ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A4Q4T8I5 | MRMLRTIVTGRMAPIAAADIPTLKLLYKLKKLDTSSPSSPKRTSDHNDRVGLIRGDITTLAVDAIVNAANKSLLGGGGVDGAIHRAAGPQLLSECRTLNGCETGSSKITNAYNLPCKKVIHTVGPIYDEIRPERSRAALQSCYKSSLELAVQHGLKTVAFSGISTGIYGYPSRDAAMVACETVASFLDRDDGKKLDKVIFVTFEEKDVRAYNQALPRFFPPATETSAGQGTKAEPDLDEGDQAEAKAEAEAKANQLPSVPTTDPADPNHIQKKRSGRWQASLGVPSSPQGIRDTRRDSSETCRAVDDDMPPTFAAAQSTS... | Function: Highly specific phosphatase involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing.
EC: 3.1.3.84
Catalytic Activity: ADP-alpha-D-ribose 1''-phosphate + H2O = ADP-D-ribose + phosphate
Sequence Length: 733
Sequence Mass (Da): 77544
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A0A1B6EIP2 | QGVSLNNEYELVAFTHFTLSRVYPTDLGLGKRVVEKPISFKRKDLLEAVTSALEVLNRNATIHGKPKYTAEDFLEGVYRSVPTTGTEYEMYFRFRQGKSQGYTKVTVMRPFAPLVTLSSSPLPPSKDKELIHVILPLSGRISTFQGFMDKFVK | EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 153
Sequence Mass (Da): 17308
Location Topology: Single-pass type II membrane protein
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A0A656AMA9 | MAGESIGVEVPIVESFNQVNTWLTNNSDLLIQYGVNVISAILILFIGNLVVKGVAGSVANVLKKKEMDKAVVDFIHGLVRYTLFIIVLIAALSRIGVQTASVVAVIGAAGLAVGLALQGSLSNFAAGVLIVAFRPFKSGDYVEIGGVAGSGFFXXXXXXXXXXXYPNFPNCPEKPR | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
A0A5B8XD93 | MLGKYSFVFMRYAHIYKITAMYNIFKLSESDIEPLQKAIRKVMEENGIKGTMLLGVNEGINGTIAGLPESIDKFYEFIRSNPLISNTEWKESWYDRNPFEKIKVKIKKETVTMRCDANFDFTGKKGPYVKPEDWDEFISRDDVVILDTRNDYEFHIGHFVGSVNPEIDAFRDLPKWLEDNKHLYEGKKLATFCTGGMRCEKLTAWMVQDFYEETYHLEGGILNYFEKTRNKNKKWKGYCFVFDNRIAVDENLEAI | Function: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
EC: 1.14.-.-
Catalytic Activity: AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA + A + H2O
Sequence Length: 255
Sequence Mass (Da): 30012
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A0A922HQP6 | MFLSSVFCPIVTMNVIVVVVVLLWLLLLCNHHHHHNASDIVPVGEAVANLRESLRFVLDVNQTMFYSERLENLYEWTDLSRFEQSVYGKMPYGIFDMFGWSSKDKLNAFGVNDKTNRRVPYDRRASDERPWKCRHWHYDPRVMPKVSVIIPFHEEDMIVLTRTIFSVLLNSPRSILKEVIVMADGCCNQYTNGTLSYLNSEIYSNRHQQHLLNNIEIFRMFSVELFLEYLPLLFGENVQHGKVRVFKTQERFGWSRSIHNVLSQVTGDVLVVLTSHVEVSANWLIPLLAPIVQNERTVAVPVLGQIDRHNFYFSVESPSA... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 646
Sequence Mass (Da): 74783
Location Topology: Single-pass type II membrane protein
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A0A182JXV6 | MNSPLAALSFAILTTGTIGAISTFVGTQLAPLPLFALILGVHTMLPISWPVSVVLAVLLCIVHIGYRILSQVNDFPPTLFPQLLAETVFLASASVSSLYYRIMSDAAHIDAVDGTRTGIEQRVKLECEREQQEQLLLSVIPAYIAAEVKRSIMLKMADACQRAGGQAQTRFHEMHVQRHNNVSILYADIVNFTPLSEQLTASDLVKTLNELFGRFDQIAQENQCLRIKILGDCYYCVSGLPISRPHHAANCVNMGLQMIDAIRFVREATGFNVDMRIGIHTGNVLCGVLGLRKWQFDVWSDDVTLANHMESGGVAGRVHI... | Catalytic Activity: ATP = 3',5'-cyclic AMP + diphosphate
EC: 4.6.1.1
Subcellular Location: Membrane
Sequence Length: 1017
Sequence Mass (Da): 112574
Location Topology: Multi-pass membrane protein
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A0A175W1U1 | MSAETATNPTSVPKPKQPKGILKKTTPTPPPPSQPHLQPGSSPSSSTFSQQQQQQHHHHHQQQQQQQQQQQQQQQQQQQRQQQQQHLRLLQHLAKTQLKPPVPTETFERLCQLPSDPTNPASSPSASDAHTFLTALRGFQPREYLDLIEERTILGKCGYTLCPLPHRNLRNKFKISTRLGAIAKTEDLNKWCSDECARRGLYLKVQLDNPSYVRGEDGKMETLLELLDTSSGSNEGSGGRGLMVGDGEDQKQLARAMAQLEIDKSKKQKQATAALAAERGEGGFLGQQGKVEVTIQEKATSEPAVPPSAEDGTHQTVEGY... | Function: Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 350
Sequence Mass (Da): 38621
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A0A3C0QNK5 | MTWELLLLSAGLSADAFAVAVSDGLCCHDLKKRNILTISVCFGIFQGLMPLLGYWLGSLFGALMEKTDHWIALILLTYIGLNMIQESLTHEEEKAFTLSTGMTLLQGIAVSVDAFAVGITLTAFGKINIIPAVSLIAMVTGILSLIGVYFGKRIGQKMGSWVRFAGGIILIGIGVRIFISHVFP | Function: Probably functions as a manganese efflux pump.
Subcellular Location: Cell membrane
Sequence Length: 184
Sequence Mass (Da): 19822
Location Topology: Multi-pass membrane protein
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A0A8T0V1J6 | MASGGWEHCNLRCMGVALSVAAGLLGACMPEIGARIFAIGGPCTEGPGMIISKDLSEPVRSQKDLDKDAAPHLQKAVKFYDGLAKQLVSQGHMLDVFASALDQVCMV | 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: Cyt... |
A0A8J6E0L9 | MGIIKELVVDYGHTSAYLKGIDCFIAACMLNLCILFGYVFLVGKYPYYSFLAAVFASVGMATLLINLRLQSAAHMDKGIPRKPFLEFVFAAVVLIGVCFHYLG | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus m... |
A0A1I8GHX2 | NRTTSEQSRSSNLRNSGSYANWTALLVSTMEQFSFIAKRKEAASMVAGGLLSYVLMQNDLELRDLAALVRDRHAAAEIQFALSNSPLATSVGCPANATCIGLPTRIFHNYSYWNVVLQPSLVPACASNCRLIADHSQAHALLFHAYDLPSRRRLRRMRQTLPRNQLWIYYSIESPMQMTTQRCGQHCLKATWLSFVDDTLAYFKQFTFPSYLLREYPDTTEEATYFNWTMTYRRDSTIYTPYYRFEPVVSATGEKHSGPIALPPKVSLTEKRFLSFIAVSNCYPSNRRQEILTELAKHMELHFYGRCGDRELPDSQSMVD... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 467
Sequence Mass (Da): 53799
Location Topology: Single-pass type II membrane protein
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A0A1I8GDW7 | MATRGQKQSDEQRLTELHDKLSQSKRVLVLTGAGVSAESGIPTFRGSTAGSWRGFTISELACPEAFQRSPSQVWELYHYRREKSLAAKPNLAHVAIAKFEQFCLKRGIDFMLATQNIDRLHQRAGSSRVIELHRSLFLVRCTACDSVTENYDSPICEALRGRGDPSPQADSTPIPEDQLPRCAGCSGLLRPYVVWFGEPLNEGELSSVQEFANMSDFVLVVGTSNAVYPAAMIAPDARRSGAQLAEFNLDASCSSSNDVSYFVAGPCGSTLPKALPRL | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo.... |
A0A267DLB3 | MKSGSPQFRFGLLSSNSGGGGGGGGARHPTLFASRSFVLLFAAIGLMWLYCFTMSSWGASSDRQDSEILRQQLLDLSKKYVKSLASETGEVVDGPYSGRLTGYDLKKTLAVMLHDMMRRLDRIENRLFSGAGGVNCSGSDSRLHEAKLRDAAMSRQTQPPPPPPIQVQQPASSSLSGAAPAPAASDEVDASMLLSGYQENCEIALESKFEYPDCEAKVEWMMKHWRDDPCYARHGVDGSECSMKIFLSEVEEFCPILPFRQHLLRQNESVAWVNRRQQLDNGAVARESARLSLLEQLAGAPGLRERVNQRWQSLASAAVD... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-... |
A0A267FTL8 | MLDCLRRGGRLCATRRQRVFILAFLLALGLLHPFVTLDNHIKKTPEKQKPEISTDSTGFRTTWSYNVTLSNSAVRLHQMSSTNSSVRAPDAKQNKEIALVVLAATRPEVHQLVRQLVAQKPDSGFRIMISLDGTEKQTNEVLQQIETPEVKLLRLSDDKSHKFKPSSDTYVKIARHYLRVLDHLILKLNYSYVVLMEDDLLIAPDFYQYFSSLRRALDSDESIFCVSAWNDNGQIGLVTEDPQLLHRTDFFPGLGWMINRRHWLQVRKVWPKTQYDDFLRLYMLNNRLVCVRPELSRTFNIGRNGGRVLSGKTGTARRSI... | Cofactor: The cofactor is mostly bound to the substrate.
