ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A8B8PRR7 | MTSFALCGRLCRNLGSRSQSKSIGRLQTLISHQLVNHQQRRFFDLQEYQSKQLLHENGNSVQKFKVVSKESEAASVIFPEENGEMKVSKWSGFRDDISRVEEFVIKAQVLAGGRGKGKFKKNPNLSGVKLTTSPNEALEYTKSMLNDYLITKQTGDTGVLVEKVMIAEAVRLKQEFYFAIVLDRGFDGPLLITSPYGGMDIEEVAAKSDTAIRKFKLPIDYKVEFETARKLAVAAFDIQLHDIDIIDQCAKEILKLHELFLKLDATQIEINPLGVTNKRQVICVDAKVNFDENARFRQKWVDELEQLNRTETDSRDFEAR... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the ... |
A0A8D2JPD7 | MAQNLENVLSNFWALDIVSPLRKKPLEDLVCKLAEMSINYVNEQKSEQHLRNWLPWQMVFVIRMEGLALWKNNVDKRFEGVEDCMICFSVIHGFNYSLPKKACRTCKKKFHSACLYKWFTSSNKSTCPLCRETFF | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation.
Catalytic Activity: S-u... |
A0A9J6P0L7 | MIEINLKVIAISLVNFIILLFVLNKIFFSKLIIFLDNRKEEIRGSFEKIDDENKKIIGEKNKLYKEELNIKKEGSKIIEEYKEKAMEERNRTLIRTKDEVEELREKAANNLKDEEVRFQKRLKAMSMDLSTEICKKVLKEVLDEESQKKIINSFINRLEKTDV | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 163
Sequence Mass (Da): 19383
Location Topology: Single-pass membrane protein
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A0A9J6P1Z8 | MKVPLSVIIQWVIMLLLIGYFLIIGRKIRKIPRKNQNFWEMVVAKFINIVETNIGEKYKGLSVYFLVLSIFLFLCNMTGLIGIKNPTTDYSFCFALGIMNFFLIQYFAIKRNGVKGYFMGFLKPMSLMFPLNLMERVLLPISLSLRLFGNIFAAYLILEIIYEGLISISPVAAIGIPIPFHLFFDIFDGTLQVIIFILLSMINMKIICEH | Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 210
Sequence Mass (Da): 24171
Location Topology: Multi-pass membrane protein
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E4XMY1 | MKLAGAGYMEIHKQGGGIHYTVNETRKCSEERLTKLLFNRLDQMLLQGTVVAEAKSGYGLDCETEMKMLRVIKKAKETHPMKIQSTYLCAHAVPPGADAAQMTKEIVEEHIPAVAKANLGVDNIDVFCEKGVYDAQQSKEMLLAGRAHGWAINFHAEELTYIKGAEMGAELDARAMSHLELVSDAAIQSMAAKKTAAVILPTTAYILKLVPPPVRQMIQNNVVVALCSDYNPNVPCFSMPFVMHLGCILCKMTMEEAFNAATINSAFSLGLTDSYGSITEGKVGSCLVLDAPSWKHIVYQLGNHQNVVKHVILEGRIHS | Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
EC: 3.5.2.7
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate
Sequence Length: 319
Sequence Mass (Da): 34889
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A0A6A6VE78 | MAPRRIEQDEIEKYWEIFSTLANGSTHLDGAQAAPVLKNSQLRDDQLERVWDLADVDNDGKLDFEEFCVAMRLIFDLINGESSDVPASLPDWLIPESKAHLVQATRALSGSQPSFEPLSDDDDDTPGLRSGFDWYMSPSDTSKYEEIYTANRDNHGNVSFSTLEGLFQDLDNVPDSDIRFAWNLVNPKARESVGKDACLAFLHILNQRSEGFRVPRSVPPSLRASFEKAHIDYDVEGRSKAQATSKWAASRDEDTPTGRKSRFGDAYLTRLGVGDRANSYGARAKGTDFGHRTTEDWEEVRLKKQLRELEEKIERVEKET... | Function: Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma mem... |
Q0W0U1 | MEKVTLTPNGEKYLVLEAECITPDNFAGRTLEEIADMQVWEGNTTHRLGKFFDISGTTAATAEEQAIVINGSVPRVKYIGSKMAAGAILCKGDVDMYCGAWMKGGSILVKGNADAFAGIQMEGGDLVIEGNAGNYLGAAYRGDWRGMKGGNILVKGNAGCDIGEYMIGGTITVHGNVTINAGIHAGRAVGAKEPGGKIIIHGNAESRVGAQMTRGTIYVLGKIGNMMPGFALKSTEEVEFDGQKMLFNVYTGDRAEAGKGTLYVKS | Pathway: One-carbon metabolism; methanogenesis from CO(2); 5,10-methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 1/3.
EC: 1.2.7.12
Catalytic Activity: H2O + N-formylmethanofuran + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + H(+) + methanofuran + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Length: 266
Sequence Mass (... |
S6HG07 | MQESKVSRRLKETTAPEVNEYIYQPRLEGFAQGFVNLGNVNKAHIVMLAEQGLIRHEHAAVLAKGVLDMEAAGPDAVTLDPSREDAYFNYEAHLIEQIGTDIGGRLHTGRSRNDILATLDRLRCREVLLNLVDLLHQVRQTALSNARRYAEIVMPGYTHLQPAQPITYGYYLSAVEQALQRDTQRLTQTLDAMNQSPLGAAAFAGTPFAIDRTRTAELLGFDGYLDNALDAVGSRDFILESLSHLSLLSVFWSRVAQDYFVWSTHEFSLIEFPDSVAATSSIMPQKKNPTVLEYLKGRTGHIVGLLMGASITVKGSNFSH... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
Catalytic Activity: 2-(N(omega)-L-arginino)succinate = fumarate + L-arginine
EC: 4.3.2.1
Subcellular Location: Cytoplasm
Sequence Length: 500
Sequence Mass (Da): 54798
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A0A6A4MJ20 | MAQKQIWSGIPLFPVLVMFFISRLAETNRAPFDLPEAEAESVAGYNVEYARDAILNLIYNI | Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Cell membrane
Sequence Length: 61
Sequence Mass (Da): 6918
Location Topology: Multi-pass membrane protein
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A0A3G3CAE0 | GGFGNWLIPLMLGVPDMAFPRMNNLSFWLLIPSIILLILSMFFNEGVGTGWTLYPPLSDFTAHVNFSVDFTIFSLHLAGASSILGAVNFISTILNMHNMNLSMDKISLFSWAVLVTAILLLLSLPVLAGAITMLLTDRNFYTCFFNVSKGGDPILFQHLF | 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... |
A0A7W9E5J1 | MTSARTTFVGHATGTVGTDDLHRRSPAALVVKICGLVTPGELDLVASAGASLAGVWWGVPGSARSLDHAGLRRMRTAAAVERCLVTFSSDAQAIAEARDALQADWVQLHAFQSPAVVADVRRRLPMGTRLVKVLHIDGETLLERPFLGAFGRSGVDEYILDTVSGRQIGSTGTQSSPETVEKFAGQLTHPFLIAGGIDSDRAEEFGRVRALPGWHGIDVDTNARSADGALDIDRIASIVDAWGRSSPTRSLVTAGAPA | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 258
Sequence Mass (Da): 27202
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A0A4U0UZ99 | PSFRSSDLRSDDDLPLHLSPPESIPLSDTRPYDRRNIFNSDSTAHTIPTRWVAAVIRCLDSTWGGGEVLVRSTTFGIPQSPATSYRTYRLNGSTPPRSSPLPFTTTSLTIHLPGSPPQKGVTTYALAQNRQKPLAGVFDAAIFNTWRRFKGQVLYIAPPMIIAYSIMQWAIEKNEHYNSKQGRSEASE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
N4UB39 | MPFPKGLFYLVQLALFLGQGPSSGEAASLPTRADNSRTVAPANCIVVKPSGASASEFTSLQAAVNSIGSSTKPACIFLNSGTYNERVEIKVKAPLTLYGSTTDTGSYKKNTVIIQNTLGSQDAGSLDASSTVNLRSNDFAAYNIDFVNGYTAGQAVALTANGNKTGFYGCSFKSYQDTLYVKAGWMYYSNCYIEGAVDYIFGNGHAWIGEYHIYRHPRSDQQSLPRTSLESQRTSDVPVQHSDKCCETRGLLTYGRRRNTFENTGAGADTSQRKYFTASDKALTKQDLWGADFKWYDASY | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Function: Involved in maceration and soft-rotting of plant tissue.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
EC: 3.1.1.11
Subc... |
A0A6A4PU68 | MATRVIPPRILRNLRYNTATKPLNSTHPSSLTPTLSPPTCLDPKPPSSTVLRPAIDPSALNFHDVEKLFSYVPTYKLLRSTAVLHATGVEPMVDLGMWIMKSKFMEIEGVKDIILAAIRGTFYNHFCAGEDAITAGKSIGSLNDGGLRGMLVYGVEDAHDNDGCDRNLKGFMHTVNVSRSLPTSSVSIVSIFT | Function: Converts proline to delta-1-pyrroline-5-carboxylate.
