ids
stringlengths 6
10
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stringlengths 16
1.02k
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stringlengths 117
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A0A7R9QFE9 | MLILWNTILAVFSIIGFTRCAPQFWHLYRTKGFMATICQSDYYRDIRVLLWYYLFVWSKVPELIDTMFIVLRGSKLINLHWIHHCLTLVYSWYSIGDQPATTQWMITMNYGVHSLMYTYYVCMACGWRLSRRLSACITSLQVVQMMAGFYINYVAMNRKLNGQPCDVSLHVAKTGVTLYALFMVLFMNFFVKSYLLKPLSVKPTRVKRD | 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: 209
Sequence Mass (Da): 24632
Location Topology: Multi-pass membrane protein
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A0A7M7IY06 | MKRRLSQRLKRKRFVCALAVGLFLIICIIKQSNLRQITQSKLLQIFSAGKRSAAFYIWDDNTTYSWMKSFKSGNYNYTELLRPKGVYKGIPYLVVVASGIMNRLRRSAIRDTWAKGLRDSDGAEAAVVFLLGRSEIQYFQKLVNTEHTQYGDIVQFDFKDTFRNASLKTVLMLRWASKFNPTYLVKADDDTIVNVRKLRLELQSLQANFSKPVIAGYELIHVAPRRMKNDKWAVSEKEYPDKLYPNFVSGCLYVISGKALAPLYETALNTRPLSLEDVFVTGLVATRAGIPRVSLKDIEILGLDEACEMHEKLAVHHISASRMRLLSRVLSSFVRHCTSLSCSCIPLASPQLKATSK | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 357
Sequence Mass (Da): 40558
Location Topology: Single-pass type II membrane protein
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E6Y3R7 | DLPTPPNISSWWNFGSLLGLCLITQILTGLFLAMHYTSDISTAFSSVAHICRDVNYGWLIRNMHANGASFFFICIYMHIARGLYYGSYLYKETWNIGVVLLLLVMMAAFVGYVLPWGQMSFWGATVITNLLSAVPYMGDMLVQWIWGGFSVDNATLTRFFAFHFLLPFIVAAMAILHLLFLHETGSNNPAGLNSDADKIPFHPYFSYKDLFGFMIMLLTLTLLALFSPNLMGD | 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: 233
Sequence Mass (Da): 26230
Location Topology: Multi-pass membrane protein
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A0A832CY44 | MPKLRGLDEWVKFKQRILRGIWEDRLIGYLDPGAEEFLVLLNKPTLLATTSSCTGRITIIEGKWHWLRDEARIVFKSHSPIESRDIVSVVKLLGSSDLWIKVTGPIIHFRTPRLLCAMRLLSHARSSGFKHSGIISINRRLGHVVEVMSGVQLMIPLASRGSPLISIDELEKLIVTINEALVEGRRRLEELSLRISSEPGPCEL | Function: S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wyosine derivatives biosynthesis pathway. Probably methylates N-4 position of wybutosine-86 to produce wybutosine-72.
EC: 2.1.1.282
Catalytic Activity: 4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine = 7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 204
Sequence Mass (Da): 23046
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A0A438JB79 | MASGNTYSDDMWSKSEVIDPPQSEDMMEVSEHVNDPVHTTLKPNVTISSSVQELLEYPVCLNAMYYPIHQCSNDHTWCSRCKSRVHNRCLTCMHELGNIRCLVLERIVMSLELPCKYQSFGCLGTYPNYNKLKHESQCVYRPYYCPYAGPECTVISNIPYLVTHLKDDRKIDTHNGSTFIHCYVKSNPHEAKSCSYSLEVKGTGRKMIWQRVPRGIRDNHRKVPGYNYLKHV | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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: 232
Sequence Mass (Da): 26816
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A0A072VLT5 | MHHMLVLMDILSNRAKADANANADSNKICSNDFECNICLEHVKDPVVTLCGHLYCWPCIYKWINSTSWEHNEKPECPICKSEISESTLVPLYGRGKTTSSSEGEAHQDGVVVPPRPLGPRSLDTATVSQPELEQAEAEAEAPPAQESSLHICLQYGPYKLDFRKFD | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase.
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: Endoplasmic reticulum membrane
Sequence Length: 166
Domain: The RING-type zinc finger domain is responsible for E3 ligase activity.
Sequence Mass (Da): 18487
Location Topology: Single-pass type IV membrane protein
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A0A0R3WA74 | MPGRGKTLLVGIAYTLVLCGIVHCFVNQVQPTAYMDEVFHEEQTITYLHGNWQKWDPKITTPPGLYVLTTFLWNLLPFQACVRNFRFLNCFIGGANFIILAELTQSILIALSIATLPVLFFTGILFYTDQLSLLALLLTILAQRSSHTVPALLFGCFACFVRQTNVIWLAFMIGQVAVQRLASTQTCVRKSALQWCIYLIKHPVDIFTALVKAALLDALHHTATIVLFVTLVLVFNQGDIVLGDRSAHKPVFHVPQIFYFFVFCALHTPIAFLHYLHTNLHVPRRLSLVWITLLLFMTVVSICFFTVEHPYLLADNRHYTFYLWSRLFRRYRSFRYTLAPVYLICGDYVCRGLRGGSLSEFLTRLGYLMTVALVLIPAGLIEPRYFITPYVIWRLTRPHIYKKLSSPVMEVAMNAIVNAVTVHIFVFYPFKWLSQPFTWQRFMW | Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
EC: 2.4.1.256
Subcellular Location: Membrane
Sequence Length: 444
Sequence Mass (Da): 51184
Location Topology: Multi-pass membrane protein
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I1S1M7 | MQPLICLLTISSLAMAFDQSARQSKRQLSGRVRSTANEFKDDGCNDIIFVWARGSTEIGNMGTIVGPDVANNLKDAFPGQVAVQGVDYAALLSTNFVPGGADPVGIREMESILSDAMSQCPDSVIVTGGYSQGAAVNHRVIEDLPQDQQDRIAGVIMFGDTQDRADGGQIPNFDPAKTEIICASAPRDTVCDGILTAAVLPPHLSYGRNAKEGADFLVSQVRGVLGAGAK | Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle.
Catalytic Activity: cutin + H2O = cutin monomers.
EC: 3.1.1.74
Subcellular Location: Secreted
Sequence Length: 230
Sequence Mass (Da): 24225
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A0A7R9L877 | SYCVWHQRSWIIQNMSTPDLKTEISLCNKFLQFDERNFLCWDYRRFVSHLAGDNVESELEFTLHKIQQNFSNFSSWYYRSCLFRSAANNHSYDFSKQWKQEYDLVENAIFTDPTDQSAWFYHKWLVSTNYGRNILPSKQLDNENSVKINRIVLNRSQGLLVLNLSRPLKHKPLVSVVVNDKMLTNCDWNSPNDTDSKVWFIHLDPFPTTQINGLTISPIPTFAKNPELVELIDLKLDSNETNEKHLFVWERKSHNLDQQWTLEESYLKTLRELHKLEPNNKWVNLTLAWNEPNKSETGSIFDTLIKLDPLRNNYYNDLSE | Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences.
EC: 2.5.1.60
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Length: 320
Sequence Mass (Da): 37960
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A0A945UHE3 | MKILQWIDRLLVVTAVAALTLLMLQICVSVTARYIFNSPVPDDLVISEFLMVFIVFLPLSSVQAEREHVFVTIFTEWMSNNTKVILETFGVFIGLIAFAVLSAATFADFKHAWDYGSYVTGLWELVEWPPKFAVFFGIAILTLRLAVDAVQSVRGIVKGTATATRSEEDRVLDAEF | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 176
Sequence Mass (Da): 19713
Location Topology: Multi-pass membrane protein
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H1ZZX8 | HPEVYILILPGFGMISHIISQESGKKESFGTLGMIYAMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGTKLIFSPTTLWTLGFVFLFTIGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGLVQWFPLFTGLSLNNKLLKIQFTTMFIGVNVTFFPQHFLGLSGMPRRYSDYPDAFMMWNIVSSLGSLVSLSSIIFMIYIVWEAFTAQRKSLSSMNLSSSIEWLQKNPPTEHSYSQLPVVSV | 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: 274
Sequence Mass (Da): 30539
Location Topology: Multi-pass membrane protein
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A0A4S2KRD3 | MSTDGFSDHDDTDFISQFQAMAKNLTSENFSGYAGTAIDSSEMSNTPDQPECIKKWAIEFEERIRIKDGNEQKKLSLLEEQGSKDLHNWAMQYRESLSRAIKDSRAHEKELRAEQTAAAEASSSISGADASQAVLWDRVCQLCSFVSPNPEDGSSTPPVSRHPGTKDPSKDLNRMRILLLQLKQQPPAIHRNAIHAN | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular Location: Cytoplasmic vesicle membrane
Sequence Length: 197
Sequence Mass (Da): 21960
Location Topology: Peripheral membrane protein
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I1S320 | MGSIDKDYAPSRLPLEDSVSLLSGEDFWRTTPNKALGLGSLKFSDGSNGVRGEDWINGAPSAAIPCGTALGASFDVELVSRLSNLLARECKRKGVHGLLAPTMNIHRYPLCGRNFESFSEDPLLSGLIAASFVQGLQAQGIATSPKHFLANEAENGRRWSDSVIQERALREIYLEPFRIVVQKADPWAIMTAYNSVNGSFCSESKTLLSILRGEWHYNGVVISDWFGTYSTVEAFSAGLDLEMPGPTKFREQDKVLGLLKRDEIEKRQIRDSASRVLDLLQKTGRIGQPGHPPPSKAEEPEYLDNLETRTLLRQAAESSMVLLKNEGSTLPLVNRRTKLAVFGRHATEPSLFGGGSASIKVPYSSTPWDAIQETYHDAALGPGVAIERLVPLPNECGLELGDITLTWYNGDTVSDSARFFSQQLKDTLYMLVEHAPGGLIDRSNFCTSMKFVFTAQHTGPFHISLSGPGNAQCLVDGEIVLDVQRGLDISTEDFLFDRSKLEVSRDKPLQLQAGLRYNFEVVNWSSKHKAQNVNREFFIQGCRLGLSPARDDDKALIDAERLVETVETSIVVVGTGTEWESEGFDRVSMQLPRRQDELILRVAEKCKGRTIVVVNAGSPIDMSGWIDHVDAVVYAWFPGMEFGSALARLLSGEVSPCGRLPTTFWDKVEDYPAGYVEELMTADRKIQYREGVFVGYRQESLQSYTPRFSFGHGLSYTTFSCSVKSHTASLVQNSPSFTDRIILTLQNTGSITASETVLLFMEAIDPTTTRPRVELRGFAKTRLLEPGHSQDLEFILKPRDFAYWDEKAHLWRIDSGSYKVHVAGSRGVGDWRDIEDVIVKFAEGITIP | Pathway: Glycan metabolism; cellulose degradation.