Pathway: Protein modification; protein glycosylation.
Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
EC: 2.4.1.101
Subcellular Location: Golgi apparatus membrane
Catalytic... |
A0A518K451 | MSKQRIGILTSGGDCPGLNAVIRGAVKASHQLGYDCVGFLKGYEGLYDPVQYVHLTPSSTRGILSQGGTILGSTNKGRFAATVGVQDRQEIEPYLIEGVKNTIEQLGITGLVCVGGDGSLAVAQQFHEQGIPVVGVPKTIDNDLSATAFTFGFDSAVECATDALDRLHTTAASHERIMVLEVMGRHAGWIALHAGIAGGGDVILLPEIEWNWDHVCHKILQRESQGKKFTLVVVAEGAHLPGGDLVGEQRSGAQMKLGGIGRTVCDEIEHRLQREVRLSVLGHLQRGGQPTTFDRVLATQYGAHAVRLVHQKKFGEMLCY... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic Activity: ATP + beta-D-fructose 6-phosph... |
A0A0N5AJZ5 | MALPLERLNLDDAFAFLYEKSVYEPVPPFHLAIYLLTRTLTAVLKEQVRKEDVLKQKDLVEISFIIYTMLSLSSLSYPEFCWMIYEPLNRFHHSLYPRFLKSLNEYCGTIEMLVQKDEVLAHEISIRRRRLLRFYGQQNFATRDSVVGIFIRKLALARSRQSISDLHRSHDCWLKWLLDKKPSNQKDLLGNCNSTFYFNSECLNTLQGVVDDASLLTPRVKDICLTAGSSANDRHIVAVVTSTNNNALKTSGEADKSSHNEEGLLSSGSNIFRCEVFAPTVSSSFGSQLSDNVPEAVANELLSSARARAFMERQIHLLHV... | Pathway: Protein modification; protein ubiquitination.
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degra... |
A0A0N5AY98 | MVIKTISSAELKSRIFHFVSKVFSANVLAFDKGFALTNTKAAKTWTTITVEDHNLASKVVIEFRIVCAEQFYGDFCERTCIPSGTNVICSSTGTLICAPGWSGEKCDQGKPVCKQCGANGRCVQPGICQCDIGWTGKSCEKCLVKPNCVHGTCQKPNECNCEKGWGGQYCNIGKNPCQNGGFCEVIADGFLCRCESGFYGHFCEFSVNSCLTAVCANGGTCIHKPGGDYECRCLPGYIGRNCDIKDISCYNFPCRFLFIIFSRNSNTLCFSKWKHMYSDALRSSLLMWSMLSRSRLQND | Function: Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Location: Membrane
Sequence Length: 299
Sequence Mass (Da): 32982
Location Topology: Single-pass type I membrane protein
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A0A0N5AUR7 | MGLSIMSEEIVQGIRFETTAPAIDIAIEEMHEQGLLTDVNFTVFYGGKYCTLLDLTTEALRLVTQQNISILFGPVSTAAAAVVSPILLHYDVPNILWGPAPKSEFGDKGAFPTTTFLIPTAYSFGMGLLAVCKEFQWNDIAFVYSTSPKDIVCIHIANEFELAMTSHEHRVTVNLKMMLNLNNDEYMNKVLSRIRDSVRVVFACLQNSEDMRKFMSVIHEHGMTNNEYVYISPNTYNYSGGKWNDGLDDVVEIAEKYFFFLGNIQNVNTNEIKVFNEKVLERSKLPPFNCQNCTSVSNYAYYLHDAVKFYLLRLNDILSD... | Catalytic Activity: GTP = 3',5'-cyclic GMP + diphosphate
EC: 4.6.1.2
Subcellular Location: Membrane
Sequence Length: 1000
Sequence Mass (Da): 112956
Location Topology: Single-pass type I membrane protein
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A0A7R9I5M7 | MIDSRSLRKGRRRTDVPTRVEHMSKELLEVTLRKKKECNAKALLIVERLLEETVSKDWLLDCLKFINKSHFEDVVEERAIISLCGYPLCGHRLKSTVAKQYHISTKLNKVYDITERKNFCSNYCYAAAKFLAKQLLTSPLWIHDREEIPTFKLLPSTVYRNPAGEEVDFGVTRLDAGEKEITTKPVDKAENPDIFEHSSNIAEIKEASDGYKNVTLSSSNILSHSAGYLNSSNTVSGEIEGVSSNLQIIENKVDFKNVIIPNKGIQDCDETLKDLSAHKVSAIESEPASGCENKPPISTPTPTHGKNTPLSQYSAPRNDR... | Function: Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 507
Sequence Mass (Da): 57134
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A0A8T0WA48 | MPGVPSASGSRMWSRWRDKITFDRLQKVGRMADQFAKPRSNPTETRDGVTLPSYRGDIINSDAFDEKSHVSDPEMLIQAYSQSASTLNLLRGFARGGFTDLQRVT | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
Catalytic Activity: D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate
EC: 2.5.1.54
Subcellular Location: Plast... |
A0A1I8FXV7 | MEMSYKQLQQQQQQQQQSSLLQSEQALRVHLPISQAYHQHPAALHQSTSLQYRPPSSGVYSNSQLDEKCPGDEDGISRPCSALYNELSLGSHVTASFVPAGICHEQLAWGSIGPSGGGCACPRLIFLAVSCDSRDRPHLTDRQTLLSPVVVCGSAASSTDCPAPGRCAIVSMPHAAALRQGFWNVSVLHSRCNSGVGGGNGDVIDGGIGGWQEYLRVGSESLASSGYCQLDGASSHLMADRLGRYCLVGESLEGGSAVKRLSLIAFVSSAGATVAGGIGDFCLRLHVVPDTPDAVQSVLSQHQHQHQHQHQHQHQHQHQH... | 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: 563
Sequence Mass (Da): 61054
Location Topology: Single-pass type I membrane protein
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A0A1B6GGA5 | DVLFTGREFFVGLSKWTNEAGARAVAAAFPEYPCTPIKVGDTQHLKYMISMAGPDVFCVSSSKSSQEVLKRIEREATFGYQILTVPEEIAANVLYINGTLVHRSEDEIPDSCKVFYDKIDFARHAVNVSELVKLSNSGLSSCCLLLRRSRHIRSL | Function: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
EC: 3.5.3.18
Catalytic Activity: H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine + L-citrulline
Sequence Length: 1... |
W2SCA4 | MSALSSQKITMRRVKHDVLCVGLGASALSLAVAYRERDPGADIVFLEAQPKSSWRPIRKLPGQDMGTTFMHDLITTENPRSKFTFVKYLHETGRLVNFTNVGKIKPAGELFEDYLRWVAEKFESQVKWATQVVSIEGGRDGSGVVDEWTITAEDRLAGSKTIISAKRVIVAVGSQSRVPKALGGGGTAVVHASNFQERLQEKLRTVSHGANIAIVGEGQPAVELLEYIQSIRGTHTTTLFTEQPSLQPAASSSFANDTTIKPSLAALKSLPPELRSRASGQSGGAVAPAAQSQLIERIYEIQYNQRVKEADEENLRLQVK... | Pathway: Siderophore biosynthesis.