EC: 1.5.5.2
Catalytic Activity: a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)
Sequence Length: 193
Sequence Mass (Da): 21016
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A0A177WI90 | MFSESYQWLTSPVCVTAVLIAIVLAAAWIKSFFKKQYNATHKSICIILGSGGHTMEMMEILKDIDCQHFSPRHYIIASTDQTSEGKVILHEQQIQSQTGKNQIYTISKISRSRQVNQPWISSIFSTLWAAWFSLMIFYRLYPDLILCNGPGTCVPIACIARLTQLLGISRARVMYVESLARVSDLSLSGKILYNIVDKFIIQWPQLKTKYPKSIYVGRLV | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 220
Sequence Mass (Da): 25032
Location Topology: Single-pass membrane protein
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A0A519LBM2 | DHTPVVSIGLRYGMLLFIASEVMFFAAFFWMFFEMSIFNEARAHIPEVGAWADTAKAWSTWPPKGIETLDAWQLPLLNTVILLLSGTTVTWAHHAIAQGDRNATKLGLGITIALGVLFTAVQAYEYHHIIHEHLFFNEEAINSGLYGSIFFMATGFHGFHVLIGTIFLIVCMLRLLAGQFTPEKHFGFEAAAWYWHFVDVVWLFLFAFVYVVFG | EC: 7.1.1.9
Subcellular Location: Cell membrane
Sequence Length: 214
Sequence Mass (Da): 24240
Location Topology: Multi-pass membrane protein
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E4XI34 | MPKTMLTLQGASLVFFAAFSSLYFQIPGLYGPNGLLPVDDLIPQSTQLDLSDFLANPNLFIFSKRLGFSVCEFMEILTLFGIFLSAAMALFKNIRGTFGFVFLFVAYLSLYRVGQTFMHFQWDIMLLEFGVLCIVMTLSPAQGISLCRWLLIRLLFHSGFKKLESGCPTWWGLTALDWHFESQCIPTPISYHAHHLPKIFLQIGVLVTYFSQLGIVLFALSPSRRLRIFSGWVSILHQLGILATGNYNFFNLLTILLALTCFDDLHLRAGNKNENKKEKDFLVIIFWLALEAIQFLLMTFAISKSIEFGSDGQFKLSDTA... | Function: Involved in the maturation of specific proteins in the endoplasmic reticulum.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 599
Sequence Mass (Da): 69367
Location Topology: Multi-pass membrane protein
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A0A5Q4BR02 | MTAKLETQPQAGILLDKAEPPDSSSNKGPLSGDITDNERAKEPAASGPVRTVAGLKWYIIVFAILSSTFLFALDNTVVADVQPQIVLQFDAIEDIAWLAVAFIMVSTAVNLLFGQLYSHLKPKWLYIGSVVVFEIGSALCGAAPNMDSLIVGRALCGLGGVGMYLGVMVLIAATTTIQERPMYLASIGLTWGLGTILGPLVGGAFADSDATWRWAFYINLPIGALAAPVYIFMLPSPDPQPGASILKRLAEVDWIGAVIMLGAIVTFTMAISFGGVMYEWDSGSEIALFVVAGVLFVVFDVQQAYSIGTTVERRIFPVEL... | EC: 3.4.-.-
Subcellular Location: Membrane
Sequence Length: 950
Sequence Mass (Da): 103246
Location Topology: Multi-pass membrane protein
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A0A6A4QIH7 | MTGSDGRLLAGGVVGALIAASPVQIVVGSFIANKKESSSNAIESSRASSSVPTSSQMLTFGGSVTPTIPTPQGPSSESSDENDHSSFTGPGLYSNVTQPINNNMQMHHHPLWPDYNTHQ | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular Location: Nucleus
Sequence Length: 119
Domain: The PPC domain mediates interactions between AHL proteins.
Sequence Mass (Da): 12396
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A0A380MY61 | MSGKELRLRQEYFLVSASAQDIVIHHKQRFGSMDTLPEKAAIHLNDTHPVLAIPELMRILLDEEKYDWDTAWEMCLKIFSYTNHTLISEALETWPVDMMERILPRHLDIIYAINEWFLEGLS | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate ... |
I0AYG5 | GTSLSMLIRAELGNPGSLIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLMSSMVEKGAGTGWTVYPPLSSGIAHSGASVDLAIFSLHLAGISSILGAVNFITTIINMRSVGMTFDRMPLFVWSVGITALLLLLSLPVLAVAITLNLTGAKSNNSFCTP | 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... |
E4X6K5 | MLGFIRAGRAGLSRAAGQKLANVRPVVSIRTQAAAVETKPYFSMEVVDGVAVVRMDQPGSSMNTISVAMQDEFAGVLDEIENNPNINSAVLISAKPGCFVAGADIQMINDVTTAAEGEALSKGGQDMFKRIENSKKKFVAAINGPALGGGLELAMACHYRVATTSKSTKLGLPEVMLGVLPGAGGTQRLVQLVGPAEAFPMLMTGATKVPKKAKSMGLVDQTVEPLGPGKISTVEYLEKVAVDYAKQLATGSIKRKQKKLKGPNKIAKTLISNGLTRDWFFQKNLVDNVMKKTKGVYPAPLTIAELLKESSQVGFGSDAA... | Pathway: Lipid metabolism; fatty acid beta-oxidation.
EC: 4.2.1.17
Catalytic Activity: (3S)-hydroxydecanoyl-CoA + NAD(+) = 3-oxodecanoyl-CoA + H(+) + NADH
Sequence Length: 764
Sequence Mass (Da): 82403
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A0A8B8N0L7 | MAQTLPLQTSNNANTAAPRAAAAAARKGKTVEETYQKKSQLEHILLRPDTYIGSVEKHTQALWVYDGDEMVHRPVTYVPGLYKIFDEILVNAADNKQRDPRMDSVKVTIDPERNLISVYNNGDGVPVEMHREENVYVPELIFGHLLTSSNYDDTVRKTTGGRNGYGAKLTNIFSTEFVIETADGKNGLKYKQVFSKNMGVKGAPDIKACKAGENWTKVSFKPDLAKFNMTQLEDDVVALMKKRVIDLAGCLGKTVKVELNGKRVPVKTFADYVGLCLKFASKNRPEGSLPRIEETVNERWEVCVSLSEGQFQQVSFVNGI... | Function: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
EC: 5.6.2.2
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Length: 475
Sequence Mass (Da): 52410
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A0A8H6QJ30 | MDQYLQMYRAALDSAVKYHLFRPKTPGDQDILFPGSLEARGNGQPALRTEVQHLACFVGGMVGLGARLNDSLEELAIAIKLTEGCVWAYQNTASGIMPKVFYIDDCPSDGSCEWTDEGHVEPGHEYGFTQILDTSYQLRPEAIESVFIMYRLTGNLIWQEKGWNMFQAIMKHTMTPIGNARIRDVTDAEPKQDDSMESFWLAETLKYFYLLFSEPDLVSLDNFVL | Pathway: Protein modification; protein glycosylation.