EC: 3.2.1.21
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Sequence Length: 848
Sequence Mass (Da): 94075
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A0A2E8B683 | MVRDDVKRDDYESAFELARLLSENGCDERVLPNWAGIAAFCTNHFDQAEKHFSEAKVAGVLDVQANSLVAEIATYKQHWAVEEKLREAELAADDLPRVELLTSKGPMIVELFENEAPESVGNFISLVESGFYNGLKFHRVLAGFMAQGGCPQGDGTGGPGYEIYCECDKSGHRKHFRGSLSMAHSGPDTGGSQFFITFLPTPHLNGRHTVFGRLVEGHEVLAKLTRINPQSFGPDAGLDTIDSATVLRKRDGVEYTPHKVK | 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: 261
Sequence Mass (Da): 28708
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N6TKY8 | MKTHRKFTPAKIPRYLPGQVADNYLQDDLSSFNIHRLRVFNAKPLVDCRPPKLNPFTCLNRKRMLEDALRCRRIDKDNKELLKKITTINRVGGRIDSYNPQAYRRINKWSAYNRDMEKLDLKNFALFQLLKDPVSVLSMKRVGWAENNSQFCITFKKMERLDHKNVVFGNVIKGNDVLMNIQYYGRKIGKPLEAIIISDCGECDVAAE | 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: 208
Sequence Mass (Da): 24252
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A0A7Y5XJQ6 | MDLQSRVSDVIADELAVPVAQLTAESRFHDDYGLDEFGIAELVLRINEEFGADLSFADVEAVTTVRDLVDLVIRRTPRSTPHP | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Subcellular Location: Cytoplasm
Sequence Length: 83
Sequence Mass (Da): 9225
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G7KEB6 | MGEMLVVNQKDNVPLIIIRPTMITSTNKDPFPGWIEGVRTMDSVICGYGLGKLACFVGNANTVLDTIPADLVVNCVITTIVVHLDQDPNKFIYHISSSLRNPFKISDLINIAYDYFVKNPWIDANGKPIVTSKRLWLTSLDAFNNYMMFRYVMPLKVSNFVNKIFFRLFQNNTYDNNCKKIRMLKGLAKLYTPYACFKGVFDDTNTENLRRVAKGYMGNGELDFDPTNIDWTNYMMNTHIPSLVKYATK | 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: 249
Sequence Mass (Da): 28489
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A0A072U9H5 | MVQFLYQAEFDPIRWLDKALINLCSCLGDFQKETPSSFSLSPRLSIFPQFMFHLRRSQFVQVFNNSPDETAYSRMILNRENVTNSVVMVQPSLIYSFHSGPEPALLDVAAIAADRVLLLDAFFTVVIFHGSTIAQWRNVITHDFQMYTQGYDHNLTFLTIKGAGHTVPEYKPQEALDFYKRFLAGSPI | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Subcellular Location: Cytoplasmic vesicle
Sequence Length: 188
Sequence Mass (Da): 21536
Location Topology: Peripheral membrane protein
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A0A953YQ09 | MVLTTLAVVVMRYVFNYGQVFIQESYVWMHGIVFMVGAGYALLHDAHVRVDVIYRPASIRYKAWVDLFGVMLLLLPILVILAQVATPYVWDSWDRLEVSREAGGLPGLFLLKSVILVFCVLVLLQGLSLAARSYLILLKYQPFVDAATASANGEE | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 155
Sequence Mass (Da): 17353
Location Topology: Multi-pass membrane protein
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A0A0R3VYJ1 | ADFSSTKLPVIHYDRRFLYHPTTSDGCLYKCIFANITPNLSQGDVAVFSERFPLQKSIFLKRRGVLLAFETGECPLLAPSLLPAHLRQIDLFITYMAKSLVPFVYSVFVRNKNPKYRFTAEETALMLSKNYVHLLPTHHKGRKELIAWAMSNYRPYNNRVEYANAIAKFIPVDIFGRNGMQLPRNSNAFHLLSLNYKFYLAFENSNCRDYITEKGYFNAMQCVTIAL | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 227
Sequence Mass (Da): 26228
Location Topology: Single-pass type II membrane protein
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A0A7M7JHE0 | MANRKMAVAGTSNGTATEAPIQSFFCGKSALVTGASGFLGKVLVEKLLRSCHGLDNIYCLIRSKDSESPQQRLEKVLEAPIFEQTRKCGILSKVVAIEGDILADGLGLSEENRKTLVERVSIVFHSAASVRFDEPLRKAIDINVLGTRRVLELCRDLKSCAAFVHVSTAYCFCNRNYVGEEVYDEKIHYQKVIDASEWMDDETAKNCLSVIMDNRPSTYHYTKALAERLLVEEGRGIPIVILRPSIVTAAWREPLAGWVDNFNGPAGFVIATGKGVLRTMYIRPDSVADVYPVDLVTRMMVASAWYCSQKKFVSPYVINCTTGPLHQLTWRQIFEYSKPIVLANPSMEIFRYPGGSFKESKFWNRIAMALDHSLPAFIADSFAVMFGRKPILGEVYGKIHRAMHILEYFTTHEWEFSIDNVHNLLDHIKHPKDREDFDFDIRPMDWLSFLEQYILGVRKYVLKEDPSTIPAARAKLNSKGGSKCHDISTSKRKPVGSEKYPEKRGPSWTDLTSQAAKGEKAEGRIWWIGTIMQMAVVYGSFRLLMRYSSRFNFLIWNLFSRIVMFAVRINVAVQSSFGKS | 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: 580
Sequence Mass (Da): 65615
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A0A832G0P8 | MRVKVITGSRLHGGFYYIGRSWGVYYGGLGFYSELPKLVLEAWECSDTRIYNLDDFSSVITGVLDKLGLSNVCLMAKESIPIHVGLGSTTQTLLAVGVAIGKLKGINYNIIELAKLLGRGRVSGVGTLLFKYGGFILDSGNPDIGGPRTLLRLRVPGEWRFVILIPEARRGLSEDEESNILREPIEPSSHIKQLMSRGALRLASAIARRDLQEALEGLREVQTGTGLYFSTIQGGVYRSDLEDLVSEASKAGLVLAQSSWGPTLYTITSKESARADANMLLLLMRELGIRGNVLLAKPRNMGARVALGG | Pathway: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin biosynthesis.
Function: Catalyzes the condensation of 4-aminobenzoate (pABA) with 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta-ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P).
EC: 2.4.2.54
Catalytic Activity: 4-hydroxybenzoate + 5-phospho-alpha-D-ribose 1-diphosphate + H(+) = 4-(beta-D-ribofuranosyl)phenol 5'-phosphate + CO2 + diphosphate
Sequence Length: 309
Sequence Mass (Da): 33569
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G7LE88 | MGGLGRTSSLSPLWLWIPIYICVVVVVVCVSVNVSAELQRIEHPAVKADATLSFLVIGDWGRKGTYNQSQVAFQMGRVADKLNIDFVVSTGDNFYDDGLTGVHDPAFQYSFSDIYTANSLQKQWYNVLGNHDYRGDVEAQLSPFLQNIDHRWFCQRSFFVHTEIAEFFFVDTTPFVDKYFLKPKDHKYDWRGVLPRKKYLSNLLKDLETALRDSTAKWKIVVGHHPVRSIGHHGDTKELLTHLLPILEANNVDMYMNGHDHCLEHISSTDSQMQFLTSGGGSKAWKGDVDKNRRDGVKFYYDGQGFMSVELKQMNAKVVYYDIFGNVLHVLNLSKALHYAI | Cofactor: Binds 2 iron ions per subunit.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
EC: 3.1.3.2
Subcellular Location: Secreted
Sequence Length: 341
Sequence Mass (Da): 38895
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A0A099NYM2 | MLTDWIKYVGLPQEYWSFSKYTWALVFLWLSTPTLYVIYSRYQYICRVFERRSNIIVSEQQNEVVIVVLGDLGHSPRMSYHARSFEKLGYQVNLCGYLESNLPDYLKTPDISVYDVPVIKNKRNLPYILFAFMKVSSQFFDLTWLLKDVIDDGTRYVLVQNPPSLPVLLIIGLIKKFWAPHIQIIVDWHNLNWSILNLKYKNENNKMVRFMKMYEKYCARKVADFNITVSQTLKEYLIETFQLKKDKVLTLYDRPSNIFSPLDSREQLKDIVTNNKLVFGDINYNQNNDRILITSTSFTQDEDFTILVEALNILDVQLKNSSSPKRIIMIVTGKGPMQEDFHRMLDSYPWKKVIIKNLWLPIADYPKILKIADLGISLHYSSSGLDLPMKIVDLFGSGVPVITMNFTGISELVKDGINGLIMKNNTDASEMADKISSLLFRDVKRYVTLKEGALLESQRHWNDEWDEKLKPLVCINNHAHL | Pathway: Protein modification; protein glycosylation.
Function: Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER.
EC: 2.4.1.142
Catalytic Activity: GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl diphosphodolichol = beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP + H(+)
Sequence Length: 481
Sequence Mass (Da): 56045
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A0A8T4Z4U4 | MLSKHYEYKRGGVILAGGSSLRFGKNKALVMLNGKPLIRHVIDNSINVVEQIVITIGQKEDPRPFLKVLPQNIKVTKDLRGYKNPLNGILSGITVLNAEYCLVLPCDTPYIKHGVLEILFREADGYDSAIPIWPNGYIEPLIAVYKVEPTVEALRLISVDKNSKVDRLISLLERVRYVDINRFKSVDPYLTSFLNINRPSDLTSAENMPRR | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytoplasm
Sequence Length: 211
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 23846
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A0A0C2S3Q0 | MTMVSQIAFYRRGAGLGENNLGSIVWQLNDIWQGVSWSSIEYSGRWKVLQYALTGIYSPVVAYPFWTPENETLQITAFSDRWEEVQGTATISVYDWSGTLYHRVEKPYTIPPLNNSVLFEASGLDRIFPDLRDPCDIWMLIMTESVVDGNRTVTSEQYFVPTSLATALLVDPEIQITYGQDLTFILSANGGVAAWTWMDHPSGTVGVFVDNVTEQPLNGFYLVPGQDRTLKFVIQTSLSKVKNPDPRDFVIRSLWNNTHI | Pathway: Glycan metabolism; N-glycan degradation.
EC: 3.2.1.25
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.