EC: 1.14.13.196
Catalytic Activity: L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+)
Sequence Length: 468
Sequence Mass (Da): 51157
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A0A220QLP2 | PGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGAQLNYXPSLLWXLGFVFLFTIGGLTGVVLANSSXDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLXPKWMKIQFATMFTGV | 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-cytoc... |
A0A1I8JNB4 | MPMPRTPQSMMRTRFFGCAFDGFVGTSPIVLTTSKRETTTLAEHYNCEPLVSGVAVLPWQPSRRCEWRQDEGLIVECLAEDAGSAGAVLAHHVAHLNDEKSGTTRCTGCSTSPLADFQPRAQGREVHRRSAGASSPNTATVNRGKVVAGPSRSLISILEPDLLGDRVLRLGNLVGIFRGDRGGNGRSKSHQNQGEEGVAELCHGYCNASAPGSHVCSVGCLFVPAVGWVLSSVVPTNDDGFCWGDAWVDAKQRDGQPSCSACRTVSRLRFSDKRQAMELLDVSSFVSTLTVWFYQRCGNVAAGLPAPHFVLSTHEMTGCS... | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 704
Sequence Mass (Da): 78062
Location Topology: Multi-pass membrane protein
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A0A2I0LGJ3 | AVTQVSVESPLRAICLPLETVYERFQQPAHGFRDLLGQYLSGEKPKGILETEEMLRVGAGLTGIGELALHPDGSLHLQPPARGGDEEIGDGGPEDSCVICLSRPRECVLLGCGHICCCFRCFQALPARLCPICRGPIDRVVPLYQA | 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: Membrane
Sequence Length: 146
Sequence Mass (Da): 15768
Location Topology: Multi-... |
A0A7R9I011 | MPMLFTFLKVNQFYKQRVHILLIMFCFHACHVCTVLSPRLMLRVSGIACISKRTSTATLDQVQRNLALCFSVTGNCNRSGVTLLLVSLSQAALEQVQSNFAPRLCHRLRCNRSGATLFLYAPEISWSIRTVERKWVLCVLITALRSETRLENDKDTLEALKELSTFFTENTLLARRNLRSKIEKRSIVINEVNLISMRDNKLADKLAHKKLVARQGLYPNSLFHAPSTLDVHSIVALAIT | Function: Required for normal Golgi function.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 240
Sequence Mass (Da): 27245
Location Topology: Peripheral membrane protein
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A0A833VNJ2 | MENPPAATAPAVAAAPVADDADPASRARELVVSFSRRYQHLLDRATPFVRKRWLGLGCLALLYLLRVWLVEGFYIVTYALGIYSLGQLVSFLSPMVDPEIQEFLDGSSPSLPTRSTDEYRPFVRRLPEFKFWYAVTRAFCIAFVMTFFSIFDVPVFWPILLFYFCTLTFVTMKRQIQHMIKYKYVPFSFGKQRYGRKKASATEDASLMKE | Function: Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.
Subcellular Location: Membrane
Sequence Length: 210
Sequence Mass (Da): 24204
Location Topology: Multi-pass membrane protein
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W2RNM6 | MPQDLPPTGGYDAVQYRRNIPTRGLRPIWYMAIMGGVVGYGWYHLFHGQREKIEYAREKAWARIHLTPLLQAEEDRDQARRYYADLAREKQLLGSETRAYNSDRYVLLFEWILKSRESSSAGGPIWFMLLMFDALAGLYGRHSRRVRDGRNDVGLGEEGEQDAGVDSKGERGTY | Function: Complex I functions in the transfer of electrons from NADH to the respiratory chain. Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 174
Seque... |
A0A401XN68 | MTKFGIIREGKIPVDKRVPLTPGQVRLLMDKFKVEFYVQSSPHRAFSDDEYRERGIPVVDDLSMCDVIFGVKEVPIEMLLPDKTYIFFSHTIKKQPHNRQMLRSILEKRIRLIDYETMVDDRGRRLIGFGKYAGIVGAYNGLLAYGFTTGRYHLKPAHKCFDMTEMLDELTKISLPEDFKIIVTGHGRVGEGVHEILKAAEIAEVSPYEFVFREHTQPVYAVLKPTQYYKRKDGKVANKKEIYENPIGYESDFIHFVRVADMYITAHFWDNRAPHILTNDMLLDPFCQLKVVADISCDVGGPIACTIRPSTIENPLYAYD... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 3/3.
EC: 1.5.1.7
Catalytic Activity: H2O + L-saccharopine + NAD(+) = 2-oxoglutarate + H(+) + L-lysine + NADH
Sequence Length: 409
Sequence Mass (Da): 46791
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A0A195FFT0 | MGFDVNRFQGDVDEELVCPICSGVLEDPVQDIDLFFSKFLACYILLLYKVVVAYKKTTMIKRTLSEYNCPPHVIDELMENCHERKWPPGLNSLETRQNSRRQYDNYVCKRVPGKQAVLVLHCDNMHMPEDMMVEPGLVMIFAHGIE | 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: 146
Sequence Mass (Da): 16914
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A0A075JPQ6 | MLKQGIILAGGKSSRMGTNKSLLPLGGKTSIEHIFSEMSSFTDEITIVANDPTLYRFLNTDIVADRYTGKGPLAGIESAMYYKKADLYFVAACDMPFVNKNVYGWLQKQISHHSASVPIFNEKIHPLAGVYKREVLPKIQEQLVQNNLRVKSFFEHIDIKYVEDYDDIPREVLEKHFFNMNDPDQYSEAKSF | 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: Cytopl... |
A0A151JT77 | IIGSSIRIIIRLELGSCGFFIVIIGGFGNFLIPLILGSPDVAYPRINNIRYTRVYFTSATIIIAIPKGIKIFRFTDIILSNSSIDIILHDTYYLVAHFHYVLSIEAVFSIIAGFVY | Pathway: Energy metabolism; oxidative phosphorylation.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 116
Sequence Mass (Da): 12987
Location Topology: Multi-pass membrane protein
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A0A0L1J1M9 | MAAVAPITGMLRRNLVLDLSTAFGFGTTFGYLWWYGYHLPRVRARDNYYVRLEQERAAAQE | 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.
Subcellular Location: Membrane
Sequence Length: 61
Sequence Mass (Da): 7084
Location Topology: Single-pass membran... |
A0A833R3P8 | MATRLASSFWQQNVHLSIILPLSVLAFTFLILMHSTKFRLPTFFASCHSTIPSDDSIMQSVSRPDLRILVGVLTTADSYERRQLIRLAYSQQRGTYHHEEVDVRFVFCSLSKEEQHIIVALEIMQYNDIIILNCTENMNKGKTYDYFSSVPTLFRDHPHDYVMKCDDDTYLRLGNLVESLRNKSRVDVFYGLVNPCYRADDMDYRMNSSFMSGLGYLLSWDLTEWIAESEIARNNTEGPEDIVLASWLNTAKKGRNRYHNFPTFYDYKGESDETCFRHDFIPETIAIHMLKGNLEWARTLNYFNATKGLKPSHLYHV | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 317
Sequence Mass (Da): 36939
Location Topology: Single-pass type II membrane protein
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A0A1I8J8N5 | GPTPPPESERIRLPQGLLRRDAELAARHVDLAEGQPQRLLIVAKDRRKNCVVGQRYPPSFGNQFLASGSWLHASRSVGDYFTILAQGRSNSFHQVNRESPVTSFTQLGLRPEVAAAASAAVGSDRPTLIQCLAAGPLLSSWNTACLAETGNGKTLAYLAPLLSNLLSLPEGVDRSRRCILVVCPTLVLMRQIAAAAGLFCSQLGLRVATADEAKREAELGVIVGVPERINDLLRCRADAGAPLLPTACVLDEADCLLDDSFVDGTSALLGRLFLQTGEPQHGVPMGAQVVLASATMPPSLEEALGSGLLPSDSFARVATP... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 470
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): 50067
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A0A2R4MGG5 | MDVPFYPTFKEKQLTSTPPPHANPINDNDDGAAPPPPKRLSAADAIVMGMRFYSRLPTGDSPHLPLYFGKMIQFLPISSLIIGVFPALTILLLGAFGVQSLFVATLAIAMSAVITGAMAEDAFGDAMDGLFGGHDVARRLEIMKDSRHGTYGVLGLIAPFMLRVITLGTLIAMSPVAAALLWLASAMIARQTAPIVAVILPPARSDGASAGAGILSKRDFMSGLVPALILFCLLVWLFAGPIALFLALVLGAGLSAFWVNLLKRFLGGQTGDTIGALQLLLEIAALSAFILI | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-riba... |
A0A1B6FJ80 | AATLQCPVLFFCRNNGYAISTPATEQYASDGIVVRAAAYGMSGLRVDGNDMIAVLQATKTARDYCARNQRPFLIEAMTYRLGHHSTSDDSSAYRSQDELNFWTQNFEPIA | Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
EC: 1.2... |
A0A1B6H231 | YQYMAALAERGHQITVLGVDKPKIKIPNLTTFIADEVYEAVFSNHSASEWMSDSKIGLMYPVFKTWDEASSTTILHSKALKELISQKRNIAKPFDLIIHDHGNAHALLGLVPLFGNPPLILATTFGSPQWMTFRAGNIFNPAYVPSMITSADHPMTFYQRCENLFYYIFLEWYTRFVTEPFQDQLMREVFGPNLPHVRDIVKQANIIIVNHHFALNGPRPTLPGLVEIAGLHISEPKPLPQDLKDFMDGAEHGVILMSFGSNVDSTWFAEGFEDMVITTFQKLPQRVLWKWDKDLPNISSNVKLSKWLPQSDLLVHPKMR... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 419
Sequence Mass (Da): 47963
Location Topology: Single-pass membrane protein
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A0A922KZY3 | MLPENINENQIKNWAQNELNLDLNEALIHEMLKKPCLQQVLNYVVWKVKNKRNAQKFFNHATMFRVLRQIDDNNQQFKDVIINQENMNEPSLFQSDMVESFDQFYANIAKSNHVKTMKDKFNCQNESKNNEKLIEQLQEAIESMETNVFNFNLDHHHQHCISSNGSSTEIAKTLDMNLKNISNLYQTIQETSKENMIKIDPNDAVKIESSDMTARINELKDQLHRIRSSTLSWMNIIDEKKEFETKTAITTTTTTTMNITGSLSPFVYWGQTSDSITLIIDLKNVKSPVIDLKEKSLYFFAVGIGAKGLNEYSISVVLHS... | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzy... |
A0A1I8HA39 | MGGGHEPEPTRESLYTPVTSKAFTDTWLFKAFDLPTTWFKENVIDKYRKKYPYYHRRYPRVPTIDQCFVDDELCNLEADEQYKRDRLVDQEIVNILRRRREQCFQWYGRQRDLIEKHCGQIQKDYDEASTNYFIKHGDMGYAHNVKNALMKQKHRMLWERKYGEVGSRGDPHKYPNQLMKILVIGDPTVGKTSFVHRYVNNMFQTDYKQTIGVDFALKVIRWFTSMTRVYYRDAHAAVIVFDLTKRSTFDGALKWKRDLDSKCALPDGSPLPAILLANKCDLLSGERQLQLSEIETFCRENGFIGWTEVSAKEGVMIEEA... | Function: The small GTPases Rab are key regulators in vesicle trafficking.