Function: Involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
Catalytic Activity: 3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[al... |
A0A8B8QYL9 | MRPAPESITPPAPRAALRLEPPQPSPATCGYSNCRWPVYPTSHDFEASAATILLVLLCGLICGLILNTAIRCFLRCDGGGRSPPPAPRRRHRQQEQEQELEPKLSNSELTVAPVVTYAPGVTKLAGTEAECSICLTEFVEGDGIRVLETCSHGFHMECIERWLSSNKSCPTCRSSLVVDRCGSTVSEGGDHCRENADQQTVSAGESSSGGAASI | 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: 214
Sequence Mass (Da): 22897
Location Topology: Single... |
A0A7G8JTP2 | MTPSSLLFFTTTTMGTLMALSSNNWLFLWMGMELNLLSFIPLIASTQSFQETEASVKYFIIQAIGSGLMLMAGVMSMLNSLGPSTKYITSFMFLLSMVMKLGMAPCHQWLPHIMSSMTWSMCLILSTWQKISPLMMLNTAVPFNIPTYLMLVATTSAIIGGIGGMNQSQFRPLLAYSSIGHMGWMLMAMQFSSAIFSLYFMTYLVITSSLMFMMFKMSAINSNFNTTLVHMSHFSFAMMMFMMFSLGGLPPFLGFIPKWMIINVMATKEMFLMLMLLITGSLLNLFYYFSMMFNFIMMKTPCRSVSISTTNLMLTFLSTL... | 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 ... |
A0A2A9NQT8 | MHHRLGRRHGIFIIISKIGCAIALWGCAMQAGASNVATLLIGRIVAGFAIGVLSMTVPLYNTEIAPPRVRGFLVGLTQQMLGIGFIVANWVGYGSQFIKSDVSWRLPLGLQLVPAGLLLVGIQFLPYSPRWLLEVGRDDEAREVVYKLHGAGRKVAAEKEYHEMYETIKAETLTRSRRLSDLWATRAMLRRTFVAVGVQVFCQFSGINVLNYFGPQLYESLGVTGGKALLVQGIYGAVGPIANFFFITLILDRVGRKKPLLFGAASFVVTYSILAAVVATNPPTAPGEIDTTNHAAQRFRHYFVSRLQG | Catalytic Activity: H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in)
Subcellular Location: Membrane
Sequence Length: 309
Sequence Mass (Da): 33893
Location Topology: Multi-pass membrane protein
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A0A6A4NI34 | MASIRKINCVWGIFFLSLIFVGESQVSKQFVQTRNTQFVFNGSTFVFIGFNSYWMMIVAASDKSQMPKVSNVFAQASAAGLKVCRTMAYYDGSNPLALQTSPGVYNEHVFQALDFVVSEARKYNVKLIMSLINNFKDLGGRFQYLQWAKDAGVQIMSDDDFYTNEVVRGYYKNHVKKVLTRVNTITKIAYQEDPTIMAWELINEPRSDFRNANLLHGWIEEMAPYVKSIDNKHLLSIGMEGFYGDDTPDRKQYNPGNYTVGTEFIKNHLVKEIDFTTIHAYPDNW | Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
EC: 3.2.1.78
Subcellular Location: Secreted
Sequence Length: 285
Sequence Mass (Da): 32702
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A0A519IUQ9 | MIATSLMTGLAAVLAATVPVPAVEAAIHTTKGDIVLELDAQAAPLTTCNFIRYVQAGRYRDATFFRTVVRATNANPNPIDVIQAATTAGSDDPGFGPIALERTRDTGLMHVAGTISMARDGPDTATSSFFIVTQDTPSLDFGGGRNPDGQGFAAFGKVTEGLELVRAIQALPATDEQITAPVAITNIELRGPVPAVCGAPSAQ | 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: 203
Sequence Mass (Da): 20980
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A0A850LY57 | MGIVKIQKLYESIKEKNFDILGGKGAHLAKLLDLKMPVPSGFVLPTTCFKLFLEKSDYYQRIQSILQNPINFENILEVSKQLQDSIMHSKFPEKFLIEVEKAWEELSKHTKIEYVAVRSSATVEDLETASFAGQAETFLCIDNLDHLYKSIKDCWASLYSPRALMYCLTNNILVDKVQMAVIVQKMVNSDIAGVMFTADVVNKDPSKILINITWGFGETIADGKVDADEILIDKDTLKILNIRIGKKELMSIRNVNACGTRIIETPHNKRDCCCITEEKIIEIAKIGLEIEKKFKYYQDIEFAIENNEIKILQSRPVTTM | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 320
Sequence Mass (Da): 36454
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G4W923 | MVSVIPWLAFLCPSSSGHSLLGKRAARRACALMTESSQPSPGEAAPPRGETGTCVVVAGTREESKNGKLKKALSDIIAPEDFEFVEVPCIAAQAGPDRERLVDTLAEEGRRVGAGEKPRFGYAAVTSPEGANVFLECLRSASLTKCPIPVTAVGKSTAEILAKAGVEPVFVPSKATAETLAAELPSVSSSSSTSSSSSSSSSSLSSSSCPGRVLYPTSNLSLGTLERLLKERGFEVTRLETYATVTAQWDEEKTQSAARTQIATFGSPSSVRNWVEKLSLREGGRELLSSQAAACIGETSGRAAEKMEVFREVVWPEKPG... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
E4XHA5 | MTEYSKKSGFAEVDQIFSGFLHALQNDDIESAVKIMNQSSGEVRRIFQPWLEESRNYLETLQAISVAKAILTSKVLSV | Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 78... |
E4WRE3 | MILSDGLSGAAVKLTLLGISLFAFYIRTFGVRKFEPVLNGSEGYRILRKLEILENGGDLDFDEQIWYPFGFLDDDKDLVLIRLVLAFRFITGVLWKTLTSHDACVYFGPFCGAVTPWISFFVVRSLVRETLPAICVSFYVAVLPGFAFSTVAGRLSSEALLPAIIFVFLPLD | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein] = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-asparaginy-[protein]
EC: 2.4.99.18
Subcellular Locati... |
A0A7C5SLE1 | MVKWLNYIIERVYESQRLQKILVVLLVGISVVLAVLIRVSSFWLNGFEFFEFDSYIEYWQAKYVYENGPLAWYTLTRNNPDTQLFWHPWGRDFIFTSYPFLPMWIGITYHIVKYTGLALHEWAALQPVLFASVAVIIAYFAGREISSSRVVGVLSSILLAVL | 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 Locat... |
A0A8H8S158 | MYLGNEADHILTASELEPWVQYALDELEFILGPSHSTHGALRTQLGHPEPWELKYVEIGNEDHLYDNGPQTYAAYRFSKFYEAISAAYPELILVSSTGDYTAVGGSNTSNPSATDFHTYQRPDYFVSQFGHFDNASREHKSFIGEYACIQGNDYSQLAVDWSAPKLPWVPWVGSVSEAIFSLGAERNGDAVIGMSYAPGFQNLNSYEWTPDLIAFTADPSQTIKSTSHHVIELLSNNRYNATVPVTTDSDFGPAYWVAGVSEPGHYTFKTAIYNSTSTVPFSISFEGVSEGVKGTLSVLNAPDGLSSNTLDNGVVSDVVK... | Pathway: Glycan metabolism; L-arabinan degradation.
EC: 3.2.1.55
Catalytic Activity: Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
Sequence Length: 376
Sequence Mass (Da): 41178
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A0A2S6MZI6 | MSPTLRRTATGRSEAERLAAFRKVFADALHQQQAGAIDEAIANWRRALKLNPGSAEAYCNLGAAWRQKRRPKEAVTCLRKAIELNPDHVEAHNNLGNALKDLGRIEEAVACHRRAVALRPDCLEAHAGLADTLEAQGSWEAAVAAYQDLLRLRPGHVEACIRLGICLQTLGRSDEAIDCLCAAIEQRPESPEALFFLGCALQARDRLAEAVACYRAAAGLQPDLAEAYGNQAEALRLQGLVDEALACAHKAVALRPGHAGFLNGRGIALQAVGRWQDAAASYREAIRADARFYQAHVNLGLVLHQMQRLDDAVAAYDIAL... | Catalytic Activity: L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP
Subcellular Location: Membrane
Sequence Length: 642
Sequence Mass (Da): 70507
Location Topology: Peripheral membrane protein
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A0A0V0PWQ0 | MILSYGALWLIPVLALPLTLAVAAHLPAMRPHSLSLLPLAPLPALATALFAPEGSAFEAPDLLLGAQLALEGNARLFLGFAAFLWTAAGIFARTYMRGDERAGGFAALWCLTLAGNFGVFLAADVATFYVSFACVSLAAYPLVVHTRSAKAMRAGLVYIVLALAGETALLLGFMLAASSAETLLIADMRESMVDSPWQGAVLTLLVAGFGIKAGLVPLHVWLPLAHPAAPTPASAVLSGAIVKAGIFGLIQFLPFGVDLRFWHEALLWAGLATAFYGVAIGLTQQNPKTVLAYSTVSQMGLVVAVLATALQQGSPEIALA... | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ... |
D5JRM6 | TSLSLLIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDXAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRLNNLSFDQMPLFIWAVGITAFLLLLSLPVLAGAITMLLTDRNLN | 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... |
F8KXY2 | METAFTFSLLPGGIGQLVFNLPHEKVNVLSPPVLEELENLIEQLDPSSGVKLLLITSGKEHQFVAGVDLKKLEPVFQDPSQGEKILALGHRAYKKLSELPFPTIAAIDGACLGGGLELALACKYRIVSDHPKTALGLPETQLGIMPGWGGTQRLPRLIGLSSALGMILNGKTVNGVKAYKMKLADSVAAWEFFPEKSLEFARNILKPEFAQKVLNRRKQSGIQNFLLEKNPAGRALIFYQAKKQVLDKTHGFYPAPLVALETIKQTYTLPLNEGLEIEQKNFVENIPTKFMNAKNLVKVFFQNESLKKDAGISIQATPRP... | Pathway: Lipid metabolism; fatty acid beta-oxidation.