Sequence Length: 260
Sequence Mass (Da): 29401
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A0A2D5Y9Z0 | MSTQTNSSLKKIRVGILGFGTVGQGTWKHLQENAHFWPKILGVELIPSRASVRSLDKERPVEISKDQLTTDSASIVDDPNIDLVCELMGGVEEAKLLTLRAFAQGKSVVTANKALICEHGEELFRAAEEAGVGYGFEASVAGGIPIIKVLRESLVSNEFPLIYGILNGTSNYILTRMEKEGASFEEVLGDARQLGYVEADEALDLDGVDAAHKAVILAYLAHGIWVNLSEVTVEGIRRISNEDLQAAENLSCRIKLIGVIRRNFTNDHVAVAVHPALIPIEETIARTDGVHNGVCLNGSVVGTVVLTGRGAGQDPTASSVISDLVDVVKGVNGISSLPKLVHVSPEQCQPATPDEIEGRFYLRLAVDDRPGQLAKVAECLADRGISLATVSQTPHEKDKPASLILTTHQTNEHSIAQALAQLKELPGVVDDPVLFRMFDPNGMS | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
EC: 1.1.1.3
Catalytic Activity: L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH
Sequence Length: 444
Sequence Mass (Da): 47695
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A0A1A7Y144 | MVLQSQNCTDGLCMQTAPSTDDVALYVGIVIAVIMCLFISAIVALFVYRKTHRDFDSDIIDTSALNGGFQSVNIKTARSADLLTAPPDLTNAAAMYRGPVYALHDVSDKIPMTNSPLLDPLPNLKIKVYNSSGLVTPQDDLGGDFTSKLSPKITQSLLDNSDTMNLRNQSLARTRDPSCTAHGSFNSQGGHLIVPNSGVSLLVPAGAVPPGRVYEMHVTVHRKDSLRPPVEDIQTVLSPVVSCGPPGALLTRPVILTIHHCAYNVQEDWFIQLKNQLAMGEWEDVVVVGEENFTTPCYVQMDSEACHILTETLGTYCLVGQSIGKAAAKRLKLAVFGPVSCTTLDYHIRIYCLDDTQDALKEVLQMETQMGGKLLDEPKTLNFKDSTHNLRLSIHDVPHTHWKSKLIAKYQEIPFYQVWSGSQRTLHCTFTLERLNSAITEISCKLCVRQVEGEGQIFQLSSTLEEELQCIDTSLMDPASNITTLTGPNAFRIPLSIRQKLCGSLDAPQTRGNDWRMLAHKLNLDRYLNYFATKSSPTGVILDLWEAQHFPDGDLNELAAVLEEMGRHDSTLASMTSEH | Function: Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding.
Subcellular Location: Cell membrane
Sequence Length: 579
Sequence Mass (Da): 63873
Location Topology: Single-pass type I membrane protein
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A0A537F5Z8 | MLPRLLWAVEFIVACGEFVIVFLHTISREAMQAKWIYLPALSCSFRVDMVEVRVSPSLEEAHEELVRAFEARKMVVMVAECSVNYSGRTGSQLGNGERLIVLKEDGCVLVHRGRDYQPVNWQPSGCIFQSQVEKGTLVVKAIRPTPLESLTIVTENMHLLASFHLKDEAAFSLHATEEDMQRAILVQPDLIEAGLKIVDFEKKVAPGFVDIYALDREGNTVVIEIKKDPAGFPAIKQLSEYLKHLQPAPGRRLRPIIVAPSLAKGAQPVVAKMGIEFKQLGLQKAAEVLQSHASSDQKVLKGWLGS | Function: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 306
Sequence Mass (Da): 33963
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A0A7J6GCN0 | MGSADDQFLSTDDDDKLSSLDNTSHVIFDNNYYKNLVEKKGLLHSDQQLFSGGSTDSLVTTYSEDADQFYNDFAKAMIKMGQLSPLTGTNGQIRTNCRKPN | Cofactor: Binds 2 calcium ions per subunit.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 101
Sequence Mass (Da): 11236
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A0A7M7JN84 | MSELSATRQIRVSPTAVRKLYTLFLVRKRDKVLLGMKKRGFGAGKWNGFGGKVDPGETIDQAAIRELKEESGLEVATFHKFAVITFEFVEGDHIMEGHIYTSNEPVGEPVETEEMLPQWYPINKVPFDKMWQDDKFWFPLWESGKRFVAYFKFQNNDILLDQTIREISDDSQKLEPMC | Catalytic Activity: 2-oxo-ATP + H2O = 2-oxo-AMP + diphosphate + H(+)
EC: 3.6.1.56
Subcellular Location: Nucleus
Sequence Length: 178
Sequence Mass (Da): 20657
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G7KYU0 | MWSSVWYGSCPGLKVLAPYSSDDARGLLKAAIRDPDPAVFLENELLLLDKVKYLSFGWLKAKKATFSFDIDRWWSNPFQCFSIG | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
EC: 1.2.4.1
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Length: 84
Sequence Mass (Da): 9579
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A0A6M2Z4V4 | KDIGTLYFIFGTWSGMIGTSLSILIRAELGHPGSLIGNDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLISSMVENGAGTGWTIYPPLSSIIAHGGASVDLTIFSLHLAGISSILGAVNFITTIINMRSMGITFDRMPLFVWSVLITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH | 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: 228
Sequence Mass (Da): 24813
Location Topology: Multi-pass membrane protein
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Q6XSL1 | MMQFLLYSSTLISSFIFIQMNHPLAMGLMLLIQTLQICLLTGLMAKSFWFSYILFLIFLGGMLVLFIYVTSLASNEMFSLSMKLTTLCITIMTSLTFISLFIDKLSTLPFIQNLEMNTYFNPNLFTHENSLNLHKLYNFPTNLMTILLMNYLLITLIAVVKITKLFYGPLRPMN | 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. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Mitochondrion membrane
Sequence Length: 174
Sequence Mass (Da): 20089
Location Topology: Multi-pass membrane protein
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A0A0M3YXT8 | TLYFVFGTWAGMVGTSLSMLIRMELGHPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLVSSMVENGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLSGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | 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: 219
Sequence Mass (Da): 23667
Location Topology: Multi-pass membrane protein
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A0A7C4NFH3 | MVYGQGSRKDLKSRAKHPSSKTSMKTIRQTGKTIWWYESLLKHKLLLVVLMLGLSYLLGVWLRTLPAFSEQQVLTGDDPYVHLRYAECLLDNGSLPSNDTLRYYPEGFDPRQELLLVPWFIAGFSWLTGLRPLDIAIWLPAFFAPLIVVPIYFISKKITGSRSSGVIAAFLAASAPAFILRSFEGFCDKEAFTTPLMFAALTLAFTSFNTIMKVATEGYKKTFTISIILSLLSGILIGVSALGWAGYLFTYLVLAAYALLMLFFGEDSRNLGLIFIPYLIVMVVSGTFVAFSTARYGGLSFFWSVTFLIPIGASLPLIALRWLKRRFVVPLVIALMVAVVIVEWSYVAGLINWLFGSKGLVRLTVAESKQPTLFDVWNQVGFPIILAILALVPRDVKDPTSRNNYLFLLSMFAVSAILASSEIRLLMFLSLTASIMAGATLSRIIDYCSSKLLVKRKKRLELNEKALLGLALSIILAALVVSSTFAIPTYSIENGPITSHATIYKSLGMSGYSQWLQALDWLKENTTSGAIIISWWDYGYMIQYYANRTTVVDPGNFYEWRNVVVAKFFMSSDENEALNILNQSFGLEGKEVYVIVSLEEIPKSHAIAFIAGYPTPPFQLQLIMGAWRWVISDPNAILTRLVLGIEGLQSDASNIIPSLKHFEKVYCNSYVALYRVMWELT | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Location: Membrane
Sequence Length: 681
Sequence Mass (Da): 76126
Location Topology: Multi-pass membrane protein
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N6UAN0 | MEIINRSTDGGQFVTDYRQPGYLRLLRWGCADECEYQCMWSTVEKFQENQLNIPQFYGKAGAGHPGARLHAVLPAQSLHAPDAVAQVPKRGAGWRPLALALAVLRRRLLQRLDLVGRFPQSRPALDRMAGLCGRIFHHSGQLLCDVRPVSDFLESWESREGDRCDCRVLPHVLGAVFPKRPQLVLLVSLGFLLFFLKHAAYLSRGRSSNCHWLAGVERKVPPEAPLRPQLPALRDLLRVGAFAGTSGQSALVFRGRLPRPVAFGNSAAPGLHLQVRHGRLPVLEEHGKAGPAGRD | Function: Involved in the lipid remodeling steps of GPI-anchor maturation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 295
Sequence Mass (Da): 32671
Location Topology: Multi-pass membrane protein
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I1S7L6 | MDFLQRLARFLDRPLFPWKKLIMGFSVGQYLFESFLTLRQYRVLQKTSPPAVLSKEVSQEVFDKSQAYGRAKAKFEIINGLYSQVQNIAFMHFDVLPKLWSWTGDLLLKWAPARFTGEISHTIVFVLTFTVISQLLRLPSSIYQTFVLEEKFGFNKQTPKLFITDMVKTQALTLVLAPPFLAGFLKIIQKTGNQFFYYLWLFFIALQVFMITIYPVAILPLFNKLSPLEDGELKTKVESLAASLKFPLHELYVIDGSKRSAHSNAYFFGLPWKKHIVIYDTLIEKSEPEEVVAVLAHELGHWKLGHTTSLFGISQAHSFYIFTLFSVFINNHSLYSSFGFLKEHPIIIGFILFSDALAPMDLIINLLMHIVSRKFEFQADAFAKSLGYPEQLARSLLKLQIQNLSTMDADWMYASYHFSHPHLSERLNALGWKGSEGVTEGVSDKSLDNEKEGVVKASGRDEL | Cofactor: Binds 1 zinc ion per subunit.
Function: Proteolytically removes the C-terminal three residues of farnesylated proteins.
