ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A076N8C4 | MGQGMATRAEGAPDLVITGTVVLDHWGVVKADIGVRDGRIVGIGKAGNPDTMDGVDPALVIGPATEVLSGNGKILTAGGVDCHVHFICPQLVDTALASGLTTLVGGGTGPSEGTKATTVTPGPWNLARMLQAMDGQPVNVLLLGKGNTVRPEALREQLVAGAGGFKLHEDWGTTPAAIDACLSVADESGVQVAIHTDTLNEAGFLESTMDAVAGRSINAYHTEGAGGGHAPDIIKVAGLPNFLPSSTNPTRPHTVNTLDEHLDMLMVCHHLNPSVPEDLAFAESRITPEHHRGRGRAARPRRHLDDELGLAGDGPDRRGD... | PTM: Carbamylation allows a single lysine to coordinate two nickel ions.
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
EC: 3.5.1.5
Subcellular Location: Cytoplasm
Sequence Length: 741
Sequence Mass (Da): 77391
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A0A8J4YU60 | MAKLPISIQAMEASCCVTVLPRKKRIVYSSWIWVLTFMIYCSYHLSRKPISVVKNVLHQNCSSLTPPENVNASVDPTWCDWKPFDGANAPTLLSTVDSSFLFAYAFGMFLSGIVAERVDLRLFLSFGMVLSGLFCAMFGLGYILKIHNIGYYIAAQVMCGLVQTTGWPGVVSCLGNWFGKGKRGLIMGIWNSHTSLGNILGTLIAASFVTYNWGLSFIVPGLIIAGLGVVVFFFMVPEPAMVGLPNPNKKMELEGTSSPHTRRRQMVGEFADTSDEERASLMANESPAIYDDKIKVVCVEAQESKEEKAIGFLEALKIPG... | Catalytic Activity: D-glucose 6-phosphate(in) + phosphate(out) = D-glucose 6-phosphate(out) + phosphate(in)
Subcellular Location: Membrane
Sequence Length: 524
Sequence Mass (Da): 57304
Location Topology: Multi-pass membrane protein
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A0A540NA00 | MHGLMNFYNLEWEGDAGSIQINGTEYFLNECHWHTPSEHTINGIRYDLELHVVHRSADKNSVAVIAFLYQVGPPNSFLLKVNIVSREQLELLQQVVDDYAVMSARPLQPANGRGIKLYVPSLTLSDDKVPHTTIKAASSPQGSINAASPKSSQSPIQVVFKQTINLPCEL | Function: Reversible hydration of carbon dioxide.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
EC: 4.2.1.1
Subcellular Location: Plastid
Sequence Length: 170
Sequence Mass (Da): 18868
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A0A4U0YAC9 | MPACPIAPIDATPAGGGALLRDVLGGVELICAQSPADRERFLALGAGRVEDCGNLKFDLPVAAAIPAVPSGREHTWLAASTHPNEEAQVLAAHQAVRQRYPDARLILVPRHPERAGEVTRLVEGQGFSVETWSPGRPPREECTVEIVDRAGLLAGLFAEVPVVFMGGSLVPIGGHNPIEPAAVGRAVLHGPAVENFRQVFAALDERDASRQVADSEALGRAVIECFDRPESWAAVGARARDVIAEHRGAAQRLVDRLARWLD | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A540KX62 | MSSPSPIPVSSQQSSHQQTQPSGTNPLRFLRPFLTRISAVSHHALSNSRPWTELIDRTAFTRPTSLTDAASRIRKNAAYFRVNYLIVLAVVLAYSLISHPFSLLTLLTLAGAWIFLYARRSSEQPLVILGRTFSDTQALFGLGVATLIAILVTSVLSLLLTAGMVGVGIVCVHGAFRDPEDLFLDETQPLGSGIASIFGGGAPSFASAGASMMSRV | Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Subcellular Location: Membrane
Sequence Length: 216
Sequence Mass (Da): 23104
Location Topology: Multi-pass membrane protein
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A0A847QR70 | LDAELTGENPLDFTGYEEKLNLSKEKTQLAEAVVTGYGKIHGLDTVVAVMDSNFLMGSMGSAVGEKITRAFEYATAKKLPIIVFTASGGARMQEGIFSLMQMAKTSAAVAKHDKAGGLYISVLTDPTTGGVTASFAMLGDIILAEPGALIGFAGKRVSEQTIGQKLPEGFQTAEFLLEHGFLDKIVARAQLKQTLSRILKMHLPSAN | Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase ... |
E3VI81 | RAELGTPGSLIGDDQIYNXIVTXHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLVSSSIVESGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRLNNLSFDQMPLFIWAVGITALLLLLSLPVLAGAITXLLTDRNLN | 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... |
A0A165JKX8 | HDVVIIGAGPCGLAVAARLTEATPSALFTDAEHERFWGKRHNSSHRKTLNKSEDLTRQSPSTSRPVSRYSIAVLESHSNQWMSRWNNRFDALRISHLRSPMFFHVDPGDRNGLLAYAYAERRERELKEVRNVVGKELSKHHRKQRRSAGKKAAAPKIVPVNERDREDYFRPSQKLFCDHCQDVSRRYKVDNLIQQTEVTSVSYDHAEDDSGRSLFTIESTTGKFYSRTVIMAIGPGVPQCVPTSYEGDVFAACHTSYIMDGGELPAHLMKKIKSKAATNVVVIGGGLTSAQVTDLLIKKGVTKVWHLMRGPTKVRHFDLE... | Pathway: Siderophore biosynthesis.