EC: 1.1.1.35
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH
Sequence Length: 715
Sequence Mass (Da): 79646
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A0A8S1GP57 | MQAAVLGLVGGVATAYSIYHHGHKSTLFSRYCVVLSVFHLSEYVFTALSNRRSLQPDSFLLNHSYGYWGAAALSWAEFSLEYYALPMLKNVNVSMIGVLFCLVGEVIRKAAMLQAGNGFTHRLAMAKRPDHKLITDGIYGFCRHPGYTGWLIWSVSTQLVLCNPFCCVIYAFNET | Catalytic Activity: [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S-adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.100
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 175
Sequence Mass (Da): 19543
Location To... |
A0A836G0L2 | MSVITLNEFFSWAVSTVMTRQNLVPSPDGSRMIHALIPMWDMCNHENGRITTDFNATSDRCECYALRDFKKGQQVFISYGPRTNSDFFVHSGFVCMDNEQDGFKLRLGISKADSLQKERIELLSKLDLPSVGEFLLKPGTEPISDTLLAFLRVFSMRKAELTHWLRSDKVFDLKHVDCALETVVEENVRKFLLTRLQLLIANYPTTLKEDLELLETTLPQMKKMAVQLRVTEKRILSGALEYVEQWIKA | Catalytic Activity: L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) + N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine
EC: 2.1.1.85
Subcellular Location: Cytoplasm
Sequence Length: 249
Sequence Mass (Da): 28643
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A0A1S6IND4 | MLKGKTHRIVGISLFGALAYILMLFAFPVIPAFSYLKVDFSDVSLLISFLIYGPVGGFMSTLIRTILHYIQTGGDMGYPIGDMASLLASVSYCLPVYLIVKRAKTKTGLITALFVGTLTMTIVLTIANWFIITPLYLYILNFSVGNLRDYIVIGVVPFNIIKGLIISAAILIILPKLKPWLVKQYKFMAIK | Function: Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Subcellular Location: Cell membrane
Sequence Length: 191
Sequence Mass (Da): 21163
Location Topology: Multi-pass membrane protein
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A0A3R9W6J5 | MPNLSLLPGPAHRHWAWQAEALCQEVGAEQFYGPWHERRKDREQRDAQAKRLCSACPVREVCLRHALSTQEPYGVWGGLTARERRKLRTGYRPAGAPQGETGPATSEAAGR | 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... |
A0A194PHE5 | MSVVLLNKDFATSNDPDLKVYLTLKWKLITTWFNILTIPYIPICVYVDWRELKRKADRPVPPNLEKLKNIRDFYFTNLILPATLYADVLFWNLWNTDRKLLMPLSVDKYVSVWEQHSMHTASLVFVIFDLVLVPRQRPKTYKWGVILLSIYLTSYIFVCLTSLLKGEYVYPGLKSFTTFKFVVLTIHMFIGHMFYYTGQWIVIDLLWGQSKSVKKIA | Catalytic Activity: 12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H(+)
Subcellular Location: Membrane
Sequence Length: 217
Sequence Mass (Da): 25648
Location Topology: Multi-pass membrane protein
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A0A427YU14 | MVSRHDTPDAQTIADHILLLPEPRALPHLNQSTPASLYHLSTLLQPHSAPSNVTPCPPTPASIAPTAADIKRKNANFAARAQAGKRTNRPARSQQRRSVGTWVLIAMGFLLVGGSE | Function: May interact with target proteins during translocation into the lumen of the endoplasmic reticulum. May protect unfolded target proteins against degradation and facilitate correct glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 116
Sequence Mass (Da): 12446
Location Topolo... |
E4YJZ0 | MDREIPDTRLGTCNSVVWPREGLPTTSVIITFHNELRSTLLRTIISVIRRTPSNILKEIVLVDDASIKLILNRKREGLIRARIRAAMIATGDTFTFLDSHVEVNQDWIQPLMQRIKENPRMVVAPIIDVINKDNFQYIGADAFLTGGVSWAMVFRWDWLSRHEMETMDHTVGLKSPTIAGGLFSVGKAWFHELGEYDDQMDIWGGENIEFSFRVWQCGGEMEIMPCSRVGHVFRDDHPYDFGKKGSNHVFVKNNNRFVHTWMDEYSTFYYGTRPNARSILPGDLSVRRHFKEKLQCKGFDWYVKNVYPRQHMPERNSIAW... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 468
Sequence Mass (Da): 53914
Location Topology: Single-pass type II membrane protein
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E4WX63 | MRTRRLIKIPLGGYILCALIVLNVYQFNENQRLAQESSKNDEKNVTKILFYTAVRDFGIHRGRHYKMFRRQFRNLYESKTNSSNYYAEIFLDNFGYPGNLVEWDDEFTDTIYTSNIPESFAVEATRNVGNHSLHVFMSNHQFDITKELIEKLKNLQLENDEIACLFKKNDAMLPKPLNSSIINQCQGDFFAVNTKTALKIQDQLVVQKTIPHKTGEPWEQLYEYTQKLIKSDYDAHLLQNDTELIRGKARKYDDLIIGDFVDTYENLPLKTFLGFQFFAGFCYGNKKIINFHDSDAFVLLPDVIKDYQLNQDISDADYRQ... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 509
Sequence Mass (Da): 59464
Location Topology: Single-pass type II membrane protein
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E4XHR7 | MPVAGIPNFVMEKKDPKVANGKEEFADYAEINSETEFEKEFDKSEKEEEITEFKEDDDLVENKKESKMPERVRFIKTKVEEDNVDEPYNIEGYKIPENHNTTIFDNVFKSEKYLTEGREYNYYHLWHFQSTINDAKDEEIEEDYDDFLEELSFYSNDSTTKNITLRTQKKEQAMIKDIFDVDVEVDDYAGYEFEPDHEIRREKEILKAEVENKIKRLKEQKQAEIDARIAQEEKLQKIREDQLRREKVLKDREEREKKREEFLRKKEEAAEVIALHRKLAAQKRLKDKMRAEDYEEEDELLKEEYETMQQVAERGQKKEN... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 827
Sequence Mass (Da): 96754
Location Topology: Single-pass type II membrane protein
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A0A519KRI9 | EAEADRLAPHKTFPGDRPSSTLLLDALTPESVGALLALYEHKTFVEGVIWDINSFDQWGVELGKVLAKAILKDVEAGEPSAGLDPSTAELMKRLMV | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 96
Sequence Mass (Da): 10389
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A0A8B8Q3G0 | MTPVQAATIPLMLKSKDVIVEAKTGSGKTLAFLIPVIQCLIKKDLESEIGTHDVMAIILSPTRELATQIHQELRKLLSSAILKGDRKISSQLIVGGSSVINDIQKYTKYGANIVVATPGRLSIILEMTDNKLSVSIRKKLNFLIFDEADHLLSFGFERNLSSILNYLPKQRRTSLFSATQTTEVEELIKSGLRNPIRVNVNKLTQDDYSDDMKSLRMPDKLMNFYHVCSSYSNKLAVLAELIKSNEYNKGSRIASALSRVPRSDSLKSNQGVIYVAASRTMATSEAGSGAGKGGGAGGSIREAGGSLGKKGAAQEEQYFS... | Function: RNA helicase.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.13
Subcellular Location: Mitochondrion
Sequence Length: 355
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): 38988
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Q8MGM9 | DILAAFRMTPQPGVPAEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDIEPVAGEENQYIAYVAYPLDLFEEGSVTNLFTSIVGNVFGFKALRALRLEDLRIPPAYSKTFIGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKXDENVNSQPFMRWRDXXLFVAEALFKSQAETGEIKGHYLNATAGTCXXMMKRAVFARELGVPIVMHDYLTGGFTANTSLAYYCRDNGLLLHIHRAMHAVIDRQRNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERDVTLGFVDLLRDDYI... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in... |
A0A7C8NVM5 | MQLTSTILLLSASLASAHYIFPALILNGQATGDWQYVKKAATLTAVDPLKTSTPTPCDATMIQKPPKQQLPMLRLAIWSDSLSQTAADFDGEGTVWFKVHEDQPANTSIGIWWPEDITEVYVKVPRCLPDGEYLLRVEHIALHNAYQTGGAQFFLGCAQLNVTGGWVGATPSTPPTLVSFPGAYNATDPGIKLNIWAPDAISYVNPGPPVYHCYL | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secre... |
E4X1Q7 | MALETAKRPAFEKPSRKASQVWKTLSDSLRPKTKSTDDIILQLQKCFLKELGPDQAQKLLKSADCSLFEEKAEFDDFGYKRILIEENEKFNLVLMCWPEGSATSIHDHTGSECIMKCLAGKIRETRYKWPVKKRQSLEKICEEDLKKNEVSGINDEEGLHLIENPSTAERAISLHLYYPPLSECLVFDEYTGKARRIRLKLS | Cofactor: Binds 1 Fe cation per subunit.
Pathway: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.