EC: 3.4.24.84
Catalytic Activity: The peptide bond hydrolyzed can be designated -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 463
Sequence Mass (Da): 53015
Location Topology: Multi-pass membrane protein
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A0A7J6FET6 | MYIKFIDLYVYILRNILIYCSCKVCNCGYDMGSFNSLDLIMILIVATAFLLGANGNKLTPLHYSQTCPQALSIVKGEVAAAIESETRIGASLLRLHFHDCFVNVSSHTIGMAKCTSFRARIYNDTNTIEASFAKSFQRKCPANGNNGDNLAELDHQTPTHFDNLYFKNLLKKKGLLHSDQALFNGTSSVDSLVKRYANNNEAFFKAFAMGMIKMGNISPLTGNKGQVRVNCRKVN | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 235
Sequence Mass (Da): 26116
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A0A7R9Q594 | MYQLFSILKPLFKPSSYVIDNNIFRLHYKATVVILIGCSLLVTARQYIGDPIDCLSGDKIPTEILDSYCWIHTTFSIESAWKLKVGTEVVYPGVDNSARHPDSRRVYHAYYQWVCFMLAFQAMLFYIPRYLWKSYEGHRIKNLCLDLNFPIARDPVVTRNNRALLVDYLYHNFNNHNTMFRMYVTCEVLNFLNVILQMVLMDRFLGGEFTSYGWDVLSFTEWDSAVRYDPMIKVFPRLTKCTFHQYGPSGDVQKHDALCILPINIINEKIYIFLWFWFYMLAILGFMALVYRTVTILMPQVRYLVIQSRCLANYDALRSVCNQCSIGDWFVLYLLCKNLDSINFKDMIVDFDRRLTGKTANGL | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 363
Sequence Mass (Da): 42639
Location Topology: Multi-pass membrane protein
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A0A7J3LYY8 | MVRMLIDYMEIPRYVVMGPKVLECIPDICSKLGFKGLGYIVSGSTFTRKIAEKVSGILEGYGIKTASAMVVGNPRYDRFLDEIRAIYTYAKKIDAKFVVGVGGGTILDTAKLISSWLNTPFISIPTSTAHDGIASPAISFLLRYKLSIYGEGDTKIIAPIAIVADIDVIKDEPYHMVVAGFGDLIAKYTAVKDWRLAVRERGEEYSEYAASMSLMSANLLAKHISSIRDKSVYGIRVLVKALIGSGVAMSIAGSSRPASGSEHLFSHALDLLSLRYGFEPRSHGIQCGIGSIISMYLHGGDWRRIRSLLLSVKAPVDSKTLGIDENYLIEALIEASKIRPERFTILSKVKLDRGRAEAILTETLII | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Function: Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea.
EC: 1.1.1.261
Subcellular Location: Cytoplasm
Catalytic Activity: NAD(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate + H(+) + NADH
Sequence Length: 366
Sequence Mass (Da): 40074
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I3T9C8 | MAPRGKGVATILAIGTANPPNVILQPDYPDLYFKEVNNDDEHLQRLKLKFKSICENSKIEERHVALTEEFLKQNTEDGKYESLPLENLPTEQVVNLAKEASLKALQEWGQSISEITHLILCTTSCFGSVPGPDTHLARLLNLKPTVNRLMIFGHGCHAGGTILRIAKDMAENNVGSRVLAVCSETMLASFQRPTDDFAPATDVLIGHALFADGAAAMIIAADPNPSIEHPLFEIVSASQTTVPDTQNSIRAQIPVENGRLVYHFVKEIPNIVSNNVKKCVIDALCSIGFDEDIEWNKLFYVVHPGGPLVLSKVEEKLGLSEGKLKESWNVLRQYGNMWSSTVIFILNEMRKRSKIEGKGTTGEGLEWGVFLGFGPGVVTETVLLRSVACVEK | Pathway: Secondary metabolite biosynthesis; flavonoid biosynthesis.
Function: The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
EC: 2.3.1.74
Sequence Length: 392
Sequence Mass (Da): 43087
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A0A0R3VT90 | MCFVFEPSILQNLGLDATLQAKGITSDPSPSGCQYLLRPLRSSDYGRFEEFTFRPSTYFIVVLEDLALRKLIGCATLFVELKMIHNRSKRGHIEDVVIDEAYRSRGLGRLLVSVLIEVGRSQGCYKISLDCDSDKVAFYERNGFKQETVSMCIRLSD | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.
EC: 2.3.1.4
Catalytic Activity: acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Length: 157
Sequence Mass (Da): 17786
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B2DBT0 | ICRDVNHGWLLRNLHANGASFFFICIYLHVGRGLYYGSFLYKETWNIGVILLFLVMATAFVGYVLPWGQMSFWGATVITNLLSAAPYIGTELVQWIWGGFSVDNATLTRFFSFHFILPFIIAGASMIHLLFLHQNGSSNPTGLNQNLDKVPFHPYFSYKDALGFAIMVGALASLSTFAPNLLGDPDNF | 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: 188
Sequence Mass (Da): 20983
Location Topology: Multi-pass membrane protein
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A0A7J3KR83 | MSKLSIAKFRALVRKIASEAISSGERRLIVLAGRESLRYGCLAVRAYCKLVKKKVSLLYSADTDQTGALIGLDNVKDELKGVASLDALSLDESDLALGGTWDLLLVDFSKQFRANDLGRLTETVRGGGLLLFCIPPLDEWFSTLTPFERKLISKPYTEYDIKHLFKRRFVSKALEHPGVWLIDLEKGEVYGRETKTISSAPARFTVNLYGIPLTEDQLKAIEVFQKLVETKGKSCLLVIADRGRGKSAAIGLGLAWYAKKLIDEGRSRFIILTAPEPSNIRTLVDFLVRGLEILNIRYNVREVGGVIRKVEVDGVEVAYTQPVTAAKSKVAVKVVDEAAGIPIPLLLGILKNSKISIFSSTIHGYEGAGRGFSVRFMKALKEDPRLNVEYVKLETPIRYPKDDPIERWLYDMLLLDAEPDKIEGEPSLDLVSYKRIDKDDLFRDESILRSLYGIYVLAHYRNRPNDLAILLDAPHHSARALIYNGKVIVSLWVAEEGGLTFASRDDMLREAEASGHVIPSRVALHCSVLDFFKLKGLRIVRIATHPNFTGRGFGSKALSMLESESSGIYHWIGASFGASEELVKFWTRNGYIPVHLSPSINPVSGEYSLIVIKPLTEEAYEYVAQANVEFRVRLLESLYDVYSKLKLDIARLLLSVGLGGMRIELTRSQEDRVREYSRGMLSYEASCDSVKALARIHFLSKPDERVKFEDYEEKLMIAKLFMGMDWESIRRILKIDKPLDCMRRIAGRMVECYLDRSG | Function: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
Catalytic Activity: acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O = ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) + phosphate
EC: 2.3.1.193
Subcellular Location: Cytoplasm
Sequence Length: 758
Sequence Mass (Da): 85264
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A0A7R9KWA9 | MGLTTGLGSQYELLNGFNQIIISKMANTSLRYSYVFEFERNFNYNYTTKWMSENWMTSFYFITTYLMIIFGGQQWMKDREPFKLRSTLFLWNLLLAIFSITGTVRVMPEILSVIREQGFFDSVCDNGYITRVNVSSLWTWLFVVSKVPELGDTLFIVLRKQKLIFLHWKRP | 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: 171
Sequence Mass (Da): 20301
Location Topology: Multi-pass membrane protein
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A0A2E8B0Q8 | MKLFLIGYRGTGKTMIAKILATAWNCEWADSDGEIERRSGKSIAQIFSQDGEASFRKLEIEVVRDLATGPHKVVSLGGGAVMGTENRTTIAAQGLTCWLQATPATIAQRLEQDSATKSQRPDLTPLGGLEEIQTVLDQRFSVYQSCADFEFDTEGKSPNQVADEILVTVAKEQKMNS | 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: 177
Sequence Mass (Da): 19329
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A0A2U9CHR1 | MADDKDVLRDVWFGRIPTCFTLNQDEATEREAEPYYLLLPRVSYLTLVTDKVKKHFLKVIKADDVEEMWFEYEGTPLKWHYPIGVLFDLHATNTVLPWSITVHFKTFPDGDLLHCQSNSVIEAHFMSSIKEADALKHKSQVVNDMQKKDHKQLWMGLQNDKFDQFWAMNRKLMEYPTEEGGFRYIPFRIYQTMSDRPFIQKLFRPVSPEGNVHTLGNLLKEMYPSAIPNDASALSHLDEAFLDGQWEQWKVEHGREYNGLDEEGIRRAIWEKNTLMIEAHNQEAALGIHSYEMGMNHLGDMTSEEMVEKMTGLQLPLNLERSFTMGLDDKVSKIPKSVDYRKKGMVTPVKNQGSCGSCWAFSSAGALEGQMAKTTGQLVDLSPQNLVDCVTENDGCGGGYMTNAFKYVQENGGLDSEEAYPYAGEDQSCRYNSSGMAAECKGYKEIPVGDEHALAVALFKVGPVSVGIDASQGTFQFYQRGIYYDRNCNKDDVNHAVLAVGYGVNPKGRKFWIVKNSWGESWGKNGYILMARNRDNLCGIANLASYPVV | Function: Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for MHC II. Involved in the maintenance of axon morphology and membrane structures, as well as in normal adipocyte differentiation. Promotes primary ciliogenesis through removal of OFD1 from centriolar satellites and degradation of IFT20 via the autophagic pathway.
Subcellular Location: Preautophagosomal structure membrane
Sequence Length: 549
Sequence Mass (Da): 62196
Location Topology: Peripheral membrane protein
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A0A072US66 | MGGSWSNNNSNNRNISRRRHNSYHEHYPPPPYYYYSSQPQPLMPQPQPQPQPPQGYFPPHQYYSNGYTPANSMLPQPHHPFYATTNTQPLDIDVNVVQALPPPPPYTDHETAKKVRNDVNLHKHTLQLYQDPNNPDHHLISFVFDALFPGRITIFYIAREEEHQCRFVPLFPEAFEPITFPFQKGVGQKFCQPSGTGIDLGFFDLDDLSNPSPEEDIFPLVICAESTPLQDHDTPVSSLADASPHMQITQAVLEKNSDTGSFQVKVVRQILWIDQVRYELRELYGIGNSTAPDFDRNDPGKECVICMTEPKDTAVLPCRHMCMCGECAKALRVQSNNCPICRQPIEQLIEIKINNDDQ | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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: 358
Sequence Mass (Da): 40814
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A0A2G4IPY5 | MTSSALQEVVAVLGCPAAGNPAQYLFERLFEATGLDWRFLTLDVAPEQLADALNGVQALNFRGCLLAGPLRSAALPFLASSSPAATFSAAASLVERQASGLVGHMTDGRGMMEALRAHIDPTTMHVLIVGAGAAARSAALELSLAGVAGVTVCDRTPERAAALVTALQALDASPCDSMPWQATIPIPSHVGIVISAVPAGDPQRRDTKPAAEFSGMRSDLVVADFALIAQPSPVMACALKAGACAIDGLEIHCEKTAIDFHTWTGIEPDTDMLREALDEYLNA | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 283
Sequence Mass (Da): 29418
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D8VEP7 | GGFGNWLVPLMVGGPDMAFPSLNNMSFWLLPPSLMLLIFSACMEGGAGTGWTIYPPLSGLQSHSGPSVDLAMFALHLSGVSSLLGAVNFMTTMANMSTPGMKLHKLALFGWAVVVTAVLLLLSLPVLAGAITMMLTDSNFNTSFFEVAGGGDPMLFQHLFWFFGHPEVYILILPG | 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): 18627
Location Topology: Multi-pass membrane protein
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A0A7J6HQY6 | MIKMASPRSFILALPAIVLVLALFMTTVTAQSKLSTNFYKNSCPNVESLVRSAVNNKFRQTFVTAPATLRLFFHDCFVRGCDASVMLSSPNGNAEKDHPDNLSLAGDGFDTVIKAKAAVDRDSRCRNKVSCADILALATRDVVVLVPTRLVSLIVVKCQTEFTTSARELGGLLTQHSTEITLYN | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 184
Sequence Mass (Da): 20057
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W2KPG9 | KILPLATLKMMLCSLSGQVPVEPVVSLKSGHVFEKRLLLKYLEQNQQRCPVTGEELDAEQDLLALKAAPSTKSSATSAKAAAFAPEAASIPQLLATFQNEWDAVILETFTLKQHLEQTRQELSHALYQHDAACRVIARLNAENATLKERVTQLASGEQDDVDMQDGAQTGAALAPEVLATVEAKQKELAKKRKDFKKKDGPQRAALLSGLADWKMASSHTLHDSDKPGVTCVAIDSKRPTLVATGGVDKHAKIFDTDKQQLVATLTGHSKKLSHVEFHPTADMVLTASHDKTVKLWTPQEQGYGVGYTLDGFDDAVASSSIHPTGNYVLSGSLDATWAIHDVRRGHLLSRYTLNGELAMPDASAGKPKKAANEARCARFHPDGGIFGTAAKSKLVQMWAVNSLSNVVTFEGHAAPVTALGFSENGYHLASGSEDGVVKLWDLRKATSFFELDLKKEQPKLKLGAIHSINFDASGSHLAVASVQSVQVLKEVSKNHWEVVKTLSDHKAAVTGVQFAPDSSFLASTSMDRSLKIYR | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin-protein ligase which is mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome.
