDTYLNFSDQHISDNSERMEKEQHNRSLSFLAKTAGLIMFYNLTLPLERKWHLLGLGYDKEIDEKEIANSAVIHFNGPLKPWKELGVTKYQPYFVGFVCLQNMADILSCYTFLL | Pathway: Glycan metabolism; pectin biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 283
Sequence Mass (Da): 33175
Location Topology: Single-pass type II membrane protein
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A0A6B1E4Q6 | MNDNRNRSPSISPGAVVVAAIFLLVSVIGINWFTSFVPVVLPPQASAESKSVDDLFYVLVIIGGIVFFLIQGMLLISVIFFRAKSGDQSDGPTYHGNPLLEIVWTIIPAGVVVFLAVLSFNVWMQNTEPKATVNMIDGNEIKINVSGARYAWTHTYQTGRLDDNGEQIVINSGDKLHTYIGQNIELELRTQDVIHSYWVPAMRVKQDLLPGNPATGGRPTELRFTPVRVEDETYPAAYPIVCAELCGDGHGRMTGEVIVYADESHFLEQFYEPAIYAILNPPADPVLRGEILIQEYICNSCHTLDSLEWSSRTGPSLNGIADRAGERVPGQSAEEYLVQSIWNSQAFTVPGYTEQMAAFGPDQTDANAMNAEQLYAITAYLCTQGEQTDCDTENQTTAIPAAIKTSFGLDVDITFGQSAGEAGTTETADEG | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
EC: 7.1.1.9
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Cell membrane
Sequence Length: 431
Sequence Mass (Da): 47045
Location Topology: Multi-pass membrane protein
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A0A814HJN9 | MTMDEIFARAKSILVIWTAEVNPENLPIFQDVVQTKAKQASTAFENVEMLVESGRSSSSFDIILFGLVSKRNTHIDIDILNELFRLLRPNGYLIIHIEHTKQSQIIDQFKMCGFSSCNPLDTNSSFLIENKDDDIKKFGSLWLCQKPSFDIGYSVPLRSTTTDSRMGQISSSSSSTTTTTGEKKTWTMEDDDLIDTDELLDENDRKKPDVKKYDCGTTSTGVRKACKNCSCGLAQELEQEEHTAAKQTVKSSCGSCYLGDAFRCAGCPSRGLPPFKPGERVTLPTMSDV | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Subcellular Location: Cytoplasm
Sequence Length: 289
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Sequence Mass (Da): 32145
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A0A183VC60 | MFTPAAKSIAKPSACDSPYEMFTPAAKNIAKPRLFAVAKPLCFVRRISSSTSKGGGGTKKLLIGTTVLLAGAGGALAYGCYNTEFRNRVEEVMPWTKCCFERTEHLLCKSKCPKRASVVNMDKKDLDASFVAKKNKELEAALIAAIETAESKVRAAKDSKLKTITSIREHAALLKKAVDDRENGDWSRVSKALDKAETFAKTDRKDEVEARNSLDALKEISFNGKNCSYTSGNKLIVLAMETAKKLNQQIDELNLLAEASRTRSRLLTQYKALVDESRKRFAKQLRELSQHIDVQDKKTVADEAKAAIDHARAEVDSLYRQLIEQQLEAEQKIAEAVEAQRLTSSKLAEQELKSEQDRTRRSDADHNAEVSFINLRV | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 377
Sequence Mass (Da): 41929
Location Topology: Single-pass membrane protein
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A0A1D2AF85 | MRALALLCVLLGALGSPCLASSGDEAPEYRGCLYHCVEGSGGRGQVHSPLCVPGDGDQGSAAPPIILRWTAWTCETDCGYLCMWAVEGPEVRAALQQPTPRHPTPWRPTPPPHAHAAQKYHGKWPFTRWLGLQEPLSSVASLLNAAAHARALRALWRAGRRGGPPYLAHCLLSLAAWLASAAFHARDTRVTERADYFLAGAVVALGVYVTALRTLRCVGAAAPRRRAALGAVLGVAYLARVHAMLTRRFDYGGWVVACLALGLLQTLLWLRWAWWTREGATHPSRRSLLVFIASLNAASLLEVLDFPPLLWHTLDAHAVWHLATIPLWALWYRFVLLDLQAGQVMWSLPLDSAGEDKEL | Function: Involved in the lipid remodeling steps of GPI-anchor maturation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 359