EC: 1.14.13.196
Catalytic Activity: L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+)
Sequence Length: 515
Sequence Mass (Da): 57907
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A0A8J4XNS5 | MKWVAQIPTVLYEPVLYEEQCTKVSFSSLEDAIAFCEKNGWNWITQDPPVKPPRVKSYGANFSWNKRTRRSTK | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
... |
A0A3P3Y9S4 | MSGADGVPNPVLHVSGNPESAPRPDAVPSESPMSAVAMPTGLPPQAHVRQPSRAAANSGPSQPLPSDAFLLPVAVASSSSPDGQPQPGRGHVRAPSKQAAPDHGGGRRSIRTHARAPSRYVMDADQQVHPTATFQLPSGVQDDEEPSGGRPRKDPQDLARKDRALPSAKQAALEQHMARSADSQLVVASPVPESRHSSGTGSNGASVKAGPAEPRSMKGGEARHRNGSPVSPGGDHRLQERRQFARSSPVGVKPRLFVSLMIVTDVALCVYSMYLNGWQFESFSTNPLLGPSSSVLDGMGAKDTGRIRAGEWWRLVTAMC... | Catalytic Activity: Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 526
Sequence Mass (Da): 55803
Location Topology: Multi-pass membrane protein
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A0A540KJK7 | MWFAGNVASGSAAGATTSLFLYHLDYARAQLGTDGRGSGVNGQHQFRGILDVYSKTLSSDGIVGLYRGEFFGWSVTTVSGVCPHPFDTIRRRMMLTSGQPSKYRNALRAFREIVHLEGFKALFRGVTANMLLRVAGAGVLAGYDQLQRVAYRKGYFIEPHQRVLK | Function: Catalyzes the exchange of ADP and ATP across the membrane.
Subcellular Location: Membrane
Sequence Length: 165
Sequence Mass (Da): 18211
Location Topology: Multi-pass membrane protein
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A0A7Y2E5D9 | MPDSDQLYYGDYLDLDRLLGAQRLESTARGRTAHDEMLFIIVHQAYELWFKQILWELEAVIGVLESEIVEERELAEAVAKLERIVVIQRLLLQQIDVIETMTPLDFMEFRDLLVPASGFQSAQFRLIENRLGMRPGDRLRYSDAPYTSRLSDEDRDRVRSSEKRPSMFDVIERWLERTPFVHTEMFDFWDEYGEAVDRMLEGDRRLILENSTLNKEEKERQIEGLERTRAHFNTLLDAESYERDRREGKVRLSHDALQAALLIHLYRNEPILHQPFRLLETLVDIDENFTTWRYRHALMVMRMIGTKIGTGGSSGHHYLR... | Cofactor: Binds 1 heme group per subunit.
Pathway: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2.
Function: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-... |
A0A8J4Y2H8 | MVGVAEMDSSSAWRKRCISCLTPAKALFKKSDGDFIRLLDCASCGQPVDRYVECERSIIFMDMLLQDIAVYRHILFNADNFTPQFYMKLGVALLLSEGYVRWSSLSHAFSPTTGIKDNEVYLYIMCLLTAIEIGIFGAIIVLYFWMRSHNRSPLSPLYNGLLLGQYGRLANVAAIIWYQAPSLVFQALVHVFIIISSIQSTRAALNAGKRESSVVVVMAAVISTSSSYILQTPLIKMYESYYL | Function: Mediator of sterol homeostasis involved in sterol uptake, trafficking and distribution into membranes.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 243
Sequence Mass (Da): 27276
Location Topology: Multi-pass membrane protein
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A0A164EY88 | LFGMWSGMVGTSMSWIIRIELSQPGSFIGNDQIYNVMVTAHAFIMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSITLLLTSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAVNFITTIINMRPEGMTSERIPLFVWSVGITALLL | 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... |
A0A1G9Y949 | MKKVLVINSSARTGRSQSRKLTEVFVDHWRSIHSNPVIRFRELGNADVPHINENWIAAAFKPAEDRSEQEVEALKISDVYIAELKEADVIVLGTPMYNWSIPSALKAYIDQVVRVNETWKRNPDNMQNPYIGLLENKTVFLLLARGAQGYEKGGYNEHIDFQTDYLKTVFNIIGINNIHVIAINGESFDAEKYRNAIAASHQEVKALMETELV | Cofactor: Binds 1 FMN per subunit.
Function: Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.
EC: 1.6.5.-
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Length: 213
Sequence Mass (Da):... |
A0A0V1PVU1 | MVFRLTVWKSGSSYGSLLQNLKLTDFRKGKLIGYTKRSLLCAVLVGDYLYSKLQSYLYSIEESEASRNVSKFRLINSVKTFFITHKSKILSNLNDCFKLLNLINFTLFLVNGRYPSLSHRLFGVSLTPIVTDLLKFNGNKVNFEFQNRQLVWNVMTEFLVFILPLMQLGKLKRMTKKIMSPYKKGQRHETGNTPVFTPYTNLPVSQCAICHNNNDIAATSSNKNSSINSSCMVTNPYVTNCGHIYCYICIATKFNSLENSDSYYEGCLRCGMKLQWFKEHGESEGEIDEDAIIVPYEDREESDNDDDEETVEQETEKHSI... | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 387
Sequence Mass (Da): 44427
Location Topology: Multi-pass membrane protein
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A0A0V1Q6G8 | MSGPTDSHPPNGNGPVLKKKSVKDYQFGTRIGEGSYSTVFSAVDIHSNKTFAIKVLSKKHIVKEDKIKYVNIEKTTLHRLGQQHPGIVQLYYTFQDESSLFFVLDFAEYGELLSIIRKFGSLSESVLKYYMSQILDAVSFIHLKGVIHRDLKPENILVGHDFNLKITDFGAAKLLGNTSDTSDESGEKIDYKGINQESSNGHHDHDRRGSFVGTAEYVSPELLKHNLCGFESDVWALGCILYQFFHGNPPFKGSTEYLTFEKIINVEYSYRNAIPPDIASIIDQLLVAEPLQRLTIPQIMASKWFRDVHWADQTYIWGRK... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 902
Sequence Mass (Da): 100650
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A0A0D9X485 | MEAAAALSDDFRCPISLEVMTDPVILPSGHTFERRSIQRWLDGGHLTCPVTNLPLPPSPPLIPNHALRRLISAISPPAPPPPAPEEKRPAAPPAASEEVCAMLRLAKSGPEGRKVVMESGDVAALLRWCAAGDETAARAVLHLSLDGDDARVGLVADGAVDALSAASREGRLELARIPGIVAVLAAVAGGGNARAIEQALVVLNWICGESGELAREAIKIGAFHLCEALVNDDNCKIAKNAVELARTLEKLLLGLKLLRNAPGGKLS | Pathway: Protein modification; protein ubiquitination.