Subcellular Location: Membrane
Sequence Length: 381
Sequence Mass (Da): 43960
Location Topology: Lipid-anchor
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A0A1I8FWF7 | MALIDSATIGTFYDVAVNQPDSLTLEKILDKVLPLSLLDINADQGSNVSKSVEAILALLSAKHPSWESYSSSVRHFDNSVTCGLVWTKNYYAYRCRTCAISQCLSLCEDCFKAGNHEGHDFNLFRSSSGGACDCGDPDVMRPLGFCCKHGEQNAAKLPSAPSELVATARAVLPRLLLLLTLHMRRNHAVSADDCISGAGWLFDLLKQMTDLGAGIHRILCDALTDERLYSASLSAPAAHSCHRRIYADSELDSDFASCHDNYTDAIGQLMSVLPDDGSVQLGGQPIVEGLRHRSLLDELTFWMVKAKFPQPLISLLLAAL... | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
... |
A0A1I8JQ02 | MEVIDLIISDCRPPRPLAQQEQALVCLVLRVLASLAASNDRDNLTPDEEAHYLRLVSLVHDLLLMPPSLDRRPLLESCLEVLLTVPLIAFEELTTPLEGTVDVACRFEDKNLSAVNSLVEFLRHCLREPPAPAASAPASPVLTEASISQRSVRCFLRSLILPKHPHLPAASSSSTTSAAAAAGGGDIDTEDESVTETEANSLLSDPVSPDQRRRTRRRRSASASGSCGSSSSVWLDRLDSFCLCCAKRMPPRWCGTQPEAGLTQFPALVHSLQIPCHPTSPTATASGGSLDAYSSDSSEEEILDPEVSVAACCSQSRAAT... | Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
EC: 3.2.1.96
Sub... |
A0A1I8HMF8 | MSIETVPNELRNLRACMICGLIKTFTQFEVDGCDNCEDFLSLKDNKDMVYDCTSANFDGMIGLMSPDDSWVARWQRISKFQKGIYAVSVSGTLPRHVQRMLSERGVPYRSLDVSENIDPASSNKRMRIEYTAEPDNSALSAPFIVYTDADLLISNSDSDNVPESEKQLLPNLLEQGWLTRQHLLRYQPDNVKSRQLNKEISAYFNPSRFATRRVHANNVDGLNAPFNSSGFHFGKADRTEITVKLWHEAWGSKPLPRVQLFVNISPIDRQHYVIVPDCELQLNQCLTPFALMSGLHLLLLTPGTQYRLGFNSLLAYASVN... | Function: Specific and highly efficient GDP-D-glucose phosphorylase regulating the levels of GDP-D-glucose in cells.
Catalytic Activity: GDP-alpha-D-glucose + phosphate = alpha-D-glucose 1-phosphate + GDP + H(+)
EC: 2.7.7.78
Subcellular Location: Cytoplasm
Sequence Length: 490
Sequence Mass (Da): 55234
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A0A0N5AAL0 | MSETGCFVVPQKKIATVFDLEKWCHSKASAVHPLGYADYMAMLHELNDSVKGVDSTEDIPISQNVINALEMLNNFQLLILECPPKTMKVPRYGNLAYADWHQRLTEVANDAVSELLPQEKKAAYAELVPYILDSFGNPIRIDYGTGHEAAFLMFVMCLKKLGVFTPDDSKALVLRLFAKYLDLVRTLQTTYHMEPAGSHGNPQLLTPESYLLPEMVEKCAPNNLFFDAVKFILKTKTGPFHEHSYQLWNISAVCTWEKVNSGMFKKYDAEVLKKFPVVQHFLFGSLMSIEPCGDIIDPNLKKANEICRKSDAKAASEKQ | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 319
Sequence Mass ... |
A0A167D020 | MQDSKLSNLPTLLGELKQARHRQILLLCGSRKWGIAQYKAIIRDNNALALSNDAQFEQAIWPQHLHQILGQEFQFVCYDGYSGIVPNKLTAAAGTVQAGGLLILLLPVLDTLKQWCDPALEKWLSEGETPSSSPFLVRLAKLITQHQVWLISEQANNDLPEHYIAPPTSLNLAPQAHSLASIIKWLSHKTAAPVLLSADRGRGKSTVLGLIAAHYKKQNIVICAQQRRAVQNSFKHLAIELGIPEPSMQQNSLHNLTYIPPDTLLAAQPDIDILLIDEAAAIPVPMLKQLLTCSPKVVFASTLVGYEGNGRGYTLRFQNH... | 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... |
A8R2C5 | MPQLDTSTWFXTIISMIMTLFIMFQXKISKHLYPSSPEPKSTAAL | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... |
A0A8J6APZ0 | MVRNNRNTEGGTTRSENSERSDPQILFDVSLEVAHKVGGIYTVLKSKTPFFVENYGDNMVLLGPYIPKDAAFEFEDLPYSQLGPAIEKMQRERGVTIHYGRWLVEGNPRAVLFDLMYPAAFTPTIDRYRRILRERFNVGFGEFKDHNAFQWDAFVFGCMVAEFLDYVRREVFTPTNTPDIVVHFHEWLSAIGLLLLKENTRLDPAKYSPPYATCFTTHATVVGRYLCAGNQDFYRAIQYVDADREAGTRGCWTEHAVEKSAARECDVFTTVSEVTATEAQHILGRKPDVVTLNGLPPTNLSLLHHLQIEHQNSKTNITKF... | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
EC: 2.4.1.11
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP
Sequence Length: 649
Sequence Mass (Da... |
A0A1B6FJC3 | LSTLILFIQIITMKVIFTKKLRNPVMLPKGFEGSVRVEEMIETREQLNYEERVEWSHGNLLNILGIIRNNSTKKMNISNVLSTFAFTIRDLDQLRSHEDRKHQRADEWSLYTRQVYKQLQQEVVQYNDILLLDMVDVYRNLPQKVLLFIEWVYKHHNVKYILKTDDDTFIDIPTVKVELNKHSDWDWWSCFRIGWPVHRRGKWRENVYQQEVYPPFPSGAGYVLSHHVLTWLNTRIETLSTKYQGEDVALGIWLEAMNASRHVGEACYWACNEKCHSHTCNAMQLTVEEMYQVWSDYKECGDKICRCPNK | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 310
Sequence Mass (Da): 36877
Location Topology: Single-pass type II membrane protein
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A0A1S9CA33 | MKCIIKTEGFGDMVFELYPEHAPITVENFVKFVNSGFYNGLGWCRLSKDYVIQGGAINNDINTILETDDLCIKGEFKANGVENPVEHVRGAISMARTFESFDSARNQFFVVHKDAHKLDGNYAGFGQMIEGFEILDLLASQPTYGPETWHKPIDIPIIKEIKIL | 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: 164
Sequence Mass (Da): 18462
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A0A267DZ92 | GSTCQSIKLIMESAPLKTWELSLYETKRRPQEAITDNTEIAVSPRALHSELMCPICLDILKHTMTTKECLHRFCQVCIITALRSGNKECPTCRKKLVSKRSLRHDPNFDQLIAKIYPSREEFEAHEERVLAKLSKFASTVSCDSAASGGAGGEPGSQQRPHGGAKKRQRPSSSQQAAGSTAHQQQADDADEISSNGSVDNHISSNHHHGYGNKRSRDDADSCLGNGAAANRGGAASSSARIASTFSSASVDTDIELLLKPLPSWSAGRGVETKYLKTVCTATVAHLISYLRLRHSLDRPEATSSVAAAAAAAAAAATAAA... | 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: 413
Sequence Mass (Da): 43424