Sequence Mass (Da): 39282
Location Topology: Multi-pass membrane protein
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A0A0N5CNN2 | MKTEYAKIYLFIFVLLQTQSECYKILVYNPKLSYSHVKFFGQIADLLVEAGHDVVTYMPDAATGLTFNGTKLARIIPGPPLIDNSTLLLEDIIKNAWDERFFDFFSIIKRIKQQMETHIQTCSGDLKSVISAQVSNNESMQQLREENFDFGITELISPCGYAVFHKIGLTNYATAFATDILAVLSSSLGVNSNPSYVPNSMQDAIQKSSFAFINSDQLLQDQHLSSPKLVYIGGIATTRPKSLNKQFQDILNKSNSVVLVSFGSLAKSSNMPQHIKNSFRETFRSFPEITFIWKYEEDDQFAHELPNVIKKQWIPQQELLEHPKLKVFISHCGQNSVEESVQGGVPLLCIPLFGDQMRNTGKVLRRKIGIFVDKHHITPEVMKNALLEILYDKRYLETSLNLREMIKNKPITPQESLLRHINFASKFGPIDNFDIALNKLSFFQYYLLDILIPLLAVFVFLLYFIFRMFRNILYKLLIIWKAKTD | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 485
Sequence Mass (Da): 55601
Location Topology: Single-pass membrane protein
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Q6DEU2 | MAPKGGNKQQSEEDLLLQDFSRNLSAKSSALFYGNAFIVSAIPIWLYWRIWHMDLVQSAVLYTVMTLVSTYLVAFAYKNVKFVLKHKVAQKREDAVSREVTRKLSEADNRKMSRKEKDERILWKKNEVADYEATTFSIFYNNTLFLVLVIVASFFLLKNFNPTVNYILSISAASGLIALLSTGSK | Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 185
Sequence Mass (Da): 21120
Location Topology: Multi-pass membrane protein
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A0A6N9GNX3 | MSVTPPNLFQFASDHSNEEFANPSDLAVLLNAIGSAGKFISSEINRAALRDFFGSAGAANVTGDEQQKLDVIGDNVVAEALLSTGLVCAMSSEENAGMIDCGDAAITGEYTVVFDPVDGSSNIDVAAPIGTIFGIYRRLSEGSPAGDTDILRPGNEMLAAGYVLYGSSTIFCYTSGDGVHFFTLDPSLGDYLLTNENVRSHGSSHVYSANEGNSGKWNVPDLNWVEHVKSESYSGRYIGALVADFHRNLMKGGIYAYPGDKSSPDGKLRLLFECAPLAFVAEQAGGAASDGTTPIRDIYPDQLHHRTPMYIGNSGEVALLEGFHKL | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
EC: 3.1.3.11
Subcellular Location: Cytoplasm
Sequence Length: 326
Sequence Mass (Da): 34636
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S6BUF4 | PLSSNLAHGGPSVDLSIFSLHIAGASSIMGSINFITTILNMQHKIFNMEIIPLFSWSMLLTAILLLLSLPVLAGAITMLLFDRN | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 84
Sequence Mass (Da): 9066
Location Topology: Multi-pass membrane protein