Function: Functions as an E3 ubiquitin ligase.
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.
S... |
A0A0D9XJA1 | MTIVYGERAVVIDDFPADVAAELVRRVAAAAAGAGKDDDVQRGGVVDQLPVARKASSQRFVEKRRGRLAATAPYQPRPPPPAAANAGKEDGDGGWLELGTPGTTHPTQ | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 108
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 11274
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A0A1H1GZ53 | MSTKARTRLKVCCISTLGEAATAVACGADAVGLVAHMPSGPGVIEDDLILNIARQVPPAVATWLLTSRTTANDIVEHVLTCGANTVQIVKPIDPAEYQKLRLDLPASTRIVQVVHVEDEYSFEIAQEYGRVADAVLLDSGRPSHDELGGTGRTHNWDLSRHIVEKLDVPVFLAGGLTPKNIIEAIETVRPYGVDVCSGVRVDGRLNRAKLAEFAAAMACT | 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: 220
Sequence Mass (Da): 23549
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A0A3P3Y5B4 | MIAVGSVSNATMDRGKKFRMARSGDHTHFNMKYFGRSRRTIRLTGGGGYQQCVVSADSAEAHASGALISAVDEDCHTFYPDTAAFQGPPPPFDPSKISSSTIAAPLTYSSWGTPMFIRYLRRANARTYIHSTHGRPLCDASLHSKGHLQLELLVSVPRLVWSSSFIQTVRCEFAVSQFDFGMATSVLTSTLVVLLWALSLTVLVLSPSVGFIPKPSSLQGDEVDDDGTAAAASTANNVLATTPTDTVVAMAAMIAISVLCSVLVVVLHQRHVFVLDTARRAIGGLVVGTGFMWVVVVVLGAALLDNILSTLLLSCLLASL... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 421
Sequence Mass (Da): 45583
Location Topology: Multi-pass membrane protein
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A0A1E4T3T1 | MTDELDLQPTATVVPTTKPDLPEFTLENVLADIKFGICSLFNNPEFAKPMAMVILFVESLALKVIIGLVPYTEIDYESYMQQLAQIEAGEFDYEKISGNTGGIVYPGGYVYFYSWMRWLTEDLDDMNSGQIAFRYLYMLTLIFTLAIYLSSGGHNGKFSVKPYILYLICASKRLHSIYVLRLFNDCFTTFFMVATILVLQQASLYKKSNGLLSYILTLLSADLFSVGISIKMNALLYIPAYLVVTYFLCDENLLKLVPILLFGIGVQIGMNWTFLSQGDEIRDHFIAGAFDFNRKFMFQWTVNWKFLTEDVFQSDLFHKG... | Pathway: Protein modification; protein glycosylation.
Function: Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-Gl... |
A0A8J7T8M9 | MKEVFDCEGKPRVDLLKAHLTKEGRVEEAVALRIVNEGASILRQEKTMLDIEAPVTVCGDIHGQFFDLMKLFEVGGSPATTRYLFLGDYVDRGYFSIECVLYLWSLKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSEQVYDSCMDAFDCLPLAALMNQQFLCVHGGLSPEIHTLDDIKKLDRFKEPPAFGPMCDLLWSDPLEDFGNEKTQEYFSHNTVRGCSYFYSYPAVCEFLQNNNLLSVIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVF... | Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Cytoplasm
Sequence Length: 902
Sequence Mass (Da): 101734
Location Topology: Multi-pass membrane protein
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A0A7K2ZS95 | PASGREAVERARSPQRPRAEAYLADYFTVRLPLHGDRCGGTDPGLLTGFGLRADGQPVAYVAQCGTPTRPAGYRAAART | Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
EC: 2.1.3.15
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Length: 79
Sequence Mass (Da): 8386
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A0A2V3YAR3 | MMKRASVVKGFGLWAAVSLMIMVMSLLCITSAAAESQPRVLRVAFCEAKGISEKDPDGSRHGLVVDYLNEIAKYTGWEYEYFDTTPDDMLKGVAAGEFDLMGGNYYLPGLEEYYDYPDYNIGYSKTVIFAREDDDSVQNYNLRSLNGKTIGVYDRAVENIRRLKQYLSMNDLDCTLKYYTFEQLVDGNLYPYLKDGEVDLLLGNSVEAKQGVRAVVSFDSQPYYIVTKAGNQEILDGLNMAMAKIADSNPDFAADRYATNFLNESTVDIRLSEEEKDYIRQKGSVTVAMPRNFHPLACETPDDMHDGLSYDILQEAAEFT... | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporula... |
A0A540KM31 | MKRLKVPAAEHSPSPYNTSSAFIRESDPRCLLMPVIVSDRDTSVGQLGDLHLLQLATRSPGDVSGLISTSIRSALDCPLNYARSYLTELLPFCVCRVVYLNSNLILIDDIAKLSATPLGGGAVLAAPEYCKANFTSYFTFAFWSNPSLSLTFADHHTCYFNTNSKVKPSRWLVINLRNVDWNLYLNTLFWNLNYWDSISTLVGEVENPKKTLPKALFYALILVVLGYFFSLLMGTGAVPLDCELWTNGYFSDIAKIIGGFWLRWWIQGAAAVSNMGMVVAEMSSDSFQLLGMAEQGMLPKFFASKRL | EC: 2.4.1.-
Subcellular Location: Membrane
Sequence Length: 307
Sequence Mass (Da): 34190
Location Topology: Multi-pass membrane protein