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: 534
Sequence Mass (Da): 57798
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A0A7S5SL67 | ALIGTALSMIIRSELSAPGNMIGDDQIYNTVVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGSPDMAFPRMNNMSFWLLPPALLLLLASAAVESGVGTGWTVYPPLSSNLAHSGSSVDLAIFSLHLAGASSILGAINFISTIINMRAPWMKLDQAPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTTFFDPSG | 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: 198
Sequence Mass (Da): 21173
Location Topology: Multi-pass membrane protein
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A0A7R9KLU0 | MVAMSSSMSSPAINADISEMLLELGKHEMNVNQNRFKYQMYRKAAKSVVDHPKRIQSVAEAKGLAGVGAKIALKIMDFVANGSNRQLDRVRQSDTNQSINELLRVSGIGPKLAAKLMADGIDTIDRLRTIADTLTDHQKIGLKYVDEFERKIPREEIQKIETLLTAKMNEFNKNLLLTICGSYRREARESGDIDVLITHRNVTSDQMKFKTNTYLKDSVRSLQKCGLITDRLSLGDTKFMGVCRLSKECPHRRIDIRFXTNFLVVPPHESTGTKCLSAMARKSRMCCFVNTEPHGLDGLLYIMAAVLPSILLSKSCKLISQFLSGIRSADRVSYREKPGLGTNILHPGLANTVIHRSRACEQPLPWIQYKCGTNATFGCNLCNKSKKWCDSYGHHWIKQTAKQHIPWPRRALRSQNCIRRPLVAPLHSRRPRNTRYSYTTSCSLLWHSLSLRMASGFQRLSDRLKE | Function: DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Cytoplasm
Sequence Length: 466
Sequence Mass (Da): 52791
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A0A1D8BKE5 | TERQALNVARMRMLGAEVIAVKSGSRTLKDAINEAFRDWVANVDHTHYLFGTVAGPHPFPAMVRDFHRVIGVEARRQVLERTGRLPDAAIACVGGGSNAIGLFHAFIPDSHVRLIGCEPAGHGVETGEHAATLTAGEPGVLHGSRSYVL | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 149
Sequence Mass (Da): 15955
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A0A7R9LQ32 | YCPLDLFSGCPQRTQTALRALIRDPQNNFRVFRDSHHVFGDSAAADSSALSPLLRDFCGQSEDDVEGALCRLVAKALALRVDTSRPEDEALMAEEECDLHHNSNHCFCTSEHALTSGSVLDCVLRAQRLDAIDSEVALQLLQRVNSNDVWTPPTLDAADQSEDLALKVFRFLVSLTAKDLSIMITMQRLEAGADVTSLPSRHLIGDAERQYLASIRIIDLDQKSDQKIKRTFSKDMRMIAAFNTSAKNNNNNNSV | Function: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate).
EC: 2.7.1.158
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Length: 255
Domain: The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Sequence Mass (Da): 28310
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A0A7R9KM24 | MLVLHKVIIKVFLVVYTMKSLYEDIKTLLNKLNQMESKQTEKLLKEDGEKVVPNIDIPDDNVPNEEVISKLNEKTCFHKVRSLDKLIRRKYHIDLETMQLHYDSNIKHDLYDLSEVRKGWQSDRFNVIEAKFRRELNASDGPKNLPQLEEDKCFSLVFGIKTEDLVAPNVETRDVWVKGLKYLIASYKDQLINDEQSVWLEKQFREADKNKNKSLSFKEVVSLLNRINISLSDKNAKQFFKARDPTLDWEEFLKFYQLINIRPALDRLFKKYSVNNTSFMGPEELKEFLITQQKMTKVTLADCEAYISRYEPKEIIASSVKICLNLCPTIILPHLIIHQLTGSSSIEAYRLALIRGCRCLELDVWDGDDGEPIIYHGYTLTSKILLRDVLKTIHKYAFKMSPYPLILSMENHCSIEQQVVMASLMKEILNEYLYDGIVDESAVIASSVKTCLNLCPTIISPHLIIHQLTGSSSIEAYRLALIRGCRCLELDVWDGDDGEPIIYHGYTLTSKILLRDVLKTIHKYAFKMSPYPLILSMENHCSIEQQVVMASLMTEILNEYLYDGIVDESAGQLPSPEDLVHKILIKGKKLPKIKPKKLIKLRNALNLDAINESKSEEEENEEEEEEEDGYDSDDDMSEYELNEESTHENINSKITENQNNEEIKNTEDENSDIKDTNITNRSEIKEKSSDGNDIKITEKNVMQDINNTEIKNSNDRILNKRNTYPITNKNDYQKNVRIAPEPLNGDHQPLGVTCSVPQTRHHRPTPEEINVSKKK | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+)
EC: 3.1.4.11
Subcellular Location: Secreted
Sequence Length: 775
Sequence Mass (Da): 89482
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Q8QS01 | MGAELCKRVCCEFGAPSGDPLRDVMGRRVNLRGYDNMPHTSSSESDLEEDDDVDYPSADPQKRRLHPGPSGGGSVLSQKKKHASQQNVYEHPYHEPVVVFKGPGHDDGEEDGNEADRSSLSTVRSSFRQDNKKKKKTKKKKTTSQQSSIMQETDDDPDLDDERSACLGGASSSPPPLPPRGGSQTTAGSGSRRLPRPATPMPSKKIKSRSGSESTTSSRVSMSSSCY | PTM: Myristoylation and palmitoylation (probably on one or more of the nearby cysteines at the N-terminus) enable membrane-binding and Golgi apparatus-specific targeting and are essential for efficient packaging.
Function: Plays an important role in the cytoplasmic envelopment of tegument proteins and capsids during the assembly and egress processes. Participates also in viral entry at the fusion step probably by regulating the core fusion machinery.
Subcellular Location: Virion tegument
Sequence Length: 227
Sequence Mass (Da): 24599
Location Topology: Lipid-anchor
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A0A099NXS9 | MFVEYKSVLLLSLLLLSSCGLGKSTRSYDKKYQIYRHLNKANETFIQNACDTLSFKCYSLYVDQLEYHCLIPLVNDTLETEKVEAKDAAQLEAEKDQAIEVIRNFNLEMRGKVALKPAGYWYYAVRFDHDIHQYHVGASGLPDYNYKLAAWSNNDPSISFDSKPYYKEPEAEDPYAIKSNFEVIETEDKTKYVSQRISNGETCDLTGLPRTTTINYFCNVNLKSPLIVSVNEWRTCEYIIDLQSSYFCDYDMWMPPKTLMNHHIDCYPNTDTFETLGEKIDIHGLVLDPLTEGVFLGRRGESRRFVVLLTKDYNLWNVNGIDQDIQFEHLLSDIASGFQKYTRNLKLSTYIDDISTIVLLDDTFKLRFETYDGSGSYIGNIMVEHDRNGYFVSYFTDEDIPEESNWLEYESILMLQ | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 416
Sequence Mass (Da): 48329
Location Topology: Peripheral membrane protein
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A0A5N5T1K3 | MIYAMVAIGVLGFVFPQELKFLDGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSIGAVFAIFGGVIHWFPLFTGVGLNNF | 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: 81
Sequence Mass (Da): 8835
Location Topology: Multi-pass membrane protein
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A0A7R9KAP9 | MSFQGLKFISNSLFLINNLKELLLHNNDLRSIPEGICRFKTLEKLNFSYNKIKHIPPELGRLVNLKELYLNDNFISEIPWEMGSLYNLEIFNLSNNPLVPPFNSLSKDRSVIRFCREHNINYLPPCDRSWLEVVYRPENSFETISVGTYNILCNFFASKLTYAPAWIINPDYRKDILIQNIISYNLDILYGKKDNVVLVTVLEKGLGHTIIVANTHLFWDPQYTDIKLFQSILLLEELEKIRIKHKNASILLMGDFNSLPDSSVYKLMVERKIGGLDFDKYDYAPFNDGFRHSMKFLDAYENQDLAFTNFTPHFRGVLDYIFHTEGLVRSSVISSVEEEYMERTVGLPNIHFPSDHILIGAQFQIKGIPKRMYNSMSK | Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
EC: 3.1.13.4
Subcellular Location: Cytoplasm
Sequence Length: 378
Sequence Mass (Da): 44002
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A0A803QTA5 | MQSCPSVTNIVGGVIQQALQTDPRIAASLIRLHFHDCFVIGCDGSLLLDSTDTIVSEKEGFGNINLARGFEVVVNIKTAVENACPGVVSCADILAIAAEEFVRLVNTNN | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Sequence Length: 109
Sequence Mass (Da): 11560
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A0A7C4G4J0 | MRISDLNIDGRVKELLVRYGYVELYPPQVDAIRAGILNGVDTVVAIPTAAGKTLIAELTIVNRILKHGGKALYFTPLRALASEKFNDLMKYSELGLKVAITTGDYDSANEWLEKYDIIVSTYEKTDSLTRHMPKWIRELSIIVADEVHLINDGERGPILEVLLTKLISLNPNAQVLALSATVSNAEEIAKWLRNAKLIASDWRPVKLREGVYYRGSIEFNDGVIVEVPYLTSNSTINIALDTLVNGGQALIFTSSRAQAVSLARKLSNYTHQYLSKEEGKELRELSKKILALEPITSINSILSECIKCGVAFHHAGLAHPHRKIIEDTFRSRILKVVCATPTLAAGVNLPARRVVIDSINRYEVGIGSVQIPILEYKQMAGRAGRPKYDSIGEAVIIAGSKASFNTLMSKYVLGRPERLTSKLASEKALRTHILSLIASEFTGSEDELMDFMEKTFFGIQYGAYSIKNRVKRVLEFLEDNELITASRRLKATILGRRVSQLYIDPKSAVIIRRGLEKAKDIKPTSILHLLCSTPDMPKIYLGRREEEKYLAILEEVEEELLIDTSLYDYDMLLAELKTAMMLNSWINEEGEEKICEEYGIWPGDLYVYVETADWLTYSITEIAKVIGKKEIVTPLQSINSRVKNGVREELLDLVKLEGIGRVRARMLYNSGFKTIDDLKKATIEQLSSIPLIGKTLAVRIKNQLGKT | Function: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 707
Sequence Mass (Da): 79237