Function: Catalyzes the oxidation of cysteine to cysteine sulfinic acid with addition of molecular dioxygen.
EC: 1.13.11.20
Catalytic Activity: L-cysteine + O2 = 3-sulfino-L-alanine ... |
A0A8S1HX18 | MKTWFLAVILSAVLHRSDGYNYLVWSPLFARSHNNFLSTIAEIVAQAGHNVTFLAPIIDESMRDDPEKLLQYTRDVLKPEASQQVSRMNEALLQGDYTSLWVEKSDVFTFAKMCAAHLTIFAHSCESVVVDKKLMETLKKKNFDVILTEAISECPFAVRDILKIPTLVLTDSFPEYDTVANLIGEPILPSYVPGFFSTQRDKMNVLQRGINALETWFGEQMVQDPNVPKMVKEKLNIEVRLSREVIPEAAFVLSNSNPFLNFPRPTLHKTVQIGGATINLTELRSEKLSKEWEEVVSRRSKNVLVSFGTMVFSSAMPNDM... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 533
Sequence Mass (Da): 60778
Location Topology: Single-pass membrane protein
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A0A8B8QA81 | MLLFLSQHTNREGFLGFFLFGGGDMDLVTKASLIHVSETIPPSASEAATTLAHTPLHNSGTGFPIMAIAIIGILATAFLLLGYYVFVIKCCLNWHRIDLLSRFSLSRRGGRRPEDTLLMYSPAMMEPRGLDDAVIRSIPILQFRSRGGKSRDFGERSFCECAVCLNEFQEDEKLKIIPYCSHVFHIDCIDIWLQNNANCPLCRTSVSSAVAAGLLLPPPRFPPDHIIAPSSTPEETSPYDNGATVGRDEDFVVIELGRPEDAGPEGQSQSQRLRIGRERMQSGGSSSSSLTQAISPSLGKLEKSGLAKKGRARKLHKMTS... | Pathway: Protein modification; protein ubiquitination.
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: ... |
E4WSV1 | MSKHNSKRKLHKQKLLVLLSSFFPAYIIFSVFKLHCYTGTENFGCPKYGIPEKFLKLWNHEKKNSLQKFTCPVSGSDVILVTTTRDKTDLHEKIYQLYTKNGFQFVALCFLQNSNVIFLDDDTFFNPFEKILPAPITCGHARFNAETTWKKPFGKYHLSDDIWPDDYRYPTYCGGPCTIVTSSAAEKIYNVASEIELTDFNMEDVLFTGVYRTFVDIQEPAENRKLCHHFAGDYTALLRKFESYIN | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 246
Sequence Mass (Da): 28544
Location Topology: Single-pass type II membrane protein
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D3R240 | MKTRIITGSIFALIMAGFLLPGYKFPALPLLLFFLVNIFGGREVYRVVIAKFNLSLRGLSLLWSVIFLTALIPCGGNTLIDRSLAQLGIFAICALTLLFFSTIILACIHGTSALTPAVAVNSAGLYTAFPCAVAVVLLTAVPDGFYWLLIAVFSPWVSDVSAYFTGFYLGKRKLIPQISPKKTVAGFIGGLVGTMIVMAVAYKFMVAALYGSGSDSPYYTIIIGSFIGAILSIASQFGDWLASVIKRETGVKDFGTLLPGHGGIMDRFDSVMFTLPATLLIVLLLAAIK | Pathway: Lipid metabolism.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 289
Sequence Mass (Da): 30932
Location Topology: Multi-pass membrane protein
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G4QMD8 | MTKGDLSKTGRNVRRNTANSSSLVHRSNRTESSDELDSLDDEIDLFDENERTGETGSSNKIVGLIVFTFVIVSFIYGGIQVKQWLEDEQQLPVQKVIFSGERRILVDAEMEALIRQNQKGSFFALDVNKVHQLLEDMPWVYRASVRKRWPSSLHIYLVEQQPVAIWNEDLLLNTEGDIFDGGDPNKKLPQLFGPGGSEKTALAGFNAMQSLLGSTGLTINALFLSERFAWRVELSNGIRLNIGRQQFIDRLQNFIDIFPLLQAQNKAINYIDLRYDIGLAVGWQKNDKKEQEITENND | 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: 298
Se... |
E4YYA1 | MVYCMGGPGIVFSKITLQKLSPKLGECLKNNLMTEHEDIELGRCVYHHANVGCTKSYEMAALFKNNYNVEETDSEGLKPLFEEVAAHSATYHANKIQANQYALHNTVMLKKIQKLRQSASDLEKDVDRMRKEIFDNSPFKDRKFYKLPRDKSVVWQQITQGRHYSTDFISRGILQPWVNVVTELAREAAKTYYKENKLHGKIERIHVDRVYQTTSGSASEYLTMIDMKHIINGEESTVTAAFRAKRSFLSLMMQEPQKMQLELINSAIVEKKDYNQKANPTAINFIIPLSGRSDSVRIFLDRLKVAALSHEIHINVKVVY... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 544
Sequence Mass (Da): 62476
Location Topology: Single-pass type II membrane protein
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A0A2A9NI24 | MPIAGSIPIGPTHGPLFFRTFADLDAWAADQKNKLEGVLPFIPRNEPSDSSAGNKGKILVCHDYKGGYVESPFSFSYTFNFWSACDTFIYFSHQRVTVPPPGWVNAAHRQGVKMLGVLIFENSDGQDDLLRLFTGPVPPTFTEGEPPSKIIARSAKANITTSQFPFSSHYARVLADLAYQRGFDGYLMNFEWFLFGGAVQARALAAWVSLLREELWKKVGPHAEVVWYDSVTIDGNLSWQDRLNAQNLPYFLSSTGFFSNYTWPTSYPNLMAQYFHSINPTLLTSTIPAPVLPTPSSLHSLTQQDVFVGVDVWGRGTYGG... | 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... |
A0A5Q4BBZ8 | MHLPFQFGGFSDFYCSLEHVQNFYAPSVYNSRVSSVVPSPQPIRRPRGVYYDGDGNPTYSPSREVDHELEIGFFVSQPVKHREELTIKHVEEHIFGFVLLNDWSSRDLQIFEMKPLGPFHSKGS | Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 6/6.
EC: 3.7.1.2
Catalytic Activity: 4-fumarylacetoacetate + H2O = acetoacetate + fumarate + H(+)
Sequence Length: 124
Sequence Mass (Da): 14319
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A0A7W8DF85 | MLAGLALAAAILLLGLGLLARWEFDDRAALQARAAQLLDAVTQEAHILLDRLHEQRLWDCSPASQRAIRRLLFGAHFFREVGSFDADGLLLCTSTDDVLGQPRAGTSRIHYAHSGLGYSTGVSLILGQDQPRSVTATVLRRDRFNLVLAPQAEAALRHGAATLIALDTEDGLQPLFPAAADATAAVRRLPVPASTDVVRETHWWRGQFALQQRAGMGDFVLFTRWHLGDVLRQQSTLAVAIVLIATLAGLVAHGTVTTWLTRLNSIDHRVRKLIGGDRIVCVYQPIVALASGRAVGCEVLMRLQDGDRLLYPEQVIPAVL... | Catalytic Activity: 3',3'-c-di-GMP + H2O = 5'-phosphoguanylyl(3'->5')guanosine + H(+)
EC: 3.1.4.52
Subcellular Location: Membrane
Sequence Length: 519
Sequence Mass (Da): 56619
Location Topology: Multi-pass membrane protein
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A0A7H0MKA7 | MGPVMLDVEGYELDAEEREILAHPLVGGVILFTRNYHDPEQLRELVRQIRAASRHRLVVAVDQEGGRVQRFRDGFTRLPAAQSFAALLGMEEGARLAQEAGWLMASEMIAMDIDISFAPVLDVGHISAAIGERSYHEDVQKALTLATRVIDGMHSAGMKSTGKHFPGHGAVTADSHKETPFDPRPLEEIRAKDMSIFKTLIEQNKLDAIMPAHVIYTDADPRPASGSPWWLKTVLRGELGYDGVIFSDDLSMEGAAIMGSYAERGQASLDAGCDMILVCNNRKGAVEVLDNLSPIKAERVTRLYHKGSFSRQELMSSARW... | Pathway: Cell wall biogenesis; peptidoglycan recycling.