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A0A6M3YPK1 | MQQPNADELEYVRAAFDNANHVAPRGPKLPGDPDFNIYFRSLLRTLDPKSSTGLGAFEAYATIGDALGWDGIRFTEVHRVAELQRLVESRLRDLARGVPDIAWFNDRAEEGADIAFQELKRALQGQEEQEAPPADNIKLFIKDEPHKISKVSEKRWRLISAQSLVDQMTDRVLFYSWVETEISDHFNVTSKGGWSPLPMGYQRLMAEFPEDTAVAVDKSLWDWTMPPWVVYEYLQAKARATPDMSDELMWLWARRFWFVLGPGARVRMPTGVVWRQDCWGLMKSGFYLTLSMNGAAQMLQHALAWRRMGKLTFPPRIWTM... | Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
EC: 2.7.7.48
Subcellular Location: Membrane
Sequence Length: 447
Sequence Mass (Da): 51169
Location Topology: Multi-pass membrane protein
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A0A540KCQ4 | MRGHQQNAIHLEEKEKREKELLVQIIEEADEFKLGFYQKRKITTENNKAANREREKLFLANQEKFHAEVDKNYWKAIADLIPNEVPAIEKKRGKKDTEKKPSILVVQGPKPGKPTELSRMRQILLKLKHNTPPHLKPSPPAPAPTKDAKPSTSAPPKAAVVAATPEAVVAAL | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular Location: Cytoplasmic vesicle membrane
Sequence Length: 172
Sequence Mass (Da): 19327
Location Topology: Peripheral membrane protein
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A0A0V1PTM4 | MFNTNHFHDRMGSEDLRNQFLSNANPPQPKDNLRPNGSYVTDDDDRSIIFGNDNSNLAPYPTSKGYSGISKNSDSSNANTHEYELDRLQSTYSINNSSAENPFNPLQGNHPYNGYGQKQKENPFRDQSVPEFPQQEYNPFEPHREQPPIPVDDEYEKMRKNEKARLKQLRRKPRFHYTKLPYFTILVTLIQVSVFIAELAKMSSLTGSAFQTKPYFNPMLGPSTYLMINMGARYAPCMQSIKGITNDTTINFPCPNSTTTDTNVCSLNELCGLSGVPVKDDVYKPHQWYRIITPIFLHAGFLHIIFNLLLQVTMGASIER... | EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 609
Sequence Mass (Da): 68833
Location Topology: Multi-pass membrane protein
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A0A2U9I5S7 | KDYKLTYYTPDYETKDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIESVVGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYTKTFQGPPHGIQVERDKLNKYVRPLLGCTIKPKLGLSAKNYGRAVYECIRGGLDFTKDDENVNSQPFMLWRDRFVF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 203
Sequence Mass (Da): 22950
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A0A0D9W8U3 | MGREERFPVWEAALGAGVAAAFATGLVGVYLSMPDSDYSFLKLPRNLEELQILTGHLENYTSDYTIQVLVGYCSVYIFMQTFMIPGTIFMSLLAGALFGQLRGLALVVFAASAGASSCFFLSKLIGKPLVFTLWPDKLMFFQKQVSKRREKLLNYMLFLRVTPTLPNTFINLASPIVDVPYHIFLLATLIGLIPAAYVTVRAGIALGELTSLSDLEDQEVSYSINWAIAGRGVVVRDKVFYNLETSELQKGGIVYTGNVTSGNPDVSRAQFAKLLKLVTFHLSSISSLYVQDGAVDSSMVCDAKVRVISDNPSAVMLLSN... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
EC: 4.1.1.49
Subcellular Location: Membrane
Sequence Length: 544
Sequence Mass (Da): 59231
Location Topology: Multi-pass membrane protein
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A0A1H0Z2C5 | MFSSTLVRFFRIATGLAFAVLIYAVLVQVLGRNVFNDSPVWTEELTRFALLYLAACGVGLSLRTGDLVNVDILINYFPTKIRRAFLIFASVATAALCATLMIPAWRFTAIGKWQTSPALSWRMDFIHASTIIFLGSILLFALLKIFEGIRDFNGPEDQIGEESE | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 164
Sequence Mass (Da): 18289
Location Topology: Multi-pass membrane protein
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A0A540MUD4 | MWLGEKGTIKGVKFRRKGSQEFTAHAPLTIVCDGCCSNLRRYLCNPKVEIPSCFVGLILEDCQLPYANHAHVILGDPSLVSFYPIDSREICCLVDVPGRQVPSISSGEWLTTWKQRWHPSRIIFQVPPELYTAFLVAIDKGNIKAMPTRSMPATAYHTPGALLMGDAVNMRHPITGGGMVVALSDVVALRNLPRPLRNLNDVPALFKYLESFYTLRKVSSLCWSFELLKSHIGELKGN | Pathway: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 2/3.
Function: Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.
Catalytic Activity: O2 + reduced [NADPH--hemoprotein reduct... |
A0A7Y2GB53 | DSKLLSREDRERLAARIRSRAVAVAVGVCSPEEIDELNILWASMEAMRRAIQKLVPQPTYLIVDGNHVIPDSAWPVEAVIRGDFKSQSIAAASIIAKVERDRLMHHLHEAHPEYNWISNVGYPTRAHYEALSSHGASPLHRRTFNLENPYPPFSEAATEPEQVDGHSSTR | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 170
Sequence Mass (Da): 19095
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A0A0G4IH25 | MLLSEGAFPSVGPHNCCYLLAPADQLAGPNAFPNNYYIGFTVNPPRRIRQHNGEIKGGAKHTKSLAPWEMLCVVHGFPSQTAALQFEWAWQHCRRSLRLRPVWAEFTKWVTRQGRTIRKAFPDAQGVGITSLFAKFAVLHKMLAIAPWVHFQIHIRYIHPVCKEFLDRYCGDVLADLSNKSLTVSWGHFDSSTVTMFARDDVSPASSADNESCAGEKACHICFSAGRPDAYFGHCPSCRAAAHLVCLWRNNAEPGRILPRDVTCPTCGTLLPWSSVIANSGRGSERQATSISSLVDPMMAMSLSTIPDVIDLRSSDDEDS... | Function: Catalytic subunit of a heterodimeric structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