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A0A0N5A9S8 | MKTWPDYIAQVRFDQPWELPVIHVIYSIEDLNLQNERYVFTDFDLSPGLGNEMFQYASILAAALDHNAKVIMPMRCSLRRAFDLDAVFVTSEVANSLLGIYGPQTRAEAQAAIKKVFTFLPGIRELAKKEFDSAMAERKKHLQTTASITTVGVHIRHGVDIVKISSNYNHGHATADRKYFLHAMNYFRKKYGTVLFIVASDDMKWAKENLFSNETGEIHFLPSKYREVDFATLAMCQHTIASTGTFSWWISYITGGEVTYYARWPREKSVLSTYVNKTDFFPPNWIPMV | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 289
Sequence Mass (Da): 33177
Location Topology: Single-pass type II membrane protein
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A0A351ZCN3 | MTVFLCGFMGCGKTTSGKLAAKKLGCGFCDTDDLIVEDQGMSIPKIFSEKGEPYFRQVEAQIVTGLCGKHLVAACGGGALLNEDTAKACREGGVVIFLDVPFEDCYERICGDSNRPIAASSTKEELKARYDARKEVYLAHSDIRLECTGSPVEIAEQIAAAARKLK | 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
S... |
A0A518KE95 | MSGQSAVGSGQQEDDAPRAASSRPRLSLVVAASSNNIIGRGGELPWRLPADLAHFKRLTMGAAILMGRKTYDSIGRPLPGRKSIVLTRDVSWRAIHDEVLVAESLDQAIAIAAQAEVELKAQVFVIGGGEIYRLALPKADRIYLTRVHTTVVEGDATFPELNSSEWRLVSSADHPADERNEHACTFEVWERRSV | 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
Catalytic Activity: (6S)-5,6,7,8-tet... |
A0A7R9PMX1 | MIGQLFKLRAGKLAGDIRMLCWRARTCTSRQSLVLGEALLQVDVEPRSVCLIQVGLRSVRSVGALLQTSQMGAELEIGLLSAFNLATFPLIYFFTFLYYTDTVSTSLVLLMYLFHLYGHNFLSAASGFIAVTVRQTNIIWVGFILLKIVENVLKDKAIAYKRKVTPQTLRSSKYFQILILTIQQSWKSGFSSFSALIIDILHESSLFIIVCLSFVTFVIWNGSIVVGDKNAHQAVLNFPQLFYFSLFTLCFCFPYFITFTPTFFHWCVANKKSLAIISLICVLIVGFNTHVHPYLLADNRHYTFYIWKRVFERHFLFKYM... | 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-diphosphodoli... |
A0A3C2BA26 | MKKILSFVMAVVASVSFFCSTETKAFNFPLTSQIKSESAMVINLDSNLTIHEKNADVQQSPGALVNIMTAVICLENSKNLNEEITIDSSVYSGLSESEYYMDLCYADIYDGDVLTVEDLLSAMMLTSSIEATQTLAYHFSDGNITEFVNMMNEKAQEIGCTNTNFTNPNGLYDAKQYTTARDMALLTEYALKVPHFEEIATQTEHTPSHPNSERHKIEEGEDPWIWTHSNLMTDTESDYYYVGAKGIKTANISSAGRNLITLGSKSGNNYLVVLMKAPFTDAYGERQFYHLDDAEIILDWIFNHFSYQVLLSDSIEIDEI... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanin... |
A0A059BLX3 | MKPPKSKQSRKQRRLSEVQEIELLDAWIESRKPDAGSNPLSLPPPPPPPPGEQDAASLPPYAGSARFDQLPISSRTKDGLRDAKFVKMTDVQRASLPHSLCGRDVLGAAKTGSGKTLAFLIPVLEKLYRERWGPEDGVGSIIISPTRELAGQLFDVLKVVGKYHGFSAGLLIGGRKDVDLEKQSVNDLNVLVCTPGRLLQHMDETPNFDCSQLKVLVLDEADRILDVGFKKTLNAIISQLPKHRQTMLFSATQTKSVQDLARLSLKDPEYISVHEESVTATPNRLQQTAMTVPLEQKLDMLWSFIRTHLKSRTLVFLSSC... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 533
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): 60166
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A0A6M6E4Y1 | MKQTIARSLIVVMAVFIIIAGKFAYIQLFQADRLQKETVEQRVRKIKEMPERGEIKDNEGRVLAMSLNAKNIAVYPNLMKSKETREKVAKVLSDVLELPYKDVLKKVGTRDSKGKLVQWTSIANRVSPEKGEKLKDSDYAGYIEISNAPKRYYPNGSLASTILGFVNYENQPGAGIEMSLNHYLSGIPGYTVAEVDHSKKEIPIGFQTASKPVPGQQITLTIDSYIQYTLEETLKKAAKDMKPKAMHAVVMDPNTGKILGMASYPSFDPNDYTSAKPGSINLNPASYVYEPGSTFKPEYMAAALDGGYINENSSWYDGVG... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Sequence Length: 699
Sequence Mass (Da): 76948
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A0A8T0MGU8 | MEAQNHEVAALVEKISGLHAAIAKLPSLSPSPAVDALFTALVAACVPASPVDVSRLGPGARKMREELIRLCSDAEGQLEAHHADALAAFDNPLDHLHRFPYYRNYVDLSRLEYDLLARHVPGLAPARVAFVGSGPLPFSSLVLAARHLPGALFDNYDWCAAANERAKKLVRADVDLRAQVVPHGRRRGPHGGARGVRRRVPGRTRGVGGRGQGEGGGAPRPAHGRRRGARGAERAGSCTPSWTPRASGAAGSTCSPCTTPTTRSSIPSSSRARWRTTGTGACAARRRPAPPPSCRRGRSRRPAGRRCPSERSHGPGRRGE... | Function: Synthesizes nicotianamine, a polyamine which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
EC: 2.5.1.43
Catalytic Activity: 3 S-adenosyl-L-methionine = 3 H(+) + nicotianamine + 3 S-methyl-5'-thioadenosine
Sequence Length: 390
Sequence... |
A0A1I8GBZ3 | MNSLLKLNKVIRSSKMVLRSMSSIKLAGVLPPIPTPFNAKEDIDFDKLQINFEVWNKHSLAGYVVIGTNGESASLTLDEKAALVTKCRQLMKPGSLLVAGAGCETTRATLATCERLVEAGADALLVLNPSFFRNHISEEALYDHYMTVAKQSPRPIILYNMPASTGYDLPVSLMARLADHPNIAGVKDSSGDVVKLATVVDAVRPGFQVLSGTGSVLHPGLQLGCVGGVCAIANVLPGPTAQLYHLHCSGDHEAAAQLQRRIIGPNGLVTRRLGVPGLKAAMELFGMYGGPCRLPLVPLSKEKRAELRAEFERNGFQPVS... | Function: Catalyzes the final step in the metabolic pathway of hydroxyproline.
EC: 4.1.3.16
Catalytic Activity: (4R)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate
Sequence Length: 321
Sequence Mass (Da): 34361
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A0A0X8FFZ2 | MGTDLPLSIGAWLIAILPMLLMMLMLVVLQWSAVKAALISLIIGLITGIFYFKLPLYGLFVSLGQGAWDTIEIIMVIWTALLFYQVCKHAGAFEAIKEGITNKSTNHLYLILMFGWVFASLLQGVSGFGAPIAIVAPLLVGIGVKPAFAVIIALTSTAWSNLFGSLGIAWSTTLGLVNIENEALTLLYTTILLFVSDIIGGFFVAWIYGRWQAIKEGLPIILTISVIHGLGQILVAQFNTEMAAVLPAILAMGAMILFARIDFYQEPSEEITVTNSPIMQDDFDNDDGGEENTGKLTINQAFVPFYLLIAISLIMLGIPS... | Function: Uptake of L-lactate across the membrane. Can also transport D-lactate and glycolate.