Function: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked pe... |
X8HU22 | MDSIELLKSALFGLVEGITEWLPVSSTGHMLLLNEFVRLGSSTDFWDMFLVVIQLGAILAVCVMFFGELNPLSRRKEPAARRSTWALWAKIVVACLPAAAIGIPLDNWMEEHLGSPFVVAAALIAYGVLFILIETRREHKAELASSMGEGSPSVRGKHFAAPSPEGDGSHAKASPADRDARIQDTEDIDWPTAIGIGCFQVLSMVPGTSRSGSTIIGGLLLGCSRTVAAEFTFYLAIPVMFGASALRLAKYFLKGNVFTMEEAAVLLVGCAVAFLVSLLVIRFLMGYIRRHDFKPFGWYRIALGIATIAYFGLRLVA | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Cell membrane
Sequence Length: 317
Sequence... |
A0A427YMM2 | MQRSLPGHGTTSSSSSSAHSALSAVRRTFRPSPSSSPNRADVDIADEDQELELADLADPRPWETRAPLKHYGSHHSVHSADHGHLPLYKDSHGNAHGHGDSAGIGMETRQRRAQAQVQYGEKEGDVTVSETDVLDDQGKWQKGHLAGPGVGGRRGLPPKQRIPGWKGLLMEHEEWVWTGVYTLLSMITRYWRIGAANYVVWDEAHFGKFGSHYINRDFYFDVHPPLGKMLVGLAGLLSGYGGGFEFKSGVEYPEDVPYTAMRVFLASFGVMLVPIAWWTAGELGWSRWTRHWVTICVLCDIGWLCISRFILLDSMLLFFT... | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Locatio... |
A0A836FYR9 | MAIAPTPVSALVHSSTLVSAEVYLMIRFNRFLMETNVRIILGFFSITIFILGIMANFENDLKIIIALSTLSQLGLIIIILSFGFRLIALVHAIFKSILFMAAGSVIHSMKNTQDIRLLGNLNEIIPYVIIRLLISNIALSGVPFISGFYRKDIIIEIIYKE | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
G8NZL7 | MQFCRSTMEILLATIRPRRSAASEPDAQLLQRYIQRSSRYVPCEQREFSSEAALFAHLDRPARRTTPYLILTDSRGKQMSSEEFASTLGGVQDSGVQQVVMAIGPADGWSPEALRRASLTVAFGRITLPHELAAVVASEQIYRALTIRAGHPYHHGH | Function: Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
Catalytic Activity: pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.177
Subcellular Location: Cytoplasm
Sequence Length: 157
S... |
A0A1W6B885 | MLFNSLSFILLFLPITAVAYNLIRRFSVSGSKLFMIAASAYFYVYTTYTGAPVLAASCLVSYASYRAIIMSPRRRKLAMIIGVTANVILLCVLKYNHFVPIGAAYATDWLRTYGMPLAVSFFTFQQISFLVDAYKGKIERVALFDYLYYVLFFPKMIAGPITRWQSLMPQTNSREMIRSSMVLAGLTVIAIGLFKKVVLSGLFARYADVGYANTAALSFAEAWVTSLSYTAQIYFDFSGYSDIAIGSALLLGIRLPDNFNSPYKAVNIRDFWSRWHISLSTWLRDYVYIPLGGSRKGMPRTMANLLITFLISGAWHGSEL... | Pathway: Glycan biosynthesis; alginate biosynthesis.
EC: 2.3.1.-
Subcellular Location: Cell inner membrane
Sequence Length: 476
Sequence Mass (Da): 53398
Location Topology: Multi-pass membrane protein
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A0A836FUM7 | GMCSYCLVIYYHNYISYNSGMVTVLCNRIGDVGILILGLILLIMLETITKGLKFSFLYILVHTIFKSMLFMASGSVIHSMKNTQYIQLLRNLNEVIPYVIIKLLISSIALRDVPFISGFYRKGIIIEIIYRVNMFILIIISLLLSYSVQLFYYLFFNKRLKFYRYINIKEYILINVPIIIMICKNYRAVGFFILIII | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
A0A519KPT8 | MKKPNTPQLSLRVPEPSGRPGDAPDFSHLRFDPAGAVSRPEVSSTPYEMRDHAFQLVRVLDDDGQAVGPWNPKLDPETLRKGLKAMILTRAFDDRMHRAHRQGKTSFYMKCTGEEAIAVAQGMILGREDMGFPTYRQQGLLIARGYPLVEMMNQIYSNAADPIKGRQLPIMYSSKE | 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... |
A0A8B8P128 | MAFPPRKLLSSPDPCLFHHPPHANCPSPPTPPPPPPPPAGKSLLQDTKRILPYALGSVLLTGILCIILVKYYVKQNSSRRRRDAPILFHTQEEFLDEDQGPPQDHPVWFIRTIGLDQSVIDSITAFEYKKGEGLTEGTECSVCLGEFEDGENLRLLPKCSHSFHAPCIDTWLRSHKNCPLCRAPIVRDARIGHISVDVEEPRLNNLGSREENLMIENHGNSENTRARVESSESVGQDDGVSPSHMDDGIICDDVNKVPSFCSGESCEVLIPSDWDSEGHKRVTDTETAPARRSLSADMTISPAEGILKTRPKQTKRSSSI... | Pathway: Protein modification; protein ubiquitination.
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: ... |
B1AEQ2 | MTPQPGVPAEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDIEPVAGEENQYIAYVAYPLDLFEEGSVTNLFTSIVGNVFGFKALRALRLEDLRIPPAYSKTFIGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFVSEALFKAQAETGEIKGHYLNATAGTCEEMMKRAAFAYELGVPIVMHDYLTGGFTANTSLAFYCRDHGLLLHIHRAMHAVIDRQRNHGIHFRVLSKALFMSAETTTSPPL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in... |
A0A8H5SBI9 | MDYYTITLIIVIIPLIFASYWHHRHVTLKVVRASAAEASRFDMIDDEIHDISHDSMGERYYNFRNKFLWVYGLAMTAEWLQASYLYSCLKNTHKLSEPTIATLFVTGFVSAGISALFVDSLADKHGKKFMCQCYCVVYSVSCVAMLGGNILLLFAARLMAGFCTTLLHSVFENWMTAEYARQGFGARGTALSTIYSMMAVTHGFVAVGSGIVAQAAVDALGSHTAPFLLSIVCLSLALMVITRSWAENRGTPGRSPIAETSWRASAVSILKDSNLVILTLAMCFFEGSVHFVFYSWPQTIMSARAHERIWANPPFGTIFS... | Function: Mediates high-affinity intracellular uptake of the rare oligo-element molybdenum.
Subcellular Location: Cell membrane
Sequence Length: 389
Sequence Mass (Da): 43061
Location Topology: Multi-pass membrane protein
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A0A427YIE8 | MAQPIEQWITDIPPVTRAWVAAAVGTSLLVECQVVAPLQLYFSWKAAVGNMQLWRFLTTFFYFGPLSLDLAFHLFFIMRYSRLLEENSFSNRKADYFWLLFLCASFLLLISPLLTLPFLSSSLAFALVYIWSRRNPSIKMSLFGVITITAPYLPLCLVAFSWLLQGGFQAALGDIVGILAGHTYVFLQDYWPREMWSTTGKPEVQTPAVVKRVFGQDPDR | Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 220
Sequence Mass (Da): 25065
Location Topology: Multi-pass membrane protein
|
A0A427YGD9 | MIESKDLHEGFEQPGSALEIAFMEMIQADLWGNATDLSLLVDLKYEDLQKLQAVGAKAQAEQAKMILRNDLPKVWDCLKRMKDGRVDIVLDNAGFELYTDLIFADFLISSTPFVSEVVFHPKNIPWFVSDVLPYDFTWAIDSLADTTFFKSHSKVPLTDDDVAHLGSLAKRWRGHLDSGRFRLSVPLDTPLGGDTPLGSFWTTQYAYQDMPAAAPHLVDELAKSGLVVFKGDLNYRKRVLIGDAKWPTTTSFEKALGPLAGKITLVSLRTNKADTIAGLPEGVEAELDTKAPDWRVSGKYAVVSFSPKRE | Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate. Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function... |
R5AAL7 | MRYGLIGEKLGHSFSKIIHEQLADYTYDLIPLTRDELDAFLREKQFSALNVTIPYKETVIPYLDEVDSRAQKIGAVNTVVNRNGRLCGYNTDFYGFRYLLRKNGIDVAGKKALVLGKGGASKAVIAVLEELGASEIITVYYKEYPETVTYAECYKNHADAKIIVNTTPVGMYPNSDDCPIDLDRFTALEGVADVVYNPLRTQLVLEAEKRGIRAAGGLEMLVAQAKYAVEIFLDTHLEDARIAEINMPLLKERSNLVLVGMSGGGKSTIGKRAAEKLGKGFVDTDELIIERIKMPIAEFFAKEGEPAFREIETKVIHEVS... | 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... |
A0A8S1H5D9 | MGISGLLPFVKNACRQGNIRELRGRSVALDVSCMLHRALFGCMDQIHMGTNTDSYLGYVKRYVDILLELDCHVIMVFDGRPLPAKKDINDGRKIRREENVRKGEILLARGQVKEAREKFRMATKISREVVEKTIECFRKVKNVDIVVAPYEADAQLAYLMMSKLADAVVTEDSDLIVFGCDQIYFKWQHNNGECMVYQKSELSKCFSGEMGGNKFDFLKFRRICILAGCDYLQSGLQGVGLATALKFFSKTSSSDLKRILPKVPLYLNMPKLRGKITPQFVEDFIRAENTFMHQVVFDPRERCQKPLTPYKTSPDSSQNV... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: 5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Function... |
A0A128A0J9 | MIQDAKLFSVRKFDFHLRHLLVIGILIVSFSISAMVRSQAADYGFQLNEFDPFFNFRATQYLLDHGLNAYVHWHDDMSWYPTGRDVFATAQVPLHVTDAVLYKIFGGGMSLYDFTIIFPVVFGSMTAIVIFALVRVLGGTSAGLFASLFFALSPPIIVRGTIGWFKSEPLGLFYGLLGVYLFLSGLKSENKKIAIAKLIGGGFFLATGFASWGGIEFFLLPLGMFFVALPFIRKDHKFLLWAVPLFVAVTMIVAGGLFARPGPAFVFGVRGFALIGPAILLVVIVFIQKYSKEQHRLRNSLLVLAALIIIGGLVLSSGAF... | 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 Locat... |
E4XSA8 | MAREKNEMTQALLPKEKTSHEEEDPYISCSFRNTVLFAIVMLGGLLYLQAMSTSECSLSISLVAPAFGYESQEVAETPEPEIPEPEEPAQDFCAPKGLVGPLAIDFDMDKLEERFQELSESNKDFFENGEHTPENCQVQKLKNIAIIIPFRDMTKDLFRTKQFLYFLYYMIPILHRQNNHFSVYLVNQVHDDSPFNRAKLLNIGFEIAKKDGFDCFFFHDVDLVPENDQNIYECFDNPRHYSGFIDKFNYNLPYNSIFGGITAYSAEAFDKINGYSNEYWGWGGEDDDLERRTIAGAKYKLLRPEAGKSHYKMIKHGHET... | Pathway: Protein modification; protein glycosylation.