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A0A954BNA0 | MPQFDPTLFAGLVFWLAITFTALFFLLSRLVLPRLHDTLEARASRIADDLDRAETLRKEAEEVRQQYEEALQEARDQARAGITHAVSEMERQGAEREAALTAEIDARITAAEQRIARARDEARTHIRDIAIEACEAASERVAGIKVKKAVVTAAVDGEMKRRNLQEVA | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Cell membrane
Sequence Length: 168
Sequence Mass (Da): 18826
Location Topology: Single-pass membrane protein
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A0A2E2EAJ4 | MTDAGSTQNAALATVERLLSLLATLLLIAGTVALVLMATHVVSDVVGRLFFNHPVYGTTEIVSFYYMVGAVCLPLAYMELRDEHITVDVFYQKMPLMMRRVVFVFSILTTALFFGLFAYQSWFDSLRAMSSREIVMGASLIEIWPSRFFMPISFGLLVLACLLRAAKVILTPYAAETHVRAEGK | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 184
Sequence Mass (Da): 20500
Location Topology: Multi-pass membrane protein
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A0A7R9LH42 | MVTVRETHACVGDYWRYLRNKITGHTVLLGILYFPLNFIKCQRSISTAGGPLRVQLTVRDALNSAMDEEMERDESVFLMGEEVAQYDGAYKISRGLWKKWGDK | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
EC: 1.2.4.1
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Length: 103
Sequence Mass (Da): 11846
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A0A8T4ZAL0 | MRGNSSKTHGFKEGMAEIIPAREKVLSPELMPKFKEPFGLLIPGPPEATIPTLRKLLSKEKASKIIAVGDVVSKSLRDSGIKGNLYVTDDKVMRERIRPLDFKGLGSMEVLRIFNPPGRLMAEAFQAIDNALRSPNPVRIVVEGEEDLLVLPAVILAPTDSLVLYGQPGKGLVVVRVTCEKKREALELYRAMPESHGT | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Function: Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
EC: 2.7.1.237
Catalytic Activity: 3'-dephospho-CoA + GTP = CoA + GDP + H(+)
Sequence Length: 198
Sequence Mass (Da): 21753
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A0A7R9L4X9 | MSNIYIQEPPTNGKVLLKTSVGDIDIELWSRECPKACRNFVQLCLEGYYDNNIFHRLVKGFIVQTGDPTGTGMGGESIYGQPFKDELHSRLRFVRRGLVAMANGGTKDDNSSQFFFTLDTCPELQNKHTIFGKVSGNTIYNMIKLEESQVDQNERPLYPHKIISAEILLNPFPDIIPRIKEKKTESKPEAKSKSKATKNFSLLSFGEEAEEEEEEGAKASEEFRGKSKSSHDLLKDDPKLSAVPAVETNDLMTSDEXV | 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: 258
Sequence Mass (Da): 28967
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A0A438E6Y6 | MEAAATIITAVVILCWLQFSSVECHWRLRNPRQPNQTEASTRPQGTLLQSNDKLQDRFYRNTCPQAENIIAKSVYDAVLVQPGLAAGLIRLHFHDCFVNGCDASILLDTTPSGEPVEKTSRANVFASQIFKYIDRLKADIERECPGVVSCADILAYATREAVKEEGLPYYLVPGGRRDGLSSSASNVAGNIPSPNESLKNMTQIFLTKGLSIEDMVVLFGAHSIGHTRCRSLFKRLYNYSSTQAQDPSMDFAHSLYLKGLCPKAGPLLQEVIDKVMVPLEPITPSRLDTLYYTQLLKGEGVLQSDQALTNNPTTNEIVKRFSQNPLEWGARFTNAMINLGKVDVLTGQEGEIRRNCRAVN | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Subcellular Location: Secreted
Sequence Length: 360
Sequence Mass (Da): 39884
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A0A8T4VTU6 | MAKKKKIEPLKNITRHELVPDHVILTDKEKQQLLTEYHIEPSQLPKMLTTDPVALSIGAESGEIVKITRESYTAKESTAYRLVVEDNK | Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
EC: 2.7.7.6
Subcellular Location: Cytoplasm
Sequence Length: 88
Sequence Mass (Da): 10029
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A0A174RLF1 | MRSFEKLKIAVAGTGYVGLSIAILLAQHHQVIAVDVIPEKVDLINQRKSPIQDDYIEKYLAEKELNLIATLDATKAYSEVDFVVIAAPTNYDPLKNYFDTSHVEEVIKLVRNVNPNAVMVIKSTIPVGYTESVRQKLDTENVIFSPEFLRESKALYDNLYPSRIIVGRPEGDARLEEAAHIFAELLQEGAIRKNIDTLFMGLTEAEAVKLFANAYLALRVSYFNELDTYAEMKGLDTQAIINGVCLDPRIGTHYNNPSFGYGGYCLPKDTKQLLVNYTNVPENLIQAIVESNRTRKDFIADQVLHKAGYYDYYNRDDYNSVEEKRCVVGVYRLTMKSNSDNFRQSSIQGVMKRIKAKGAEVIIYEPTLEDGSTFLSSKVVNDFTKFMEQSQVIIANRYDTCLDEMKEKVYTRDIFSRD | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Length: 418
Sequence Mass (Da): 47502
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A0A812XC59 | MIQAFDVQVNVSRTAQRSVRRPALAGWHIWHRHLHTQLLTPTSPEEKRPKICPKIEKPQALTNIDGIIAESQALMAARGDLGVELELERVAKDAGLFVINATQMVETVESMIESPVPTRAEVSDLQNAIWDGFACELEIDVKALYYWDLMEVYAVPVSAYFEFYFGDARPFWMEMAEGDEGVLTRGPSVAFAFPIGALTAAVSEGPRSPPPKAKAPAAPAARSAQRISWADLAEEAQGQREEEEEEESLQAASAQARVSWADLQDDTVEVSWQWS | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 275
Sequence Mass (Da): 30481
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A0A132P3M6 | MTQETALIFQEQTLSEELSDHMIENQVSEVEIPMGIAQNFQINGKKKWIPMATEEPSVIAAASNGAKICGNICAETPQRLMRGQIVLSGKSEYQAVINAVNHRKEELILCANESYPSIVKRGGGVQDISTREFMGSFHAYLSIDFLVDVKDAMGANMINSILESVANKLREWFPEEEILFSILSNFATESLASACCEIPFERLGRNKEIGEQIAKKIQQAGEYAKLDPYRAATHNKGIMNGIEAVVAATGNDTRAVSASIHAYAARNGLYQGLTDWQIKGDKLVGKLTVPLAVATVGGASNILPKAKASLAMLDIDSAKELAQVIAAVGLAQNLAALRALVTEGIQKGHMGLQARSLAISIGAIGEEIEQVAKKLREAEKMNQQTAIQILEKIREK | Pathway: Metabolic intermediate metabolism; (R)-mevalonate degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from (R)-mevalonate: step 1/1.
EC: 1.1.1.88
Catalytic Activity: (R)-mevalonate + CoA + 2 NAD(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADH
Sequence Length: 396
Sequence Mass (Da): 42934
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A0A2S7DSI6 | MSYLPYVIAAYAVFVLVLLWDLIAGHWQVRRALKTTQARRLRERKRTLPSDAELDR | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 56
Sequence Mass (Da): 6628
Location Topology: Single-pass membrane protein
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A0A5S9NC89 | MTALLLIDLPLDPEAPVSWLLWDSVGGSVVSEGVLNNAKELSTLAETAEGVPCYALIPGDAVSAHGVVLPKGGRVGLSALPFQLEDKLCSDLDSVHITTGVIKANHVTDVLVLSREIATYCKDVLHRSGLRIKALLPDYAVLPDDTVVVGAHQVAANFHAKSAGLSTTNFQVWQQLVSDGEQADQAVQWYFSDDYSGDLTELAAETTERCGSRLHAFARGFKPWPMSLLSGEFALKDESSEAISRLRWPVILLVALLFVHWLGLAIQTRTMNLEADALDKGMVEIYKDVFPGARVVNARSQMRSQLNALESAGATGAMMPWLDKVAAASRGRSGVSLSQLNYENDPPVMKLLVKAASYELVDQWLAALKAQGLDVDRGAFGQDGGGIAGQISIRGAAQ | Function: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 398
Sequence Mass (Da): 42677
Location Topology: Single-pass membrane protein
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A0A254TTU9 | MPSLPDSPPPVPPPVPVETHPNRTVGVKPTAAQRALPDPNRLAPEDAYYTSSLPRARPTQTGYDESLRALNGNSGTAASVAALRPPPAVPGVGSRKVRGTSRRRRRKGAWKKLLWVKQSYPDNYTDTETFLDHLQRNPRVRPYDFWPLVADSTVIVQHVSSVAIFVCCFVGIVQGRVSPVSVVCWGSVGTALGWIFWDSWILREHVENAHVAERSLEGDDGSSSSSMTSSVNPSGTSSRANGQKENQVHGLGLNMSQGESSELLRRHSTGYVSDAYGAQEPASPTPGPANGTLGGGSQEPDYLSMFSSRNRQRLSTVKSAFLIYFALLGLSPILKSLTKSTASDSIWAMSCWLLIMNIFSFDYGSGEGAGATKFPASLSTNAAVMASTVLASRLPSTTHVFSLMLFSIEVFGLFPIFRRQLRHVSWTGHVLLTLALVGVAGGAVGITLRGGWMAAVVGSILGSILTALAMGGCSWWLISLQKYKNVVTGPWDPARPIIRRHWD | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Membrane
Sequence Length: 503
Sequence Mass (Da): 54285
Location Topology: Multi-pass membrane protein
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A0A804KQG5 | MILNGCVAMKPGPCKAINYSNLSYFSHDRAFSASPKVKNLCAASQEFDPLPSRGCNVTHFSSVLSSFQSGHHRSLSSLVPVFPKLCTSGPRHRMVPRASKDVPLSFRYPPMTKKPRWWWRAVACIPYLMPLHETWMYAETAFHLHPFLEDFKFLTYPFLGSIGRLPSWFLMAYFFAAYLGVVRRKEWPHFFRFHVVMGMLLEIALQVIGTVSRWMPLAVYWGKIGMHFWTAVAFGYLFTVLECMRCALGGMYADIPFVCDAAYIQIPYD | Function: Involved in protein precursor import into chloroplasts.