EC: 3.1.-.-
Subcell... |
A0A1C9D4Z8 | WSGMVGTSLSMLIRTELGNPGALIGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLMSGVVESGAGTGWTVYPPLSSSIAHAGASVDLAIFSLHLAGISSILGAVNFITTIINMRPIGMTFDRMPLFVWSVGITAILLLLSLPVLAGAITM | 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... |
A0A344ANV3 | MVLSYVCLLVFVAVAASVQDFVNVGSYISLDFVGCALSFISILLMIFFFIFCGSVIGKLEAVLIGISSIFSVVCFLSNDTMVFWVSYELAIIPLVYSLLLGSPYSERFLAFWYLLGYVCLTSLPLLFSIQYVNFLAHTTNMGFKYGLEGPGGFILGVIMFILFSTKIPLPPFHAWLPIVHAEASTIVSVWLSGFIMKLGIIGMYRFVLPLIQDNSNMITVLIGYSVAILLSCLSELDTKRWLAYLSLGHIVIAVVGLLNSEGVNSEAPIYCLGHGFSASLLFICFLFIYESFGSRSWLAVSLAGRISVGFLLVISTSLLT... | 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 ... |
A0A7L3PLJ7 | MASLALELLGFSLTLLGLLGTLMTTVLPHWWRAAHVGTDILTAVGYAKGLWMECVWHSTGIFQCRAHLSQLALPPELRAARAMMVTSCCLSLLASGLAVLGMQCTLCAQGSPKKASLAVSAGATFVLAGLLCLVPVSWSTNDVVMDFYSPALPGGVRYEMGQALYLGFASALLTI | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular Location: Cell junction
Sequence Length: 175
Sequence Mass (Da): 18462
Location Topology: Multi-pass membrane protein
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A0A0G4J6T3 | MHGIRRVDPSQVTEAQRAEKRKKIAKYVAMRDDVLAMRKDRRHDKEALALTRQVLEINPELYSLWNYRREILLGMMDKRSCDVAELLADELNVVGRAIQRNPKSYVSWHHRLWVVQRGGSDILKEIDLTSQFLMADARNFHCWDYRRSLVDLSNVSPSEELEFTRKKINDDFSNYSAWHYRSTLLTKIGIDQEVLDREFALVADCFFTEPDDQSAWLYHRWLCVQHPDIACLEKQLSIMDELLDLEPNCKWALLTSVRLLSELCRLDRTRSVPKRRIGDIFNRLPVLDPQRKTYYRDLCDRICVQLGPCIE | Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences.
EC: 2.5.1.60
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Length: 3... |
A0A1E4IJB6 | MRHGLFLRALETAACLALGAMMLLTVADVLGRHALGRPVPGTVELVQYALAIVVFAGLPVVTRDGRHISLSLLEGRLGAPARRLQRLVLGLASAVILAAQGWIVFGTAQLMRAQGDVIGFLNLPVHPAAYLMSILSFVTAAALLLDSTFANGREAPSGGAAH | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 162
Sequence Mass (Da): 16912
Location Topology: Multi-pass membrane protein
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A0A8J7NKY8 | MDLKGKGLTLNEVNPCARSIEVLDKEFIRMRAREIRKELLQGMKKPYKKLIDVSSGDAHMAGMKPISFLRQVLAVCLYPELLHSDRFPADVKQRAQRLLKNCEGGSLGSYSPPCGILSIRRNVSEFISQRDRGVPSDPDNIFITSGGQDAIRCILKILVHGEGHAQTGVLMPVPSYSYFKIAVLECGGAIVPYHLSEEQGWDLQVVELRRALQTARGHCSPRALYIINPGNPTGHVQSRKSIEEVIRFAAEEKLFLLVDEVYQQTVFGEGSAFVSYKKVLYEMGPSYSDMVELASLHSVSKGFTGECGLRSGYVEFVNLD... | Pathway: Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.
EC: 2.6.1.2
Catalytic Activity: 2-oxoglutarate + L-alanine = L-glutamate + pyruvate
Sequence Length: 477
Sequence Mass (Da): 53082
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A0A8T2MI97 | MAVQLVEGCLYYVDSEGNRVCGDQFAVGSGSMYAYGVLDSGLRPDLTVEEACDLGRRAIYQATYRDAYSGGTVNLYRVHSQGWERVSQDDVLSLHQQFASGSA | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processin... |
A0A8T2MLT7 | MYYLSLSQTPQPRELLAIEEESERLARELREVSRNRESLRNQLAQLCRYRGVLICTHSLTTSQATPPFLKSSSLLDNRQDVRLSFVAGVVHPWKVLAFERLLWRACRGYIIINFREMEEKLEEPDTVRDEGREGKREGKREGGRGSIGVGRNVGWQQHACVQVGWQQHVCVQVGWQQHVCVQVGWQQHACVQVGWQQHACVQVGWQQHACVQVGWQQHACVQVGWQQHACVQVGWQQHACVQGEMVQWTVFLISYWGEQIGQKVKKICDW | Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Location: Membrane
Sequence Length: 270
Sequence Mass (Da): 31250
Location Topology: Multi-pass memb... |
A0A8J4Y8N9 | MVEKRPKGTPLITVCNHYSCIDDPGLWGVLKWRHLWSATTMRWSPAAHDIAFTRRIYSWFFSSGKCVPIIRGGGVYQHAMDFLLERLGEGHWVHIFPEGKVNMTLETMRLKWGVGRLVYDSLVSPIVLPFYHIGMDRILPNHPPYIPRLGKWVTVVVGEPLDFRAEVQEMRKRNEDPATARRRITDRIQEELGHLRERAEELHGKLMAERGEAWKPMVHARNEGQVGR | 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: 228