Function: Catalyses the transfer of galactose onto proteins or lipids.
EC: 2.4.1.-
Subcellular Location: Membrane
Sequence Length: 381
Sequence Mass (Da): 44051
Location Topology: Single-pass type II membrane protein
|
E4XEG7 | MARISRKNILNFIFGISIGFFISKALLNGRRCCCLSRIDKTLKKISAVKMLKNSIIFHFSFFEISKPRAQRIRQPEIKQPETEVSTTATSASTTTDEKPPVIDIEPLKRLPDPSKQCPYESDDLEGENHRPAAFLPTWREVHALSNSLGIVDGCYQPSDCTPVEKVAIIIPYKDREDHLLKWLWHMHQMLVRQRRSYCVFVSEPMGAGHFNKGSTMNAAAKEAINRGFDCIVLHDVDMLLEDDRNIYQCQDGPVHLSPFIDKFHYKDHYGTEFGGVTMLKKEHYLAANGYSNLFWGWGREDDDMVYRVKFAGLQIRKPVN... | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 628
Sequence Mass (Da): 71568
Location Topology: Single-pass type II membrane protein
|
A0A7C8LAG8 | MVYTTQFLALAAAMLPSAVLAQNNQTYANYSSQSQPDLYPQTMAALNFSFPDCVSGPLKDNIVCDTSANYVDRAEGLIALFTLEELINNTQNSGPGVPRLGLPPYEVWSEGLHGLDRAHFVKSGDEWTWATSFPMPILSMAALNRTLINQIASIIATQARAFNNVGRYGLDAYAPNINGFRSPLWGRGQETPGEDANFLTSSYAYEYITGLQGGIDPDNLKIAATAKHFAGYDLENWGGNSRLGFDARITQQDLAEYYTPQFLAASRYAKARSFIPC | Pathway: Glycan degradation; xylan degradation.
EC: 3.2.1.37
Catalytic Activity: Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.
Sequence Length: 277
Sequence Mass (Da): 30366
|
E4Y1S1 | MQFTVDFFHRLLENTKPGVAYYPIIFSQFDNKHVGDEADNFKIAEMRGFWREYGYGMVSLFKEDFDKAGGFDVKIIGWGMEDVYLASNVVRKRF | EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 94
Sequence Mass (Da): 11049
Location Topology: Single-pass type II membrane protein
|
A0A1I6GSJ2 | MAHLLQQFVQRVPGLEAQLNQMNQREKLLVSVAAVLFVITLAYFIAWKPLADGIAEREAKIDAQQELLQWVRENTGRYLAQTGGVQSKDSTPTSSMSGSMSERVTRLASAAKIEVTRMQPQSDSLVVVIDQVPFNTLLQLIENLETQAGLVIEHLDATEGGEPGIVRVRRLQVAE | 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: 175
Sequence Mass (Da): 19351
Location Topology: Single-pass membrane protei... |
A0A194PMN8 | DGTITENDIESSSLFTAASSKSSQNSPKGFYLKFEIDVVFLLLLGLALWTRTYNLEEPRYIVFDELHYGRYVSLYTKGIFFFDAHPPLGKQLLYLAGRLGGYNGNFTFDRIGSPYTESVPIKALRMVPAISGSLLVGITYQLMLEISTYQWTAILAALLVLFGVFYAHLAMLPKAGPHDSVMTSAFQASLQGGLASITRGQPLHVSHGSQITLRHSHGRTCWLHSHAHVYPVRYTDGRGSSHQQQVTCYSFKDVNNWWIVKRPDQASLAVTNPPDAIRHGDVVQLLHGITSRALNSHDVAAPEVSCYIDYNVSMSAQNLW... | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Locatio... |
A0A5E7ZQE4 | MIPEVNDTILAQLQNLETALAHEARVYNDRIEQVHAANKASALNLIHYLTLRKADLRPLQDKLHYLGLSSLSNSESHTLHQVRSVIQWLNHQPYLGHPDDIDPMTARAIAQRQSMHLFGQRPSNEIPFIMVTLDARMAGDVGLVTQFLEQGMDVARINCAHDDEATWEQLVSTLKQAMAEVGKSCRIYMDLAGPKLRTGIPGKGKDKKRLKIAEGQTLKLVEPEYEAGEKERVVSCSVRGIIAQLKPGQKVLFDDGLISTTVVKVKGNQAHFAIDRVSGTKPHLKVGKGINFPNAQLEIVSLTKEDKQALPYICQEADMV... | 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: 501
Sequence Mass (Da): 55873
|
A0A8B8N7P0 | MVLPWLFHSILLLSSLLRHATAQTTPPPGNCSQACGTVGIPYPFGIGAKCYLNNWFEIKCESERPFLASVGLEVLQITLATYVKEQGIIRVQSPIMYSNCSDAGDTSAPVSLEGSPFAFSQTKNSFAAAGCNMRAFLREAGSRSIGCESDCDEGRTASNISSCTGKNCCQNEIPVDLKIFNVTIGSISPGKDEEGCNYAFLVKKQWLVSNMIDPLTSLHMKNFPAVLDWGLNKLALDALGLTYYPAPDFTSHAYRCGNASDKSYLNSENSTTQCACFPGYEGNPYLAVGCQGTCVDIPGINTCGPNEAKFIIIGVGMALL... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Subcellular Location: Membrane
Sequence Length: 701
Sequence Mass (Da): 77630
Location Topology: Single-pass type I membrane protein
|
A0A6G1MB70 | MGKTFLSLPYEIKYKIFAEVLGDRFDFVFKSGMQVREVREKAVTDEWDDDYCLLVRVVPTRVPTRYLLVSREVKTVAIKVASDMDKLASQKQSEVTNDIVLKGGLPACSYYGWGQVFDQLWDDKKPSRIILAHHPPNPWHFLAQVNSMASVRSIYFTKAVTNWGYRGFEKLWYTHYPHNGSEIASWISIFLSASFPVLETIAIGVGKKVSPRHKSGLPIVQMLRWLRTGPRNCLEYQFGLPRLEAMDERNPRYRSLELIFEKKGKGIEVPLDLNSYCMPPFGYKWVKKISPDSEITGRGRYINEWDDFNRVEICKEEEGD... | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 707
Sequence Mass (Da): 81355
Location Topology: Multi-pass membrane protein
|
A0A165FBS5 | MRWLTLILAALLLSLQWPQWFGKGSWLRVWQLDKQLVAQRASNEQLLARNQALTAEVRDLKVGTDAIEERARNELGMIRQGEVFFQLLDPANTPHR | 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.