Subcellular Location: Membrane
Sequence Length: 269
Sequence Mass (Da): 30879
Location Topology: Multi-pass membrane protein
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A0A059XLK7 | MSLTVYTLSNLVELKKPIFMIGSFESFHIGHNLLYERAKELASQSEIERDIVIVYFSDVENLPKNHSVMFTDELFRLQAFAGIGIKYAVQLKYSIIRQMSPDNFIDTLVKKQNDFDLISGTDFKYGINAHGNIETLKNRFGNRFHPVQIMRLNNEQKVSTGFIKEALFAGDIDLVNILSVFKYGFHALIGKEDNRLKLDFRANLAKMRPGVYCANIEIANMYYYCLLTIHSNNERVIEMIDFTWTSDKKHQSKITINSFLRPFYPNSQEKINPDDVERAKEYFIYLSKK | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
EC: 2.7.7.2
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 289
Sequence Mass (Da): 33618
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A0A800A3A4 | MSTSSIKMVDVPKIANAGRSIRHVFIRDLVMACSIGIHQHEKDDEQRVRINLDLAVDEGGQEINDNINNVICYEELAKGVEEIVDQGHVNLVETLAENIATMCLADVRVRSALVRVEKLDILEGAESVGVEIERFNSEV | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 139
Sequence Mass (Da): 15426
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A0A8B9WUH0 | MTTPSLQPGAGPGLCYVGPQLAHLSDGCVHLSDGWPGATSEGTQSLPWKQQPCGIRKLSRAAALNGQVRSPVQSGNSPPQASWSRGGGGDEGVGWPALMAGHRASLRLHVTDTPRCLSPAARMSGAPQPTPRTPRLSRPSVCCARISPASWWPVTCACVPIPPTVTAVSSRLPPAPLPPTIPLRWGCAEARAVPPNPAVGPAGLLSENGSFQAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGFGNRVSVMSYSAKFASCFYGPFRDAAQSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADLLMVKPGTPYLDIVREVKNKHPELPLAVYHVSGEFAMLWHGAQAGAFDLKAAVLEVMTAFRRAGADVIITYYTPQLLQWLKE | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
EC: 4.2.1.24
Catalytic Activity: 2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen
Sequence Length: 399
Sequence Mass (Da): 42397
|
A0A5S9QCF9 | MILFRYLTSEMLKTVFAVTLTLLVIIMSGRFVKYLGQAASGDFAPEVLFWVMMYRLPNFLEVVLPLGLFIGILLSYGRLYVDSEMTVMSACGMSRRRLLIYTLIPGFITAAIVGYVSLVVTPSGIQAYVDLLAESRSEIGVKAAVEGRFRIDKGSGRVTYIESIDRNDQVMKSVFIAQPEPIVDGGRPLMSLVTAAQGRFEIDSKTGQRYLILDDGVRYVGQSGFMDYQVTSFSQLDQLIRDSEVKTYRQELDGKNSADLWRSSELEDIAAIQWRISLGLLVPVAAIIAVSLSKTNHRRGRYGKMFPAFMIYMVYLVCLNAIRDAIAKGDWPVFPGMWVVHLVFLVLGLILLYWDSMLRHWWLNWRRQRG | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 370
Sequence Mass (Da): 41936
Location Topology: Multi-pass membrane protein
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A0A9E0FJ15 | MRILVVSATQAEAAPLQQLLTEHPVGHDVQYLVTGIGMTATAYALTRYLLTLPVDLALNIGLAGSFRRDLEPGASVWVKEDRFSDLGAEDGETFLGLRELGFTDPVNVLPYGLDRISPPAGIPGAVGATVNTVHGKETTIQEFRNREQADIETMEGAAFYYVCEREKVASLQLRGISNYVERRNRANWKIAEALASLSRAAHYFIGKL | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Function: Catalyzes the hydrolysis of futalosine (FL) to dehypoxanthine futalosine (DHFL) and hypoxanthine, a step in the biosynthesis of menaquinone (MK, vitamin K2).
EC: 3.2.2.26
Catalytic Activity: futalosine + H2O = dehypoxanthine futalosine + hypoxanthine
Sequence Length: 208
Sequence Mass (Da): 22792
|
A0A0F7PBW7 | MTTPDRTRAEFRELVAGSETVVARVEVPLSVDVSPLAAYATLAGDDYGFLLESAEKTAASDPDGAFSPAAGPEERHARFSFVGYDPDAVVTVDADGDDVTALRDSRAVEFVDTGEGDVVDRLRNALPSVDRRGFPERDRQLLDGGLVGFVAYDAVYDLWLEEVGVERPASPVPDAQFALTTRTLVFDHLADDVSLVFTPIVAPGDDPDAVYDEIHAEADRVRDALDGAPSPDTGGFERRDERAGSKDAYERAVARAKDAVYEGDIYQAVISRTREIDGQVDPLGLYESMRSVNPSPYMYLLSHGDRTIVGASPETLVSVDGETVSNNPIAGTCARGRSPVEDRRLAGEMLADEKERAEHTMLVDLARNDVRRVARPGSVDVPEFMRVLKYSHVQHIESTVTGTLREDRDAFDAVRASFPAGTLSGAPKIRAMELIHEFEERPRGVYGGGVGYVSWQGDADFAIVIRTVTIDHGDTDTLRVRAGAGVVADSDPEREYAETESKMDGALAAIERIESPAPEVSR | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia.
EC: 4.1.3.27
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Length: 522
Sequence Mass (Da): 56620
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A0A497RI97 | MQIGILALQGDVLEHELMMNAVLANKGIDSKILWVRRPEQLDSLDGLIIPGGESTVMSRLVSEMRFGHKLAAKIQERVQKGMAVFGTCAGAILISKASKDQVVKDFSQALLELMDIEVIRNRYGRQRDSFERPLTIERLGNEPFPGVFIRAPIITSVGKKVEILAKDAGGIYAVKQGKLLATTFHPELTDDTRFHELFLEMILND | Pathway: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
Function: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
EC: 4.3.3.6
Catalytic Activity: H2O + L-glutamine = L-glutamate + NH4(+)
Sequence Length: 205
Sequence Mass (Da): 22831
|
A0A7R9M1A3 | MGNVPVLNIADPALIKTLLVKDFHLFPNRTKLRPSSNAITTQNLNQLSGDDWKRVRSIVSPTFSSGKMRKMYPRFRECLTDFMRHLDGIARTGQTIDLWKAFDDFAIDVIATTVFATKIDTYKSRDNRFVVNARQKFSFNLIQAMAGIMLPKFLSQWLKVTDPKSNEFFIDTVRHIIGQRKEMGTGQKYNDFVQLLMDAKLRDIKDRKMMQDDVDDHVDEGDEESEIRRKVLDINYARKQLTENEVIAQAFVFLLAGYFTTFSALAYFTYELALNPLIQQKLYDEINGAIDSDGEIPYDVLTRLPYLEAVFAESLRLHSGALPLARLATTDYKLGDTGITIKAGQQIEIPIYAMHLSEHYFPDPYKFDPGRFMPENKHKIKPYTYLPFGAGPRNCIGMRFALIEIKICMAHLIRRYRFYRCPQTDVPIEYKRFIHVMLPKRLVVGFEKRIQ | Function: May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 451
Sequence Mass (Da): 52247
Location Topology: Peripheral membrane protein
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A0A0S7FZ37 | MSTAMAKREAGNASPVVRQIDKQFLVCSICLDHYHSPKVLPCLHTFCESCLQNYIPPESLTLSCPVCRQTSILPEKGVGALQNNFFITNLMEVLQREPECSRPEACSVLESVSAAVAGKPLCCPNHEGKVMEFYCESCETAMCLDCTEGEHRDHMTVPLRDVVEQHKAVLKTQLDAIHSRLPQLTAAVELVSEISRQLNERKTEAVAEINSTFEELERVLHHRKTALITDLENICSSKQKVLHAQLSSLLQGKEHIQSSCSFTEQALSHGNATEVLLVQKQMSERVTALARHDFPEKPHQNAHLDCQVLSAVCYYSNSSILITSSTNRSNTYEFIKAGVVYSRWRLRVCGAPSRTWAFSLQHQPWHTPLSPQGRD | 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: Cytoplasm
Sequence Length: 375
Sequence Mass (Da): 41996
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S9UDN8 | MTSFSPKVHLCGSIGEVSDVAKKDILAILRSATASSGRGASLALSGGSTPKILYSSLQDSKADLQHVKFFLGDERLVPLDCADSNYHMAFECLLKDLPQENLFPVVLGEAQESVTDPQTGEAEARKVAQVYEKQLLEHLPLATDAQSGSKIPVFDIVLLGFGSDGHTASIFPDSVAEHDEKNVVSVSFPSITMKPKVWRVTLARHVIQHAKHVLVLACGKDKEWVVQGVLRDEVEGPAPVARFLRGCKGSVTFILDGDAYGSSGKSGETKL | 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: 271
Sequence Mass (Da): 29113
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A0A2E8KE97 | MKIAIDAMGGDCGLTATIPATLAVLEAYPDITQVHLFGDEAAINNALDSAEGLVANPSLKQRLQIRHAACQINMTDKPATVLRERSETSMLLALRALAADEVDACVSSGNTGALIGLARHCCGTFEGVRTVAICAQLPNLDHPSYLLDVGANVDCSASQLHQFARMGCGLVNSLYPLDQSMGQKPKVRALSIGVESGKGNQVVTDAVALCADDASMDFAGLIEANQLLMDDCDVVVCDGFTGNIALKACEGTADYIRRYVQQALSDNSRQLSGVEPSSQRLLQAVQTARFNGAVLLGLRRTVIKSHGASDAAAFQAAIVKAITLEQGDFTQKMMKQLS | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
EC: 2.3.1.274
Subcellular Location: Cytoplasm
Sequence Length: 338
Sequence Mass (Da): 35700
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A0A8C2BCF0 | MAEHTASICNRTDEQQASHSVQEKGFHISGLCVYSGRPGKSHEPKEIMRWKRRQRYCSVALFLIGLVFAGGLVIQGQWPSQITKEKSAAQELQTMKTFSNLTMLKTTKLQEFEQSLSPLNSNENVILALDESLQQELESSLLSNISSSEEMTAARILREEPYEYILNEPNACLLRAPFLVLLIEVEPKKTAARNAIRKTWANESVAGGLGLIRLFIIGVNQDTQRNDSILQQTIEEESHRYHDIIQQDYRDTYNNLTLKTLMGMYWITKYCPEAKYVMKTDSDMFVNTEYLIEKLLKPRGQPTQKYFTGLHMLDFSPNRNKESKWYMPREVYPGSRYPTFCSGTGYVFSGDLAQRIYVASLIIPRLHLEDVYVGMCLAKLKIEPTPPPNELLFNHWRVPYSSCRYSNLITSHGIHPNEIIQYWQHLQSNKHNPCQTTW | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 438