Subcellular Location: Cell membrane
Sequence Length: 546
Sequence Mass (Da): 59059
Location Topology: Multi-pass membrane protein
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A0A267GL31 | VNFLLIMYAPVMQLVSFILLVAFMTRRRSLHESREQLRQELGLTEGEVMVGFFHPNCNAGGGGERVLWLAVRALQIEHGNKVQLFVYTGDLDAYKDSPEFDPAAEGEMSQADKERLAGKAILAKVERTLGVGMPDPDSIRFAFLSGRDRINPARYPRLTLLRQSIGGAFLGLEAIGLANPDVMIDTMGCHFAGAVFRYFGGCKTACYVHYPLISTDMIEVVNANSVAVNNPTTNSPFKRLAKLVYYRLFALLYGWFGRRWNLVMTNSSWTTGHIASLWGCQLPRLLYPPVYVKEFAHLGPDSLAGRLPIVLSVAQFRPEK... | Pathway: Protein modification; protein glycosylation.
Function: Required for N-linked oligosaccharide assembly.
Catalytic Activity: alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-... |
A0A267F0N3 | HRLWCTGLVRHLWRRRRRQAAIVTAAATALLALLLLASALLSRPLPPPFQLESASTAIAVESIDLFDSRRDVIVLLHMQKTGGSHLNRQLVSGLRRPDMRCQCGRGGLGGARRRKWRCNCRNSRGDLWLVSRYSTGWLCGLHADFAALSACVPGQLAALDSDFERPRRLRYVTMLRRPADRFLSEWQHARRGATWRKSQPTCRGSRPPPCRTGDGAWRGVSLAEFAACRANPALNRQARMLANTSGLPCRAVFANGNRTADLLLASALHNLVGMAAFGLTEWQILTQYLLSRRLGLSFSRLFWQQDATVASNWRASGNFS... | Function: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
Catalytic Activity: 3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[... |
A0A8J4GEW3 | MRRLSSRGPVPAARSCPGMTILNAMRATRCRTVHVKAYAPVFQGYEISSSATMERTASKEAMPLALPPPPAQASPSQPAAGISTDTSAVAAAAAPTGVLGPSLPSFPKPGDTQWPPRRPFAAVALDQFIDSVGDVGRHLHRMVTEPECLIKKQKEQLVPGENGRMRLRAATKPVVLVLGSGWGAHSLIKVIDTDMYDVVVVSPRNHFVFTPMLPSTAVGTVEFRSLLEPIRTSNPCVTYLEAECNSLDPEAKLAVCTSQFALDDGRRPQFEIQYDKAVVAIGEQPATFGVPGVREYCFFMKEVTDAVALRKRIAEKFELA... | Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
EC: 1.6.5.9
Subcellular Location: Peroxisome
Sequence Length: 462
Sequence Mass (Da): 50735
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A0A2B8JCQ8 | MKKWKIVALTGITALSLAACSTEAGSDSKVVVETKSGNITEHDLYNEMKAKYGAEILDTMIQEKILFDKYKITDKDVEKRLKYVKLANNVKSDKELETLVVSTGGFKTLKEYKETIKLSIAKAKELTKGVSIKEADVKKAYEEQKTQVSASHILVADKKTADEVYAKIQKGEDFADLVSKYSTDTSTSSNGGSLGYFTKGSMVQAFEDTVFKMKKGEISKPVKTDYGYHIIRLDDKIEFSYEDLKPMLEEDLKLQKVGSSFSSVYTKLKDSYKVEVKDDQLKNDLKELEETQNAAATSASATQTAN | Function: Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cell membrane
Sequence Length: 306
Sequence Mass (Da... |
A0A4Q4UUB0 | MWKRTICAFTLGVGFLTVSGSAIEETTFPVAPFRGFQNAVYYTNWGAANYTAQQLPVSELTHILYAFADIGANGTVISSNPKIDVEQRTAWDPPRANHGRNAYGVVKQLFIHKQRHRNLKTLLSIGGWAYSPKLAPVAATETGRQTFASSAVKLVTDWGFDGIDVDWEFPDNDDDKENFVKLLEACRVAFDKYSHLHRLRYRFQITVASPASPHQYKHMDLAEMNRYVDIWHLMAYDYAGNWSVTSSHQANVFANKNITALNTHDAISHYESQGISPHKILMGLPLYGRAFVGTSGLGQKYSSVGRGGPEPGIWYYKDLP... | Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
EC: 3.2.1.14
Subcellular Location: Membrane
Sequence Length: 524
Sequence Mass (Da): 58539
Location Topology: Multi-pass membrane protein
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A0A059BR84 | ECLLGLLRTKTVIYVTHQVEFLPAADFILVMKDGRITEAGKYNDILHAGTNFMELVGAHEKALSEVDSIQDTPANRGSSSSVQNGSADANGKIPEEDESKASQKGEVIDDVGTKGQLVQDEEREKGRVGFTVYWKYITMAYGGALVPVILLAHILFQLLQIGSNYWMAWATPVSEDVKPAVTGSTLIAVYVALAAGSSLCVLARATALAIAGFKTATELFNRMHFCIFRAPMSFFDSTPSGRILNRASTDQSAVDTSMQYLVAAFCFTMIQLLGIIAVMSQVAWQVFIIFIPVIAICVWYQQYYISSARELSRLVGVCKA... | Catalytic Activity: ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.
EC: 7.6.2.2
Subcellular Location: Membrane
Sequence Length: 711
Sequence Mass (Da): 78485
Location Topology: Multi-pass membrane protein
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V6DJL8 | MWFNQLKTIVFLATLTGMLMLIGGLFGGTQGVITSFIMALFMNGISYFYSDKIVLNMYRAKVLDKSRYGFIYDMVQDIANKANIPMPKLWLVDTPMANAFATGRDPKNASVAVTSGILGLLDQRELRGVLAHEISHIQNRDILIGTIAATIAGAIGFLANMAQRMAFWSSMSNNDRDRRNNPSVISLFLVSILMPIAATLVRLAISRSREYLADEHGAELSHDPLALASALEKLNAHIADAHLKENNGMQVATSHLFIVYPFLPKGFTALFSTHPSLQKRVAHLRKIYQDMQIGDQR | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 297
Sequence Mass (Da): 32957
Location Topology: Multi-pass membrane protein
|
A0A059DHM6 | MKMITIFLGFIFLLPRGLGNLKVGFYHSTCPRAESIVHQVVQSRFQADQSITAALLCMHFHECFVRGCDASILIDSTDSNPMKKSAAPNLTVRGFEIIDEAKKNIEASCPSMVSCADIATLATRYAVFFAGGPNYDVATGRRDGIISARDEVNLPGPTFSVSQAQRAFAAKGFTLAEMLKVTCGASSSGDPTVSLDQSTPSIVDNKFYSEILVKRGILQIDQELTVDKSSTAIVAKFGLDANGFRLSFANAMVKMSNVGVLTGNAGEIRKNCRNINRT | 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: 278
Sequence Mass (Da): 30008
|
A0A8J7FE39 | MVGPAYVKAVPGDAKARQSLFFRIEARMAQVIAIAMVFATLALGLLMAAQVVMRYGLESPFLGIEELAPMLALWGYFLGMVYATRDQDHISGGIVALIFKNHTLIQVIRLAGSFACLLAVCVFGYFALKFAQFNLDLNRKSIYMRWPKYLWDFSMVSGFALMAFYYCLQIIAEIRDLKKGSDSSK | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 185
Sequence Mass (Da): 20721
Location Topology: Multi-pass membrane protein
|
A0A7R9HZZ7 | MGAQHQGARKLYGTAVRWRSTMILWRLPVRARKVRRWINNLHSVQPCLQVIYAWARDAPPLALPEGVGFQVGGKSPIQYLVLQVHYAVIDKFEDGSTDNSGIFLHYTERPLSKLAGVILLGTGGAIPPKRTEHMDTMCKIKEKKTIHPFAYRTHTHSLGKVVSGYKVRANDDKIDDWTLLGKRDPLTPQMFYPVMNNETIETGDMLAARCTMESNRDDWTMIGATNKDEMCNFYLMYWVDKTTPLEMKYCFTPGPPYYSWKTEPLLNNIPDKSASILDD | 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: 279
Sequence Mass (Da): 31858
|
A0A7R9K9E6 | MDNNQDNSIKSKWEDLNCKLSLPVMRAINKLGFRTMTPVQAACIPLFIKNMDVAAEAVTGSGKTLAFLIPLLEILQRRDEALKSHEIGAVVISPTRELATQTSEVLQHFLGFIPGLSQMLVVGGRGVVKDVSEFRDKGANIVIATPGRLEDLLMRKHDINLPSAVKTLEVLILDEADRLLDLGFDKSLTTILSYLPKQRRTGLFSATQTKEIEMLIRAGLRNPVIVSVKEKDSNRLAGEEALSTPLTLCNHYMMCEADAKLATLLGFVRAQGRKKYMLFLSTCACVEYFTVVLKALLKDLAVFGIHGKMKNKRTQIFDSF... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 450
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): 50015
|
A0A1Z4EAZ7 | NWLIPLMIGAPDMAFPRMNNMSFWLVPPSFILLLASAGVESGVGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTITNMRTPGITFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNVNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMVAIGILGFLVWAHHMFTVG | 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-cytoc... |
A0A7R9JTB3 | MILTSCCCVLSIGSSPVVSECDGEYTYEPRKNMLLWTLPIIDASNKSGAMEFSATALPGDFFPVTVNFVCKRSYANLKVTEVLAVEDDSPVKFSEETVFFTEKYEVV | 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 membra... |
A0A058ZV49 | MDKVQTQVAAVVIMACNRADYFERTIKSVLKYQNAVASKYPLFVSQDGSDPQVRKKALSYDQLTYMQHLDSKPVQTERPGELIAYYKIASHYKWALDELFYKHKFSRVIILEDDMEIAPDFFDYFEAAAALMEKDKTIMAVSSWNDNGLKQFVHDPEILYRSDFFPGLGWMLTKSTWNELSPKWPKAYWDDWLRLQENHKGRQFIRPEVCRTYNFGEHGSSLGQFFREYLEPIKLNDVQVDWKSKDLSYLMEDEYIRHFAAILKNAKPIYGADAVLKASNVQGDVRVQYKDQPDFERIAPQFGVFQEWKDGVPRTAYKGV... | Cofactor: The cofactor is mostly bound to the substrate.