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A0A183UY96 | MNAEFLLFVLIAIHSSNICAKQMKFLFYSPSLGHSHLQFVGTLADFIVDAGHIAHVLIPDLGPHLKENGTAKAQRVIRITPSRPSPYTQFDLVKNAFMANVTSFDSKSFQMLTNMSLMLCEDILNDDRLIDELRAERYDLGFTELYDYCPLGILHHVGVKSIALLSAVSISDLLADSFGLPSPSSYVISWYKPFISAPELSFLERLENFVSVTAMRIIHLPQMLMTENMMFRRLLGPNFPDLRLLARNASAAFINTLHIFDLPRPISSKVIFIGGISVKKPSTLSKQFSDILDRPNSRVVLFSLGSITRTKAISFELKLAFLEAFAHFPEYDFIMKLDVDPESAKLIAKYRNVHYFKWIDQVNILKHPSTKAFITHAGANSMIEAMFSAVPLVCIPLFGDQYYNAVVATRKNVAVFVDKTTITSDKLIDALDKVLNDSRYAENSRILREKLEKYPLNSKELFIKWSEYLAEFGDFTDLNLMIVRLIVIAWSLLFVSHGLKILVYQTALSRSHLMYSGGLVDILVDARHEVHKLIANWNPTISDNGTKKATSVYRFTLSKPSPWLKINHFSEPFEAKVINYHMDSREAALHWQTIAEFCKEMLADEKLLHWLQNSNFDIAISTTYDFCVFGLFHVAKIKPVIGFLVTPISDIVLYALGISNPASYTQDSFYPSDNGDQMTYLQRVNNLYTRTLMQQIYIPRFIAMQDEIFHGKFGKRMPSLQTLFSQMSYIFVNAHPLVDYPRPLSHKSIFIGGIQLNDAGQLPQEFDRVLSMRPDGAVLVSFGSTALTSKMPKNLKRIFLEVFAAFPQLTFFWKFDEPHDKSSFTNISNVYMAKWLPQKQLLGDKRMKAFITHVGLNSLMESIHEGVPLVGIPLFADQLHNAGIIRKRQIGIVIDKRNITVENLRNSLNDVLYNDRYRQTAKMLSAMIRKNPNNPTKTFLKYVEFAAQFPNVGEYLQLQSTNLSSVEYFCIDIIVPFIFIAITLLYFCFKALLIILAKCMQREAKDKFE | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 1009
Sequence Mass (Da): 115030
Location Topology: Single-pass membrane protein
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A0A6N9GR67 | MYQRNNSLTSKPRSESPELKLRLISAAVGLPLLGLTLFFGFWPVSVVAIAVAAVVGLETQQLAFGKSKSVAPKGSAALVGAFIAGLGVFGAALGELKIDYSSADTAERIVVVILVVLVAEFLITSRFARYQAISRRKLIISYGIIVVLAVTLLPFIVSSDGGHELLAYGILVMFAADSGAYFVGRSIGRRRMAPNVSPGKTWEGFAGGLVAAVVASLLLSNLLSLDFSIVKIVVIGLVIAALGVVGDLTESWVKRLADVKDSGGIIPGHGGILDRLDALAPIFVFIYFIV | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 290
Sequence Mass (Da): 30516
Location Topology: Multi-pass membrane protein
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A0A183UL14 | MNDEERAALAKKLDEDLDLFVENLASKKKVEGERKPFDFDEWCRELDQHPAFMTELRPNEQGEYSEAVQALQALKYEDSETEDRVERAEWHKEEGNKHFKYKKYRWATDCYTNGIKELCADRTVNSVLFANRAAAQVHLGNLRSATRDCVFARRFDPTNLKAIIRCAECLIKMGYGKQCIEWIDSSKVLLAKSPSNSLEGEADRRVEQLKRVDELRLQAVQSAIIEERDERKAKAVMAKEMQKKKRLLAAFAARNLHFKPTIHFDDASLFEWSQIEVRLPQTKAHEQVYLDEEDVLHWPLLIQYPEHGQTDFFTECSEMNTLEELLQPLFQNAAHWDRDHDFRQENVRLFVSLDSDENELNEVLLSDTLREILSMEHFVIVHGLPVVQVLAMKRKVTKESPKVRFSECDDDSSKVDISSGRSRSLTDDQSDEADESDLHTTSSHRIRRTSRTEAERMYYQMINERVVNDVTLEFFYKPHTVTALIAICAFLLAPAFTREDAHTDNNALTGLIATAVLFLVVSALAFPNGPFIRPHPVFWRLMFGFSVIYMMILQFALFQNFRDIKLVLKWLDPQGLSREKLEEKAYAVNCSDITLERLWSYMDIFAVGHFLGWAMKALLIRHSIICWYISIAWEITEVVFAHLLPNFQECWWDAIVLDVLVCNGLGIWFGTWVAHFFEMRQFHWESIKDIKTARGKFKRAVLQFTPESWIKVDWYNNFALRRTLSIYAFVMIWLVSELNTFFLKHIFAVDTSHPLVFWRIVLIGFISAPSIRQFYLFATDPRVKRMGMQSWVYLAVCALEAAICIKFGRPQFPHIKITFILIWIAFLAVGTFGCVWLSVWWARKFAPTKQVNVGGRLRECYLDSSYENLGAIADDVRACRKRLQISESDFN | Pathway: Lipid metabolism.
Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) is replaced by L-serine.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
EC: 2.7.8.29
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 891
Sequence Mass (Da): 103774
Location Topology: Multi-pass membrane protein
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A0A183UMP0 | MERCHSLTFDTDTYSSTSIVIAYHNEARSTLLRTVMSAFLRSPAKLLTEIILVDDFSDDGLMRSRIKGAQLASAPVVTFLDSHCECNVQWLEPLLARVNENPHVVVAPVIDTIDMNTFDYAAGNANLRGGFDWDLRFQWQNLSSTLRDERRANPTLPIKTPVMSGSIFMLRKNWFETLGTYDPMMDVWGGENLEFSFRVWQCGGSLEIIPCSRVGHVFSTQRSQTFRGGRLSVFERNTRRAAEIWLDDYKQFYFARVPTARFVDFGDISERLKLKERLRCKNFTWYVSEVYPELRFVFIYFLYVDEIFFDNIVDFISSFLFFAFLSLCARFH | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 332
Sequence Mass (Da): 38608
Location Topology: Single-pass type II membrane protein
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A0A803JQR9 | MGEHWYHADMSQAWAEHLLIRDGRDGAFLVRQSESVNGAFAICLMYQHMIHTYRVLPDDCGLLSVQSVQGVDVKKFEHLSDLVYEYMHKQNGLITALQYPVGCEAELSTEQVNDYVETMKSPGWKDISYTGTRIVSCQRGMALGTQRTLLQEDVEDTRKQGLGLFHLSPLLEKQCRELDREIGVTWNSLRVLTKVFGQMISDFNSEDEQMLDRLMNNISAVHEIIASLENKVVQTLKDSLTSFATSPASRGSMSPRVPVTATSNRTGKTDPQDGLQQDRNQPKKNCPKSLSLFVGTWNMGGSPPPRSISSWLSSRGLGRSLEDTGPCVSHDLYMVGTQENPQGDREWAEFLRLALISHTGKQFKVVSMHSLGGVKLVLLVKQEYESLISHVQISSVRTGMSNTLGHRGAVGASLDFCGISLGFVTCHLVSGNEKVQKRNQSYGEILRGLTLGDESLKCFQLPLRLTHLFWAGDLNYRLSMPLQDILQCVYSGRYQVLLPVDQLSQERERKKIFLGFKEDSVTFPPTCRYERGTRSYDLHKARTTGTRLFAPCWSDRVLWTSYPDTDIKCTSYGCTEDIVTSDHSPVFATFEVGLDCTSQQDTSCTVRFQSIEAIIKTQSRSKGFIEFRSVCMRGSPQSKENSTHSTEGSAFLKLGWSDLDLPEITLVGQDRRSALTRHILFNIRSTDGGESYGECCVSVNPLNSGTDHHFQAFLSQRGEETGSIRGWVIVSRFLDVNPLKSPNTLQGDNEKGLSSVRESSSLLTCAPVSPRNPSASQLLARTARRRPASLCCVMESYSNAEYFLFEGMPSTPTSPRPHSALVSGDHQSSGLHGRQFDLRPEMGKNSALVPISKPSKATSRSLASHKGC | EC: 3.1.3.86
Subcellular Location: Membrane
Sequence Length: 868
Sequence Mass (Da): 96542
Location Topology: Peripheral membrane protein
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A0A815E2L2 | MDIHSLMGRASTMMSGKRNDDSMCDRLNYRYTVAILVIFAIINMNRLYTDQIKCWVPAFFTPNYDEYVRSVCFVQNTYYIKHTDKVPKKYENKKENEILYYQWIPFLLLIKAFLFYIPRMSWNTFGLKSGVQISDLVESSFDYKLPTTDAIHRQMCLKYVIDTIDDYCNDHRRQINTRKHLNIFQRILTAGWCLTGIYLGNYLVVLYTTTKLMYIGISIFQIFILSILLGSNFAFYGVRVIDRLFRGISWDTETRLFPKTTLCDFTVREFGHPKQAHEYTVPCVLPQNLFNQQMFTLLYFWYAIVILLNIADFVLWLYTISLENRRSFICKRLHSKKYPLTDKTKDQEKIKIFVNDYLEADGFFMLTLIKENSSDFVATEIIYRLYTEKFLEKYFKETTTTTIYDAIDIKPYDDYTNNTKRRQPFCSMIC | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 430