Sequence Mass (Da): 26454
Location Topology: Periph... |
A0A0D9V3C9 | MPVIPAQAPPTLPPPMGVTVIMPNSGTPASTSQSPPGPTAGTAISSPLAPPSGSWGGNAPSGLLVGVAVAGFLLALVSMGLFLCLKNRGKRRRPAYTTNLARRNTLVVPDRVVSPDVYQPSNGPAASPSGTNSYDFSGTTSWFTYDELAAVTGGFAEENVIGEGGFGKVYVGALGDGRRVAVKQLKVGSGQGEKEFRAEVDIISRVHHRHLVTLVGYSFTEHHRLLVYEFVSNKTLEHHLHARGLPVMDWPKRMKIAIGSARGLTYLHEDCHPRIIHRDIKSANILLDDAFEAKVADFGLAKFTNDSLTHISTRVMGTFG... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Cell membrane
Sequence Length: 496
Sequence Mass (Da): 53692
Location Topology: Single-pass membrane protein
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A0A7Y2E3Q3 | PNKTWEGAAGGLVGALVVAWLYAEFRNPMFGLSNALVLGAIAGVLGPVGDLIESLLKRSAGVKDTSNLLPGHGGVLDRFDALIFTVPVHYLYLKYFTTLLQ | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 101
Sequence Mass (... |
A0A2S0L2C1 | MRGTSVKKNLDWRLEMKAWDNLRKSFKIAILTVLCITMVFSTGLLYMISYGASDKSSSKSSKQTESAKTSSVTNKVQAPEINAKSAVLYSENTNTVVFSKNKNERVAPFSTTKLMTALLVVKHIKNLDQKVTISKEAAALGGSSMELKEGEVVTVRQLLYGLMILSGNDAAYSLAEVVSNGNVDEFVKMMNDEAKALGCKDTNFVNPNGMKEENHYTTASDYMKIARAALKNKQVYKFASTKKYEMGATNLNEARVMKSHTDLINTKGSGVVAGKTGFWNGEASIVLAYDKKDLKMVLVLFGDDKENRPKDAKAIFEYAY... | 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... |
Q8HJB7 | MTTNTRKTHPILKIINNSFIDLPTPSNISAWWNLGSLLGLCLTIQILTGLFLAMHYTADITSAFTSVIHICRDVQYGWLIRNIHANGASIFFICLYMHIARGLYYGSYMYIITWNIGTILLLLVMATAFVGYVLP | 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... |
A0A3G1XSW2 | IFGIWAGMVGTSLSLLIRAELGNXGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSVVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRINGLSFDQMPLFVWAVGITALLLLLSLPVLAGAITMLLT | 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... |
A0A8J8WAG4 | MRVHEMVVPARPVINSAPLPHATTPLLANNTRPTQGLAMLTGEVAPSGRGAGAEPRRGGRCVRVTPAVRYRPVRSLLLLGLLVLVSLFVLFTLSQMAVVQHTMMAHLGTGVAPGVAGGGSGAAPGGARGPKGPQRPWRSQFNQFKIEPLLVRNAPSVEVNLAMASNLRMANQIAAIIIRNSLLVSHSAHSTLAPQTPRTAQGKAQVASSPHNLPSHDQPNMNTNTHHFINTFYNSSTQAQQMRSGLHMSDTLHPGQQSSTAGQGQEASTPVGARGRAEQEGAKGIAEPSPLYEPIDSDVMELAARKNDSNRKRNPSSRLS... | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 613
Sequence Mass (Da): 67577
Location Topology: Single-pass type II membrane protein
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A0A455TA43 | MLNKKYPVLYLTAGLDEVGRGALVGNVVAGAVILDNSKLIQGLKDSKKLSYNKRTKLSVIIKLKALSWSIGIASSREIDFLNISNATKLAMKRAIFNLSIQPNFIFLDGKFKLNINMPCLSIIRGDNIISEIKAASIIAKDYRDREMLKLHNIFPKYKFNKNKGYPTSHHLKMIRNYGITKFHRSSFAPISKMQ | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subce... |
A0A1H1JFG7 | MNLLHKLDRMLSNLFLLLGMVLLVVLFALTSLNVILRFFPIFSIGWFDEIVEVSFAWMVFTVAAYLWRDRAHPFIDFLLESLKGRRSQYVLLIFIESMNIFFLVAFTYYSFSLMMRASAWSPIFQIPKSFFYMSMPIAGAYMTIVSLFFWAGHLRNLCSSNPTPFTYSSCQK | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 172
Sequence Mass (Da): 20118
Location Topology: Multi-pass membrane protein
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A0A223KUF8 | MKKLLVLVSLILVLIIAGCGTSDNNEEQTGQGSNETTANNDTNNAAGDDQEEPVDLENLVFPQMSTEVAENERVVEIVTNKGTIVVKLFPEHAPKAVENFITHAENGYYDGVIFHRVIEEFMIQGGDPNGTGAGGESIWGEPFEDEFALELLNFRGALSMANPGQPHMNGSQFFIVQAGPLDDAYEEQLKKAGYPEKAVEFYMENGGTPWLDHRHTVFGHVLEGMDIVDEIAQVETGANDKPVEDIVIEKVNVTK | 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: 255
Sequence Mass (Da): 27934
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A0A1H3JRA8 | MLEGFIDIHCHILHGVDDGSKNLEMSEKMIQIALDDGIIGLVLTPHIRAPRFMLANEIVWEKFDELREDIRKKYPQIHLYLGGEFYYYSSILEDSPQMIRTINETDYVLVEFSPVIAYDDMLRAFQKLKANGYEVILAHLERYEVLRKNIDNVEHIKDMGIVLQMNANTIVTPFDREHKKFMKRIIKDELVDLVATDAHDLDTRKPCLSKAASYVTKKTSDEYANAIFVENQLKILKGKRII | Pathway: Capsule biogenesis; capsule polysaccharide biosynthesis.
Function: Dephosphorylates CpsD. Involved in the regulation of capsular polysaccharide biosynthesis.