Pathway: Protein modification; protein glycosylation.
Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
EC: 2.4.1.101
Subcellular Location: Golgi apparatus membrane
Catalytic... |
A0A1B6G9B9 | TTFMVLRKRDSHITFLHVYHHVAMVFFTWFTFSYIKPHHGVIPAGINVFVHTVMYTYYFLATFPQLKPYLWWKKHLTKMQLGQFVIILLYISLLYYNGCSISRAFSYIWMFNVFVILLLFVNFYIKAYVKSSQDGESKLQDKIS | 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: 144
Sequence Mass (Da): 17260
Location Topology: Multi-pass membrane protein
|
G3E6H9 | ILPGFGMISHIISQESGKKETFGSLGMIYTMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVL | Pathway: Energy metabolism; oxidative phosphorylation.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 135
Sequence Mass (Da): 14760
Location Topology: Multi-pass membrane protein
|
A0A840I5D7 | MRHLTDLSRLDDAGLAALLDLSLDRRADLDEGRAVPPRLAGRLQFNLFYEDSTRTNLSFETAAMRLGAMVSVVPVAASSVHKGESLRDTVLTLCAQGADILVLRSGESGAVSTARDAADDAGFGTAIVNAGEGAFGHPTQALLDAATLMHATGRRAVDGLRGLTVAICGDVAHSRVAASTAPLFVRLGATVRLIGPPELLPTKPFLPEIAMTTDRSEGLDGADVVMPLRVQKERMPEDRYTGSADYHQDYGISWDALAAASPGAFVMHPGPMNRGVEIDSAVADDPDRSLILSQVRQGVATRMAVLETLKGR | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Length: 312
Sequence Mass (Da): 32994
|
A0A058ZU28 | SSREHHAPSWLLSFAKNCKKLSLFLHLSTTYVNGERPGILMEKAFEMGESRIDSSTQSKLDVHHEISLVSDLIETLPPNEVPQKLKEIGLARARMYGWQNVYEMTKAMGEMMINADRGRVPVVIVRPSVIESTFREPFPGWIQGNRMVDPLILSYGKGRLPGFLVDPDTVLDVVPADLVANVIIAAMAKHGITASPSIDVYHAASSTVNPVMACDIF | 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: 217
Sequence Mass (Da): 24001
|
A0A543ARU2 | MSYLLLTVQLGLAGVFIVSAVAKMRAMSDTVRMWTDLLTAVRLPSTLAGWGSWALIIGEALTGVALLIPAPWFPIGLWPATALLVGFTGLAVVSARTELDLRCACFGRATTRLGWRHVWRNTALLLLAITGIVAWTLGAAAPTEPAGIAVALLAAALITVLAAFYDDIVDLVVEF | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 175
Sequence Mass (Da): 18531
Location Topology: Multi-pass membrane protein
|
A0A0N5AN05 | MLCAPLWSGCLTCGLFPILTYPTAEADSLMEDDLKLKCGWPFPAVQSSLYRYGSYAVMTVVFSGAKLLFSFEKLVILGLNQMTVVNRRTFMDALSDTSRPLITVANHRTTMDDPLVWSFFTWREFFANIRRFRYTLAAHNICFTNIFYSKFFSLGKCIPIIRGAGVYQRGMEYCLEQLKTSQWVHIYPEGRVTPHPIRIKWGVARLIMDSPIPPLVIPIWVQNMSKVWPPNPPYYPKFGNHVTVTVGEVLDMAKYLPLLKGKTELEKRKELADFIQGKLYELGNTVSQIQWIHE | Catalytic Activity: 1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-phospho]-glycerol + a 1,2-diacyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-3-phosphocholine + a cardiolipin
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 294
Sequence Mass (Da): 33821
Location Topology: Periph... |
A0A1E4CFT8 | MSGSELSAWVRSGPAWLIGIAYLAAYVAFDWASYVQPFDPFGITPWNPQTGLSFALILLFGRRYIPLLFVAPFLADLVVRHLPAPLPVGLLLWLVVGAGYSAATLILSSSKYGFQARLPRLYDIWLLLLVAAVSTVIVACLYAAILASANLMGWADFFVAALRLWIGELIGIAVVTPFLLLLAAGRYLKITWETLAQFAAMCASLWAVFYGPATPQLYRFYLLFLPIIWIALRSGLPGACTGLVVTQLALMFVIEFLLPGSVDTTTYQEMMLVLTLTGLAAGGVVMEREQAEYRLRLQQEAHARLTRLGSVNELSAAVAH... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 536
Sequence Mass (Da): 58273
Location Topology: Multi-pass membrane protein
|
A0A8J6DZB7 | MPLNVAFIHPNLGIGGAERLVVDTALGLHDRGHRVHIYTAHHDASHCFDEVHPETGVIPVSEMFHWFPDSIFGRFRALCVYIRMILVALNLVFFKRSEYDIFFVDQVSACIPFLKLAWRSKVVFYGHFPDMLLTDRRTLPKKLYRGVLDKIEEVTTGMADRILVNSKFTEAQFSTQFPRVGAKGRLVIAYPPVHIGSMVGQELFDTAEPENAEPSSDYQWLSINRYEGKKRVDIAIRALAEVKVNDPRTYSRTKLTIAGGYDDLVRENRDVYSELCRLAKELGVAEHVQFLRNIGNDEKMKLLREATVLMYTPSGEHFGI... | Pathway: Protein modification; protein glycosylation.
Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Catalytic Activity: alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-al... |
W2RLJ7 | MSEHIPRHLTLKHPLSTLSVIFGIWKAVLLLLALASPGPGYDTSTTLLDWPERYTLLSKLVRWDSIYFTQIAQHGHLFEQEWAWGTGITSVLAWGSRLLFATSSPSTWQITVSGLLLSHLTSWMSMMLVWLISAHLAVGTSDAKAQVAFVAALLYIVSPAGIFLSAPYSESLFAALNLLGFHLFLLGRNGHARGATARAALMTVCGGLASGLATAVRSNGILSGMLYGWDASLSLLALLDQGLRTQQVTRLLSLIVGGCAVGAGMMLPQYQGYVEYCTGHMESELRPWCKNTIPSIFTFVQSHYWNVGAFRYWTLSNLPL... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 433
Sequence Mass (Da): 47612
Location Topology: Multi-pass me... |
A0A850SFQ3 | MTDKFPGGIEVHGRVPPEYAQILTTEAMAFVAKLHRAFEPRRQELLARRAARQKEFDAGKLPDFLPETKSIRESEWTICDQPQDLLDRRVEITGPTDRKMVINALNCGASTFMADFEDANCPTWDNMIDGQRNLRDAVRRTISFEQGGKQYRLNDKVAVLIPRPRGWHLDEKHVLVDGKPVSGSIFDFGLCFFHNAKELLARGSGPYYYLPKMESHLEARLWNDIFTLAQKELGVPHGSIRATALVETVLAAFEMDEILWELKDHSAGLNIGRWDYIFSCIKKFR | Pathway: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2.