Sequence Mass (Da): 51243
Location Topology: Multi-pass membrane protein
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A0A0A9YPJ0 | MITLLSNFSMAGVDALRWPDTDNAFKGVPADAIVDTWFLMSSPTPILSLVLFYLYFVLSLGPKLMESRKAFDLKYTMVLYNLYQVVFSSWLCSRLIFSWAAIKYIYNHACMPMDRGVNPLVSILNDSTWWYFMSKVVELLDTLFFVLRKKQNQVTVLHVWHHSNMVLSTWIYLKYIRGEQAILPGFINSCVHVVMYSYYLLAAMGPTIQKHLWWKKYITKLQLGQFLTILCYLSLLVGFDCKVPSGLTAYIALNTTIFLVLFLNFYRQAYTKKDRKDKKNFCLPEQTQTKPVKAE | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 295
Sequence Mass (Da): 34347
Location Topology: Multi-pass membrane protein
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A0A3B9RUI7 | MDERPNHVQMPIYKATKQRLMLSFITGLLLTMLGGYLYISDAQRFPLRVIKVKSTFTHITPEQIQTILTPLTQKSFFFLPISQMGHHLMTLDWVEQVRLTRHWPDTLTIFIQEKTPIAHWNEALLSTKGDLFGQRTQLDREQNLPFLYGPPDNHQEVLQVYQKMSNILKMCQLKPSALTKRPNGAWMLTLVNNTVLYLGKYPLTLRLKRFCQAYVTILASKSQQITHIDLRYPHGMAVKWKSEIENHG | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Subcellular Location: Cell inner membrane
Sequence Length: 248
Sequence Mass (Da): 28903
Location Topology: Single-pass type II membrane protein
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A0A6L7JHT5 | MDRSRPGQGGDATRLRAGAVKQANRPSRIWLVGLSGSGKSTVARELAALLDWRVLDSDQEIRNLAGMDIPEIFDVLGEDHFREMERSIAARAAEACRVVVATGGGQMANGCLAEVMLGSGAVVYLRARPRTCASRLATQLGTEGRPMLGGEGSLTKKLDSLLKRRRPIYESAHHSLDVDGTEPRRLAMNIREMLDADPA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 199
Sequence Mass (Da): 21536
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A0A6T6YAQ3 | MSKAIPQLDSKHPFVYKTLKTRLPGILERTIEYNKETLTKDQIESIQHFLKEIVNDAPIRLISDQKEDAKEWNKVLQVCVDKKQTWTTAPWFVWETYVYRRLLQASQYWDTKLDLFKIEKSKSLIGTEQALKQRAKISTQYAGKWDYDTFRVILFQDLWGNQADGSLFTVDTIAGLGSTKGHGENTDRVLVNDTKSVWNHLNQPAKQGHRVIFFNDNSGLEIVSDLVLASYLLHSKKVSTVEFYLKPYPYFVSDANPEDVKDTIEFLISSHDKSMKELGADLKSLVKANLLKLKKEHFLASPLAMSEMPKALKEDIKSAHLLVVKGDLMYRKMLGDRMHPPQTPFKDIVSYFPCPIVSLRTCKSPVIVGMTKKVFDELSAEKKDWTCLGLHGTIHFVNSSSAR | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism.