EC: 3.1.3.48
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Length: 242
Sequence Mass (Da): 28132
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A0A8J5CR89 | MKPRWGPYHRGALELAGLYSRGKRTQEIVCVCMCITLMVVNLYFMAVHFRVEKVGSICLVALAGIFTADFASGLVHWAADTWGSVELPVLGKKLKDLTCAHEYAVAVSNRFDVLGALGDPVELWIPSNVKLYRLPRSVLGSAPGQGVVLSPTEMLEKIEESRAARLAGNRDQHRGSVTPD | Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Membrane
Sequence Length: 180
Sequence Mass (Da): 19708
Location Topology: Multi-pass membrane protein
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A0A165JV82 | MTTDSQNAERTMGAAPVRLCKRCQEIEATTIMRTEPLCSNCFVEYIKKKVAKQLEAYRIKNASKNNRRRVLLPISFGVSSLSLLHVLDGHLQSQIRRTNRTGYELHVLHVNTSGVDADAPQIGRLEVLKEKYPRHTYSELTLEDVFDHANEYLETTLRDVNINIGDVAPPSSKHEKLVGLLSALPSPTSRADVVETLRNNLIIAFAKENDCQSITWGDSATRLAEKTISETAKGRGFSLPWQISGGESPYGLHVSHPLRDVLKKELVIFAENVDPPLTPLIHSRPAPTMTSAPAKSTTIDDLMGQYFASIEESFPSIVAN... | Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with NCS6 that ligates sulfur from thiocarboxylated URM1 onto the uridine of... |
V5NFZ1 | MPILQILTGLFLAMHYTSDTTTAFSSVTHICRDVNYGWIIRYMHANGASMFFICLYMHVGRGLYYGSYTFLETWNIGVILLLTVMATAFMGYVLPWGQMSFW | 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... |
A0A8J4XQM9 | MVPQRLWLKKFALIALLLDEEEELNSKRHCFGYTQNGLLHMLDRNRRIKPDPERFQICKDKFDIIVTCEERVYDQVLECLEARIPEENTPVHVINIDIQDNHEEATIGAFMICELAALVSGNIYETIEHFLLPPARWQHPQRSYCLHLDTRHSRFTCTASVSPLTPTAPGAGTSLETIEHFLLPPARWQHAQRT | Function: Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 194
Sequence... |
A0A3P3YA61 | MLSSIAPMRSGLLGGVTVRGVAGSGPLPVALPRTCHFALGRAACTLPPAVMGARDDGDELALWDALQAGALLSTGRFTHAGRCASLQWTYKHRASNSTVAISSTHSVDGARQQTTAPADFEVTAPVSLSSYCHRGCCRAVIRKPSDDTGAFLEIYRQGRPPLTTSLKKVCGELPKGGSCLSGASFSANCDKFAFSADVKPDDRQSFWNDTPAHGNDAGSQPSRGTQYDYKQDWGEGLGLLRTIVVLVDIVDDRLLATVLDKAFNEKFSWGQVVFHPRQPYLLAVGYPQTGRRLGLLHFNTRRSSMFVASLERRDECATCI... | Catalytic Activity: Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.
EC: 3.4.19.1
Subcellular Location: Cytoplasm
Sequence Length: 748
Sequence Mass (Da): 81249
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A0A5Q0U1C0 | MKLISSLMFSMSSMAILMKHPISIGVALTTQTILMTMITGMMNMNFWFSYILFLVMIGGMLILFVYMTSVASNEKFKLNLMLVTAATTTFLTSMLFNKSEMNLSFKIKETLNFNSNNTKTMLTKYFNFPSMTIMMFMMIFLLLTLVVIVKLTKKSMGPIRKNI | 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 ... |
A0A679ENZ2 | MTFSYAIIVLYSLLLSCALFVVLTMNTVYAVFFLIFAFFTASAVLLYLGFEFLAMVFLIVYVGAIAVLFLFVVMMLNVRYIPWLKKDLRFAPLGFLILAFFLLLFLFAILHIESDIYWSLNIPYSFLSANLESAHSQISSAENTEMLGTLLFTHYGYPFLVAGYALFIAMVGAIVLTLRHIPLPSKKQDAYVQVTRLLSTVRLLAKDKA | 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 ... |
A0A3B0N237 | MTEERYVIWFDEPECDQVAVAGGKGASLSSMVRQGLPVPNGFVVPAGVLEACVDAEALKAYARAQDYAAAMKLVEDTAVVPQEVMTAYEELGGKVAVRSSASAEDSEAASYAGQQETYLNVVGAEDVRRRVIDCWTSFFSERALFYRGQKGSLDDLRMAVVVQQMVDCVFRRIRPPIPTTSGHLFRGIRPPVTRCREAAYFGYQS | 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: 205
Sequence Mass (Da): 22519
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A0A8T2N9H9 | MLGEGVEVANTGEELLIERSIRKGMINPGDDRQTIQHNGPVTSFNYTIRVKCDENYYGNKCNKQCRPRDDYFGHYVCDQFGNRGCMEGWMGPDCKTAICKQGCNLLHGSCSEPGGCTCKYGWQGPYCDQCIPYPGCVHGTCSKPWQCSCEKNWGGLLCDKAEHACVSNPCANGGTCHEILSGFECQCPPGWGGATCAKGKAAHPALEEKTPVSLTLSLPFSDWELFHRTEYMDECASNPCDKGGTCIDRENGFECLCPPQWAGKTCQIDANECMGNPCLNAYSCKNFIGGYLCYCIQGWVGQNCDISIYACHGQCLNGGT... | Function: Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Location: Membrane
Sequence Length: 587
Sequence Mass (Da): 64343
Location Topology: Single-pass type I membrane protein
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A0A8T2NE13 | MNGATFPSPTAEMAEINRIHYEIEYTEGISQRMRIPEKLQVAPSASEDQDAGPQDALHSVLMQVPERIVVAGDSEVSQYPRPRDLDLIQSTPLESLSLKTPPRNGQVARNDST | Function: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface.
Subcellular Location: Membrane
Sequence Length: 113
Sequence Mass (Da): 12487
Location Topology: Single-pass type IV membrane ... |
A0A8J3XWY2 | MQHARAGEGGPQRHEQLGDRLRSKRIVVLGQEVDDEIANRICSELLLLSAEDSQRDISLYINSPGGSVSAGMAIYDVMQYVPNDVVTVTMGLAASMGQFLLCAGTPGKRYALPHARIVMHQPLGGIGGTASDIRIQAEQMRYTKKLLAERIAFHTGQPLERIEADSDRDRWFTAEEAKEYGFVDHVVAGVRAL | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
A0A1E4SXZ1 | MTEASDSLPPSFASDSNPPPASSTPFEVIFNPRLKRTSTTNYRTELEAQQQKAEDDARSQLTRRESEKNTFDKMSAQNFKRQLSFTKPDDDSKIEAPIETIYTRDSSAIDEGKEKHSLLGDIKNKLHIGSPHSLHSHHQKHETDQSEQTKLSKYEFGLNVSDQLNSSNSSSISISDVSPNESTSYTQPHAKRKNKKKNRLKDKQFLLPDDNSLTFKVLRYPFLIFIAMWLTVLSIVYLIVRLSIYISEQVMANTGQRRKMVNKLKNSKSYPEYIEHAKALNEYLKLDKWCEEDRFYCYDWKTLRRIVRDLRKLRRAGKNQ... | Function: Lipid hydrolase.