Subcellular Location: Cell inner membrane
Sequence Length: 96
Sequence Mass (Da): 11137
Location Topolog... |
A0A346TJ53 | MLNRVIYKRSQMLFSRAFSSKVELPALPWEISSLEPTLSAYLLDFHYNKHHQTYVNNLNSLLQQEGEAIEKGDFETATNLAPLIRFHGGGHINHTFFWHTLASKSQGGGERPSDSGKFGQEVSKTWGSFDNLITDFNTRSAPLQGSGWGWIVYDKNSKALAYTQTFNQDLITEKAGLIPLLNVDMWEHAYYLDYKNARPDFLNNIWDVVNWQKIEERFNDATK | 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: 223
Sequence Mass (Da): 25640
|
A0A8S1GSR0 | MRLPPLISLFPMLWIWTLLGALCLLTESSRILIYSPRMMQSHVNFMTRLANLLASRGHNVTVIDSILRYDIEHGLSEDVEGKEVEKQLKQGDVAKILWDSQPTPEDQRKVMNGLGQVHREQCLYLTRQDFIKKWKNVHFDIGIHEIFDTCGIGIMAAIGVNKTVIVSSTVMMEAVAIAIGHYSPIQEPSLLSDYGNNLGYLDLIRNLKFHSAWAHFFEMQSKLQEKTFKELWGVRQTSEDLIRQTSAVFVNTDPIADARRNHEKTKLFISHCGQNSMLESLKAGTELLTVPMFGDQHRNARAAEENGLVTRVEKNDLGNS... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 684
Sequence Mass (Da): 78317
Location Topology: Single-pass membrane protein
|
E4YF17 | MTNHDRLKARLAIHDNTVPNVFTTSTESQSATETRVVRLCQEFLDKLEIQPELRLDVRKHITYASKGLTSLGPAYESLDASRPWIVYWTTHALDLLDVVWSDEKKTEICEFLELCQSKNGGFGGGPHQMPHLATTYAAMNAIAILGANGFSRAYEIVNVENMKTFLNNVKNEDGSFAMHVNGETDTRAIYCAASVATMLQLKTDKLFERTPEYLARCQSWDGGFGPNPGAESHGGFTFTSLAALALINKTSVIPNLLSLVRWLCNRQKSVEGGFDGRANKLVDSCYNFWQGGSFPIVHGLLEQKHAPKNSWLCDSRALMD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
EC: 2.5.1.58
Catalytic Activity: (2E,6E)-farnesyl diphosphate + L-cys... |
E4YGK6 | MIFSTLLKTSGFLSPRDVIGWTLASGAKKNTVRDKKEAMDYMYQWFVFLWGVYALENYLNFRQWKVVRKSTYSDLNSMLKSHFTEESFKKSKSYANDKMSYGFVHEFYENIRTTVFTVLFVSPWFWGKAKDICAQYGFENEYYETCVVIFLTTIFESVIGLPWGYYSNFVLEQKHGFNNMTVKFWLTDKLKKLFTIGIPLNSAIMCMIVWVVKFFGENFYLYAWALVSVLMFVMMYIYPEFIAPLFDKYSPLKEGELKEKIEKLAGSLEFPLKKLYVVDGSKRSSHSNAYMYGFRNNKRIVLFDTLIASECTGKNEGKGC... | Cofactor: Binds 1 zinc ion per subunit.
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.
Sequence Length: 7... |
E4WX83 | MADQAQAIQAIQQLAAQDPEIQKLQAQAQFKSVIHGHTDRCWEKCNLGKEATQSSLSGRAKSCLDNCVRNFFTCEGTVNEVMQKMTSGNK | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer me... |
E4Y0A5 | MYEKLGSTNNYKKLGSAKTYKRHALADARNEEKIQKHFLVRKKKWRKTVQNRALFLATDAMKEDNSDSENESEPENDENSCKICFEKYESEGDRQKAAIVACGHQFCCGCLSSLPRKSCPTCRTAFNKKRILKLFP | Pathway: Protein modification; protein ubiquitination.
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: 1... |
A0A2U2N055 | MRLFPTGLHECPYFGDRPARLGFVDPRLPLDSSAYDQLLAHGFRRSGEQIYRPICPGCTACRSLRLPVHRFRPRRRHRRCRRDNHDVRLRSRGRVLDPAHHALYTRYVRARHPGGGMDDADPDLYWRFLTADWCHTEFLELRAGQDLLGVAVTDVTDGAFSAVYTFYDPDLPRRSLGTLAILMQIEEAQRRGLDWLYLGYWIEDCPRMSYKADFRPHEVFTPEGWEAVE | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-aspartyl-[protein] = H(+) + N-terminal L-leucyl-L-aspartyl-[protein] + ... |
N4TWX3 | MPSVRKEPEDNEAETSSDECVTEARDSRSQTGSTEQRGYIGLVRLYKRAIQAFDSHFVTACKGRISRCGTRRPTMLHPLKFPEGSTNYRASRRSLSAGRNSSPAHLDFRAFVDTLREDNDLADVTAEVDPKLEVAAAIRLAYEQRTKAPLFHNVRGAKDGLFRILGAPAGFSSDPKFPYRRLAQHLALPKEAGVTDVIEKMLSAKGKKPLPPVHVSTGPCKEKIIMGDDVDLTKLPAPLLNKADGGNYIQTLGINIIPHPTEPWTNWSIARAMVYDKTRMVGLIMKPQHIARIFEEWKKSGKDVPYAIALGAPPIATMAA... | Cofactor: Binds 1 prenylated FMN (prenyl-FMN) per subunit.
Function: Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of ... |
A0A7C8NGL0 | MVCCSFLLARLWFQKQKKRLDACLYYMDKADWIRMEFRHWPIGLLYDFYTALDPTKTPTLPPTNHDRPGSPPLAADPEPGAAPVPWTITLRFASYPHDFLTTLTPTSTHDAFINSIKEADFSRNGTAKAVMSLSPSDTRELFASLQDHDYDRFWGVNDKLLNHSGITVKNIPIRIYNPETGQVIQGSVPTRQPGTIRGDAQTLGTALNSLVPIIFPSKRSVVLARPVMHGIVLPLSAPLLELMREAMYPDGFLHITLAMM | Function: Involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation.
Subcellular Location: Membrane
Sequence Length: 260
Sequence Mass (Da): 29179
Location Topology: Peripheral membrane protein
|
A0A4U0WJV7 | MTDVDILSVAFESGGLGDEDLVNQMMTFLIAGHETTVTALTWALYLLAKHANVSKNSAMNCDYLHAVSSEVLRIGAPVSLALRLADSDTSLNGQIVPKGAYIILAPWALTTSTHLWRDDAPVRYETQFEEGSALAKGEMGIQGGATTKPQSGLWNLAVNILFRLERRSFASALAQHRLPVNPCDGMLRTLTNIMKPASKRVPIPKNGVDYRGKIVLAPMVRSGELPSRLLALKYGADLVWGPETVDKAMIGTTRRCNSLTSTIDFTRVSSNGARNPSLGTNQRESIIYRLHPQREGRRLIFQLGTSNPENAVKAAKLVAA... | Function: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U47 in cytoplasmic tRNAs (By similarity). Catalyzes the synthesis of dihydrouridine in some mRNAs, thereby affecting their translation.
EC: 1.3.1.89
Catalytic Activity: 5,6-dihydrouridine(47) in... |
A0A380MU61 | MTQEMLIIIVRIIAIILILIIAWTIIRIIQRTHLKQEKKSTQIHNDHSSLDESQIQKTSRLNPGFFGKNLSIPSAEELPNAPQADLPIAIMARYGCYFSGEDIQNLVKTFGLQRAPSGVFEMVNKNGRDILFTVLNIHQPGIFAENLDEMDAIEGILLVLQLPNGDDAVESYETFSAISKEMAELLDGRLCDFRRRPMGPKDLMQYRKAAEDFQIQFDEWLATHQRR | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 2... |
A0A4U0XEC6 | MASASLSAISAGGSYNILEDIKNDVEIVYFPKGSVLVEQGERNPGLYYVIDGFLDVSVPLDENSTEPNVLGTIPASHGIGASDLLGAPLQKTATGSSRSGSTAGEGGKKRPPNRKSLFLTKPGGLAGYLGTVSSYRSFIDVTAKTDVYVGFLPRASIERIVDRYPLVLLTMAKRLTSLLPRLILHIDFALEWVQVNAGQVIYHQNDESDAIYIVLNGRLRAIQESEDGGVKVIGEYGQGDSVGELEVLTESTRPGTLNAIRDTELAKFPKTLFNSLALEHPGITIKISKIIATRMRALIEDPLSDQGRERTAKGVRSKGS... | Function: Intracellular phospholipase B that catalyzes the double deacylation of phosphatidylcholine (PC) to glycerophosphocholine (GroPCho). Plays an important role in membrane lipid homeostasis. Responsible for the rapid PC turnover in response to inositol, elevated temperatures, or when choline is present in the gro... |
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