Sequence Mass (Da): 50502
Location Topology: Single-pass type II membrane protein
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A0A804ILF6 | MLLAVLFTNTEGNILVERFQGVPTEERLHWRSFLVKLGADNLRRAKNEELFVASHKSVYIVYTMLGDVSIYVVGKDEYDELTLSEVIYVITSSVKDACGKPPTERLFLDKYGKICLCLDEIVWKGLLENTDKSRIRRLTRLKPPTDV | Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
Subcellular Location: Cytoplasm
Sequence Length: 147
Sequence Mass (Da): 16868
Location Topology: Peripheral membrane protein
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A0A357CF06 | MDHGLCHERLISLARFFIDQSQISGDSVAITGADAHHLRDVLRLKPGDVITVLDGANREYCVRLDTVDSGHAEGSILSNCLRQTEPRALLTLAQCLPKGDKMELVLQKGTEIGYTAFIPVVSERSIVKLDADRAAKKGERWRKIVQSAAEQSGRARLPEVHSLHSWQQLCDRFTDFDLVLLPWEGEEAAGLKETLKAKNIGAGVGAGAGVGAGASNGTSILVIIGPEGGLAVSEVEKARSCGALTVSLGPRILRTETAGLACGVAVLYESGDFS | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 274
Sequence Mass (Da): 29153
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A0A6I9XPL7 | MTKLRVKTVLSLLFIILHNAPRLGLVLARTMNYNNPSYFKIGGVLSNVDSKEHFEKTIDHLNFDFQYVNKGVTYKHTVIELDSNPIRTALSVCRSLIAEQVYAVVVSHPLTGDLSPAAVSYTSGFYHIPVIGISSRDSAFSDKNIHVSFLRTVPPYSHQADVWVELLKHFNYMKIIFIHSSDTDGRALLGRFQTTSQNLEDDVEIKVHVESVIEFEPGLHNFEEQLREMKSAQARVCLMYASKKDAEVIFNDAANLNMTGAGYVWIVTEQALDAPNAPDGLLGLKLINATQEKSHITDSLYVLVSALRAMNQTEKITEAPKDCSDSGSIWETGKSLFQYIRKEVLPHGSTGRVAFDDNGDRIFAEYDIVNIQYTGPNNNKTQVSVGQYFYPANGTKMKLRVNESKIIWPGRLKTKPEGFMIPTHLKVLTIEEKPFVYVRELPESENKCLPEEIACPHFNMTDDKQIFCCKGYCMDLLKELSKTINFTYSLALSPDGQFGSYVIKNTSVGGKKEWTGLIGEIVNERADMIVAPLTINPERAEFIEFSKPFKYQGITILEKKPSRSSTLVSFLQPFSNTLWILVMVSVHVVALVLYLLDRFSPFGRFKLANTDGTEEDALNLSSAIWFAWGVLLNSGIGEGTPRSFSARVLGMVWAGFAMIIVASYTANLAAFLVLERPKTKLTGINDARLRNTMENLTCATVKGSAVDMYFRRQVELSNMYRTMEANNYDTAEDAIRDIKIGKLMAFIWDSSRLEFEAAQDCELVTAGELFGRSGYGIGLQKGSPWADAVTLAILDFHESGFMESLDNLWILHGNVQQCEQFEKMPNTLGLENMAGVFIVVGVGIGGGVGLIIIEMAYKKHQIRKQRKMELARHAADKWRGMIEKRKTLRASIVTQRRIQSNGLNDPATVSLAVDTVARSNVGSRSPGRAWPGDSDLRQRPISRSDDIRLSPAAYTADVSHLIV | Function: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. This protein plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors. Plays a role in associative learning and in long-term memory consolidation.
Subcellular Location: Cell membrane
Sequence Length: 963
Sequence Mass (Da): 107634
Location Topology: Multi-pass membrane protein
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A0A191T4V7 | MLLEKLSLRLNHIFIEKNLLSMHQRILICLSGGQDSTALLHLLIRLKKSWDLQIAVVHCDHFWYPNSQLIGSHISQWMNFNKIDYYQGIVCYALHNEAEARYWRYWTVQKVAQFHQFEKIMTGHTATDRTETFLYSLLRGSGVKGLQALKWQKKICGILFIRPFLSFIRKECKDLCYIKKLPLWVDPSNHIIHWQRNRIRKRLLPYLRHYFNLQVDKNLAKLIEILHINNLFLKIFISNLKNNYYFYFMIDSRFYDMVIFTLDISRCDIIMIKNQKIFIKNPSENISKFVQKRSLVCYKNFYHFNLK | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Plastid
Sequence Length: 307
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 37052
|
A0A7D9GWR2 | MFATRFDPLGGKIPAKRASKDDSDKEKRKKARKEPDVKVRKSAHKHKKEHHKKTEQLKKEKSDFSKDIGANEKDDVEKDESAKLEKDDDGDIIMSSEEENSIERAIIQTKSKAKNAALRRYKRALEMQDKITDDAKVSSENAAPETELAEIRNVAPMPQPKLPRDRNLASQVAKNKNLQWLAKPDYHATDIKQRFDSFEPKLGEKLVSNLKTEFGIEEAFSVQVNVIQSIMKAVTKNRLDPRPYGDYLVNAATGSGKTLAYLIPVVEALKNRVVPRVRCIILAPTKPLVNQVYLTLLKLTKGFDLNIIALRSGESLRIEHDRFVNNHPDIIVATPGRLVDHISKFDLDLSQLRFLVVDEADRLLNQSFQNWCDVLVGKIEAEQEDDQDSNSFYNKFKIRCVKVILSATLTTNSEKLSHLKLFKPNLVVINNSEELVHELYQLPPHLEEYYINIPEALSFYKPLIFLRFLLDQPDLIDHGLIFTKSNETAVRLSRLLQLLSSDSNQKLSVLCINSATKSSQKRKILKEFDINGGILIATDLMSRGLNFDSIKFVVNYDLPLSTKEYIHRVGRTARANKQGRAFSFCFGEGDFRWFKKLVFSGGVINRNGKDVHQIKFIRRDEITGNGAEFALDLGDDDKTHYDSCLGKLKDEVLG | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 654
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 74377
|
A0A7R9MSY6 | MDSRTKSMRQLYCLRVNQIDSKSLDTELNAIFEAKVNDLEMQRLLELSPELLALIKTYIWVNTVWGNGISIGQSLLGLKYYDMSDTNTIRQHLNALQNVGLVLVEIVVPWLRQRVITDSISHTVDKVDQLYKCVHFMNGLVFLYYGKYRTLWERVLRLGTGLQSSQQNWSNNEL | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 174
Sequence Mass (Da): 20213
Location Topology: Multi-pass membrane protein
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S1SMU3 | MAYNAISFLSFCTLLVLPLLFQATLADSKDKKPYPFDFLKHLQGCHKGDKVKDIRKLKKYLEQFGYLSYSKNKTHANDDDFDDLLESAIKTYQLNFHLNSNGALDTETVSKMMMPRCGVADIINGTSGMRSGKKKPHRAAGSKSIHEVSHYAFFPRSPRWPPSKSHLTYAFLPGTRADAVNPVAGAFQTWAANTHFRFSRIDNYRDADITIGFQRRDHGDGNPFDGPGGTLAHAFAPTLGRFHYDADETWSVSARPGTMHLETVALHEIGHLLGLGHSSIENAIMYPSITAGTSKGLARDDIEGIKALYNR | Cofactor: Can bind about 5 Ca(2+) ions per subunit.
Subcellular Location: Cell membrane
Sequence Length: 311
Sequence Mass (Da): 34581
Location Topology: Lipid-anchor
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N1ZIV2 | MLNTLKKTILLADRDVNYMRSIKQYLEEDEKVEVVDMVDNGEKALERAEEKRPDMILMDVLLGEKDGLWVLEELSKKRINSNCIILSVIGTDDVVRQAIDLGAMYYMVKPVESNILLKRVTQILNTQKRAQNTNLLQQEYLQKKINLNFEEQKRNELETVISKLLNKMGITASIKGYHFIRKGVMMVIENEDAILSMTKGLYPDIAKEYNTTAGKVERAMRHAIETAWKRTGKEIYSELAGYSPIEKPTNSQFIAIMSEYLRV | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process.
Subcellular Location: Cytoplasm
Sequence Length: 263
Sequence Mass (Da): 30313
|
A0A944Y952 | MRNRTHLIIGAGKMGGALIKGWILSEIITPEQLLIIDPYPSEEANKAIKAGALHLKTPNNKLQDVQTTILAIKPQKINELSNGLSKYLPQDSLIISILAGTKIEKLQGVFNNHAIVRAMPNTPSSIAKGITGFVKNSKVNNNQTLEVMKLFQALGKVYELNNETHINTITGISGSGPAYLFYFIEVLERAAIEHGLPEEFAAIFARETIIGSAALLENSNDTPAKLRQNVTSPKGTTEAALKILMKKNGLEQLIQETVHAAIKRSKNLE | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm
Sequence Length: 269
Sequence Mass (Da): 29352
|
A0A0H3J9X1 | MNKNEELMKLAYKAISDGKERVNSDYHRLKYHLMPPVGFMNDPNGFININGEYHLFYQLNPLFPKGKKVYWGHVKSIDLVNWQQLPIALSPGDWYDKDGCYSGSAVDYNGKFTLIYTGNVKNSCGNRETYQCIAQTEDNINFIKSSDNPVINNQPEGYTRHFRDPKVWKHDGVWYMVIGAQTVKEQGTAILYSSYNLFDWNLIGEVAGSNIEDLSFLGYMWECPNLLNIKGKDVLIFCPQGVEKQGDLYNNIYQCGYLVGNLDYKTGKLNYKNFMELDRGFEFYAPQFMEDDRGRKLLIGWIGLPDEDEAPTVKNGWLHCLSMVRELDMKDDRIIQKPAEEMKLLRKNEISYRNVEIKNEQVDFNNINGDSYELLCDFSWSAVSEFGIKLRCNETLSEETVIYYDVKSEKLILDRDKSGLSLKGVRKCDVKNHGNLKLHIFMDTSSIEIFVNDGEEVFTARIYPNRDSRDIIFYSKNGDVKFDVKYWEL | Pathway: Glycan biosynthesis; sucrose metabolism.
Function: Enables the bacterium to metabolize sucrose as a sole carbon source.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
EC: 3.2.1.26
Subcellular Location: Cytoplasm
Sequence Length: 489
Sequence Mass (Da): 56747
|
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