EC: 2.3.3.9
Catalytic Activity: acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+)
Sequence Length: 285
Sequence Mass (Da): 32609
|
A0A0N5AC72 | MSICKIDPEFTAWFRELAYYQWLPVILICEAFLCYAPKIIWKFLSKHRGKLFITLYKSVLLYVQDSLVKFGSYVTILYLVVKLLFLINIILQFVLLNQFLGPQYTFWGIGIITDLFRGRHWQESGHFPRVTFCDVQIRELGNVHNWTIQCVLMVNMFAEKIFIFIWFWFSIMAILTLVNLGYWVFITFEPSQSIRFVQKYLGFHRKHVDDVRIRNFINTVLAKDGLTTLRLMSENSGDFAVAKIIKKLWTNYIGEKPSSLNDSHGIVQITDEIDTAYMEDEKVAYDDDK | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 289
Sequence Mass (Da): 34068
Location Topology: Multi-pass membrane protein
|
W2RY63 | MAESIPEQSATEKTVFETAPASLKDAPSEVVAVEKAEPLHTNGVTPVPEAAPIQDALVAAPVKDNATQVTTEETLNGTSAPTQDKSTAAQPAPVQTTTGEPNGTNGVSVNGTSATTEDDTEIPLFSPTLISPEVSAILPEGYTMRPLRRSDYNRGFLDTLRVLTTVGSPSFSTFSDHFALMASIPSTYHILVILDSSDQIVGTGAVIVERKFIHNMGLVGHIEDIAVAKNQQGKKLGLRIIQALDYVAEKVGCYKCILDCSEANEGFYVKCGFKRAGLEMAHYYGRD | 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 Leng... |
A0A059CSG9 | MIKVEKDPKLSDIRTVDALKIVQTSNKPKPAYLSKILIALLSYGGVPNEFLLDMVENALGDANSVFSSKRAAPRETNSKTRPFFGGVGVNRDILDILVVDLDDDNHVSSPNSTVLSISGKRSERDPHGENEVEAERTSCSCESIEEDGSGGDGARKKLRLSREQSLVLEETFKEHNTLNPCRTKTKQTEVDCEYLKRCCDNLTQENKRLQKEVQELRALKLSPQLYMHMNPPTTLTMCPSCQRVSVPSTSLSPPSSSSVTASVIGLIGPVHKGANSNVSVLFLFQGTETKKVFLFRGTIFEQKNAFGNVCSR | Function: Probably involved in the RNA silencing pathway and required for the generation of small interfering RNAs (siRNAs).
EC: 2.7.7.48
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 312
Sequence Mass (Da): 34394
|
A0A1M5A4G1 | MQPDARLERILATSALVIIALISLGNVVVRYVTNVSFAFTEELSVFLLVVLTFAGAAVALRRNRHVRIGLLERALPERARQPLIVFQWLSGATVLGLILWFGAKLTLQEYQWQTQSPGLGVPQWWYLVWLPVLAALMLLRLTQQTLDRLRGRLDDEP | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 157
Sequence Mass (Da): 17788
Location Topology: Multi-pass membrane protein
|
B0R7G7 | MAAGASSDPDAAGGGIGMDAPESDEEAPLGEHIEEMVTRLGIVVAIAALVSIVVFPVTKPLITWMWNYVLPGGEAIDPRVYQPLELIITQVKVASLAGLVVALPAFVYESYVFMRPGLYRNERRYYLASVPTSLVLSVVGVLFAFFIVLPYTMGYFQSYTEPTADVAFALGTTFNLLLLVMGYLAVVFQIPLFIMLAIMLGVTTREWLESRRLLFWGAFAGIAFTFSAIDPTGIVPVIVAITMVVLFEGTLALLRWTGN | 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: 259
Sequence Mass (Da): 28185
Location Topology: Multi-pass membrane protein... |
A0A1B6FIC9 | FQSQDDSCVPLSINCWPSENGQGGCDVNIEYELEHTHLELNDVSIHIPLPIGCTPVVSECDGDYAHDPRKNTLTWTHAVIDSSNRTGSLEFTAATAIPGDFFPLTVAFVSKKPYADLRAVDVVMVDDEQSVKFSTETVFYAEKYEIV | 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 membra... |
Q5UKX7 | MTIMRKNHPLLKIVNNSLIDLPTPCCISSWWNFGSLLGICLIMQILTGLFLAMHYTSDTATAFSSVTHICRDVNYGWLIRYMHANGASMFFICMFIHVGRGIYYGSYMLSETWNIGIILFLTTMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIITALVLVHLLFLHETGSNNPSGLNSDSDKIPFSPPTTPSKDLPPYPIQKTTLK | 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 membra... |
A0A833QEZ1 | MAMMRALLLRKSLSSSPLFHDTTIRSCLLNMDCSAWLYCQLSSPNSYHSSAKFDLTDLTQPHLWYPNARKKKRNVFLHMGPTNSGKTYHALKRLEASSSGLYCGPLRLLAWEVAQRMNKAKVPCNLITGQERDEIDGAQHTSVTVEMADVSSEYQCAVIDEIQMVSCKTRGFAFTRALLGICSDELHVCGDPASVPLIQRILEVTGDNVQIQYYERLSPLVPLKVPLESFSNIKKGDCIVTFSRADIYRLKKKIEAGGKHLCSVVYGSLPPETRTKQATLFNDDRSEMDVLVASDAIGMGLNLNISRIIFSTMKKFDGES... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.13
Subcellular Location: Mitochondrion matrix
Sequence Length: 562
Sequence Mass (Da): 63546
|
A0A2I0LL39 | MYPTCVAFAWVSLNAWFWSTVFHTRDTAVTEKLDYFCASAVVLHSVYLCGVRTLGLQRPALISILRAFLLLILAAHISYLTLVRFDY | Function: Involved in the lipid remodeling steps of GPI-anchor maturation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 87
Sequence Mass (Da): 9932
Location Topology: Multi-pass membrane protein
|
A0A6J1IVD8 | MSIVELDFFAMDNRSLNSDSNPTLFRRHRSFKDIQGAISKINPEILKSLIASGSTEHRSDFATPIPQKFPPLSLHRTPKVDQNLSTPPPVYSATTSRMSPEIASEKYPLTIFYNETVSVFHVSRDEAKNIMRFAEKGSGTGTGIGKGEAENGKPMAEITSNQHQQLVAFDSEDDEDLPLARKRSLQRFLERRKESGVMIYRLIPAVPYGCRF | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 212
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 23835
|
A0A679HW30 | MIWNRPDLMNRLANLLWGLGLLLILVTGVLMVIRMPFFPVRDVVLAKPLERVQMEDIRAGIAPYIGGNFFTVDLKAIRQGAEQQPWVYRADVRRQGFGSLALDIDEQVPVARWGNEGTRTTSDWLNRDGEVFEVPDNSLGNAGQGLPVLHGPLDTGNELMTRYVRYSSLLEPTGRTIRQLDLSPRLSWSMRLDNGTRVELGRERTLNSADEQVQTFVSLYPQLVGNRPVVPAVVDLRYPAGVAVRYPASPAAASTPSDRKGKS | 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: 263
Se... |
A0A833VBP2 | MSNSTSLFLSPNPSPTIEIPTIAPPPPQTGVNQLTPPSPAVNQFTPPPPSDVNQLPLPSPSVNQLTPPSPSSNQLTPPPPDAIQLTPPPFGANQLTPPPGANQLPPPPPGANQLTPPPPGAGQLDPELIENKNTPNTPNPQITKSPPPVPQPPNTVPVPVLAPPPPPANPVSAPVQIPPADLVQQPPPSISPPSITAFESLPLPSPPPPVDPLIALVSPAVPVPVQVQTPPSPPFPNPIFSPLTNPTDTSSVPAVHVESPPTRDSSTMVPQTGTSDSSPATIGIALVAGFMLFCLMYLFVVCVKRLRRNWATKFPGQYKT... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 671
Sequence Mass (Da): 72676
Location Topology: Single-pass membrane protein
|
A0A158R4I2 | MLKLILLTVALNIGFSNSIEVCLFASCGCHSHDVMMRNVGKDIEEDANISWVQSSIFEFGFGLFQVPKHWNQVRTYDYDANGSALNWYINVPIDFGRPWDIRGIITYLSILIRNQKVCRKMVQSQAFRSFKQRNIVLKCRNPNFTITLMASLLNSTTVQYSNWPIADGYLTSFNVPANPSYVAKTLTPFSLLSKNCFKFVKNKALVYQSIILQIDVFDIEAKQIIYGSRSGILFEPVRPISNRIKHFGCPSYMPSKLLKMILTTLGEVNHLVIWQTNSDTKTYLVNQTIPSNVVICSWVPMKYLLAHRNILYIVTHGGIN... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 431
Sequence Mass (Da): 49445
Location Topology: Single-pass membrane protein
|
A0A231V4K4 | MRITSTAILALCLSTMAAPALSQDEGGAMASATAALKGADGADHGSVMLKQTPNGVLLTLDLKDVPAGVHGFHIHETGKCAPDFKAAGGHFAEGKDHGFLAEGGPHPGDMPNIHVDDSGALKQEVLNTRISLNEGEDGYLMDEDGSAILIHSGADDYQSQPSGDAGDRIACGVIETN | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 177
Sequence Mass (Da): 18131
|
A0A941EH50 | MAEVEARDWQRDGACRRADGSLFFSPGKDEAPEQRKQRIKAAKEICAQCPVWQRCRRYALENAEEFGVWGGLTEYERKKLIGPPRRR | PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO).
Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Function: Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA... |
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