EC: 3.1.3.-
Catalytic Activity: beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate
Sequence Length: 403
Domain: Subfamily III proteins have a conserved RTxK motif about 40-50 residues from the C-terminus; the threonine may be replaced by serine or cysteine.
Sequence Mass (Da): 46147
|
A0A0A9WT63 | MFTILTVVVLATLSQAYKFDRYDLFMPDVVPKKMDVYLCSPVRVNYTRHYYIVGFEPNASMDTAHHMLLYGCKVPGNDGTVWNCGEMANEDGDETHSPCAEGSQIIYAWARDAPQLILPEGVGFKVGGDSPIQYLVLQVHYLHVEKFKHGATDRSGITLRYTEQKLSKSAGVLLLGTGGRLKPMSEVHMETSCAIEEDKILHPFAFRTHTHQLGRVVSGYKVQNNSGEMEWTLLGKRNPQDPQMFYPIKDPSLTIQKGDIVAARCTMFNKNNETVNIGGTSKDEMCNFYLAYWVSNDEPLENKYCFTSGPPSYFWESGLPGYPSLNNIPDIDASTL | Cofactor: Binds 2 Cu(2+) ions per subunit.
EC: 1.14.17.3
Catalytic Activity: a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a [peptide]-C-terminal (2S)-2-hydroxyglycine + H2O + 2 monodehydro-L-ascorbate radical
Sequence Length: 336
Sequence Mass (Da): 37707
|
O21829 | FGSLAGLWLITQILTGLFLAMHYTSDITTAFSSVAHICRDVNYGWLIRNLHANGASFFFICIYFHICRGLYYGSYLYKETWNIGVILLLLVMMTACVGYVLP | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 102
Sequence Mass (Da): 11570
Location Topology: Multi-pass membrane protein
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H9A9G2 | MLWSSNDVTQQGSRPKTKLAITGVELKISLISATSENGVIGNGPDIPWSAKGEQLLFKALTYNQWLLVGRKTFDSMGVLPNRKYAVVSRKGISSSNENVLVFPSIEIALQELSKITDHLYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDINFPKIPENFNLVFEQFFLSNINYTYQIWKKG | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Sequence Length: 182
Sequence Mass (Da): 20305
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A0A2S8MN13 | MPNSSPLTAWKALKEGNERFVAGKAQHPSQSIEHRASLTSAQKPTAVVFGCGDSRVAAEILFDQGLGDMFVVRTAGHVIDSAVLGSIEYAVTVLNVPLIVVLGHDSCGA | Function: Catalyzes the reversible hydration of carbon dioxide to form bicarbonate.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 109
Sequence Mass (Da): 11416
|
A0A0A9XD33 | MTIADIARRAACELPYNGVKDRLVVFTQGNLPTVYATRSGVYGEVTVSLIPPEKIVDTNASGDSFVGGFLAAFAFGRDVARCCEAGNYAAGEVIQHDGCTFPPVPKINL | Cofactor: Binds 3 Mg(2+) ions per subunit.
Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.
Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
EC: 2.7.1.20
Subcellular Location: Nucleus
Catalytic Activity: adenosine + ATP = ADP + AMP + H(+)
Sequence Length: 109
Sequence Mass (Da): 11554
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A0A089PSX2 | MQDRNFDDIAEKFSRNIYGTTKGQLRQAILWQDLDRLLPACGAGPLRILDAGGGAGQTAIQMAERGHHVTLCDLSSEMIALAKRAADEKGVSHRMHFVQCAIQDVAQHLESPVDLILFHAVLEWVAEPRTVLDTLWSTLRPGGALSLMFYNANGLLLHNMVATNFDYVQAGMPKKKKRTLSPDYPRDPQQVYGWLQEAGWQITGKTGVRVFHDYLREKEKQRDSYAQLLELETRYCRQEPWISLGRYIHVTARKPQVDTRTNDE | Function: Catalyzes the methylation of 5-carboxymethoxyuridine (cmo5U) to form 5-methoxycarbonylmethoxyuridine (mcmo5U) at position 34 in tRNAs.
EC: 2.1.1.-
Catalytic Activity: 5-carboxymethoxyuridine(34) in tRNA + S-adenosyl-L-methionine = 5-methoxycarbonylmethoxyuridine(34) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 264
Sequence Mass (Da): 30033
|
A0A3D5CC12 | MAAPSKKKRSRSRTKPHPGSTNHARRDHRSPVAAPKPATLRDWIGAARLRTLPLAVTPILIGTGAALLIERPMHWVIALACLVVSVSLQIGVNYANDYSDGVRGTDAYRVGPARLTGAGKAKPRTVLIVALVYFAIAGLAGLAITIRTEQWWFLAVGAACILAAWFYTGGKRPYG | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Subcellular Location: Membrane
Sequence Length: 175
Sequence Mass (Da): 18779
Location Topology: Multi-pass membrane protein
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B7PA38 | MASSSKRIVYVGGLAEEVDEKVLHAAFIPFGDVVDVQIPLDYETEKHRGFAFVEFEQAEDAVAAIDNMNDSELFGRTIRVNVAKPMKIKEGSTRAVWSEDSWLRQHAGETLNEDEEGAATAETEDKAKANPQVYFDVSVDGQEVGRVRILLYKDVVPLTAENFRCLCTHEKGFGFKKSTFHRIIPGFMCQGGDITNHNGTGGRSIYGKKFDDENFELKHTGPGMLSMANSGPNTNSSQFFLTTAKTDWLDGKHVVFGQVISGMEVVKKIEAYGSSSGKVSKKVEISNSGELT | Function: Catalyzes the cis-trans isomerization of proline imidic peptide bonds in proteins.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 292
Sequence Mass (Da): 32131
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A0A6P7G5X3 | MLSNRSKLILIGVSILEMTIIFIIFEGSKLKDNICCNSSKPVTFLGSVDDYYRLLNISFKFSVMNQVCHENTPLLALILVFSATSNVKKRHTIRSTWGQVGKNKKLLFMLGDPGSPKQQKDLEVESLLFGDIVQGNFRDTYKNLTYKHVMVLKYFVYHCPQAKFLIKTDDDVFINWPSMENFLTYDLSHSSDRPTIYCFRKTGSPVERSNSKWVVTYSEYPEAVYPPYCIGCFIIYTPEVIFSLYKEAQRSNSFLWVDDAFITGILFKKLNYSHTDIEFLMLSDENFYAILRKSTNVEIKPFLFRLLHYETEMKIVWEYISNQVPPRSIYKF | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 332
Sequence Mass (Da): 38776
Location Topology: Single-pass type II membrane protein
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A0A0D6XSJ8 | MQTEWIHAMGTTIRLSIRHTSATALLTEAKKRIHDWEQRFSANRADSDLMQINQQAGKQPIQVESELFNLIEHGYHVTISSQLKMNILIGPLVKLWRIGFNDARQPSSSEIATALKRINPKDLQLNPQKQTVYLQQPGMELDLGAIAKGYFADELKAFFMSQGVKTGIIDFGGNVVTIGTPLKAKYWHVGIQHPFETRGTPIETLRVVHQAVVTSGIYERCFTSGDSVYHHILDAQTGYPVENDIASVTIVSDHALDGEIWTTICCFGYAAQNIALLEQLDGIEGVIVRKDGEVLATQKVNRLPKN | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 306
Sequence Mass (Da): 34120
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