EC: 3.1.1.-
Subcellular Location: Membrane
Sequence Length: 779
Sequence Mass (Da): 89092
Location Topology: Single-pass membrane protein
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A0A1V1PKQ5 | MRRGLPLAYPGMKIGLFGGTFDPAHEGHAHVAETALKRLRLDRIWWLVTPQNPLKPQSSPLATRMKSAGAMAHGSKHVVTDLESRLGRHYTFETLRALKAIYPGVRFTFVMGADNLANFRQWKNWREVAYAAPIAIVARPGVPARDKARMPRTWTWLSARHHTQSSTAIRARKRQAVANRKPG | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A220EKL7 | TLYFILGVWSGMVGXSLSILIRMELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLSLLLISSMVENGAGTGWTIYPPLANNIAHSGASVDLAIFSLHLAGISSILGAMNFITTIMNMRSNGM | 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... |
A0A6U7DPM0 | LMXSAPDMAFPRLNNMSFWLLPPSLSLLLSSSLVENGVGTGWTIYPPLSANIAHSGASVDLSIFSLHLAGVSSILGAVNFISTIINMRPPGMSFDSMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLF | 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... |
A0A076MHF5 | MTTTLARPGGGTSTEPAPRPALTRLGPGRTLAELVLGTVAAVVFSLVLQFGSNKLGVDPGTYVPDALVNLAVAVIVVVLFGSLAYSGAARWPLWVRLGGSWAALTALSTLLLAIPLQGTRFFLGGSSVDNTFRLQYLERLTETAGLGDVNYHGLAAYYPGGWFWLGGRFANLLGLEGWAAYKPYSITWAAVSGVVAFVLWSLVVRRRMALLASVATVLAGFVALAPEEPYAWPTTAWLPPVMLLAWHALRSRERVPAWTLLLIGIYLGFSAVTYTLHVAYGVAAVVVLALVALALDVRAGQQPWPVVRRLLLRLVVIGVV... | Pathway: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
Catalytic Activity: Adds an alpha-D-arabinofuranosyl group from trans,octacis-decaprenylphospho-beta-D-arabinofuranose at the 5-O-position of the eighth, tenth and twelfth galactofuranose unit of the galactofuranan chain of [beta-D-galactofuranosyl-(... |
A0A158CT56 | MTDQYAVIGNPIGHTKSPLIHGIFAEETRQDMAYTAIEGPLEPEQAFAETVRAFAAAGGRGMNVTAPFKLKAFAMADERSERAALAGAVNAMKFENARIIAENFDGIGLVRDIEVNLGLPMAGKRVLILGAGGAVRGALLPFLAARPAEVILVNRDIAKGRALAAQVSARGPISACGYGDLEAMGRFDLVVNATSASLTGDLARFAECLQP | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 211
Sequence Mass (Da): 22126
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A0A1E3T5M4 | MAKCVMVLYPDPLGGYPPKYARDSIPVIDSYPDGSSLPTPSKIDFTPGELLGCVSGALGLRKFFEENGHELVVTSDKDGPDSEFERELHDADIVISQPFWPAYITEERFAKAPNLKLALTAGIGSDHVDLDEARARGVTVAEETWSNSVSVAEHAVMQILALVRNFVPSHQWITDGGWNIADCAERAYDLEGMDVGVIAAGRIGRAVLERLQSWGVHLHYFDIHRLSPELEKQLGVTYHPDVESLARSVDVVSIHSPLISQTHGMFNEKLLKSMRRGSYIVNTARAEETDQKAIVAALESGQLAGYAGDVWFPQPPPKDH... | Function: Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.
Catalytic Activity: formate + NAD(+) = CO2 + NAD... |
A0A8J7NDC2 | GIRKSFLRTPQTRGSVPDWSSPCKEGSSDSEMDKAPQAGKKKTKRVRKNRKTAKTEVKDNEEDEGPVEKKRKACECKTEQLKKEEGQSKAFDHRGFTAQVERWPSNPVDSIISYICNKPSSMVVSDFGCGDCKIARRVKNKVHSFDLLPINDLVTVCDMASVCLFSVRIFPDPSPRWLGGCLSLMGTNTGDFLVEANCVLVIR | Function: Probable methyltransferase required to silence rDNA.
EC: 2.1.1.-
Subcellular Location: Nucleus
Sequence Length: 203
Sequence Mass (Da): 22645
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A0A540LML4 | MHLKNLEASRCSCWSVESDKMWKQNFQCINLQLLMSFEGFIRDKYTALPDTRERILATEITASWKYQYESIFSIPQKPLYFTERYLSVKKALADTFYGPPKEGVYSPSVQSTLYHMAKTVLNGFPDIEAVQLKMPNIHFLPVNLSNKDNTIVKFEDDVYLPTDEPHGSIEATLSRFWSKM | Pathway: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3.
EC: 1.7.3.3
Subcellular Location: Peroxisome
Sequence Length: 180
Sequence Mass (Da): 20921
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A0A482I474 | TLYFLFGIWAGMIGTSLSMLIRLELSTISNMIGNDQIYNVIVTAHAFIMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLXSSWVETGTGTGWTVYPPLSSIIAHTGTSVDFSIFSLHIAGVSSILGAINFISTMLNMKIK | 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... |
K1ZBC6 | MTVHTFGNIAGKKEIELYTHTYVREDTLALYGFGEISELEMFELLISISGIGPKAAMGILAIADPKTIGMAVINEDPSILTRVSGVGKKIAQRVILELKNKIKDMPMHEKTQLESDSDAFEALVAMGYSVSESREALKQISSDITDVGERVKLALKSLGRK | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A0A1V6F3D8 | MNVLIIGSGGREHALAWKIARSPLVQKIYAAPGNPGIDRLDKGVCVNVAADDFEVLRTYIEAERIELVVVGPEDPLAKGIVDTLGTEDTLVFGPSARAARLEASKSFAKEFMARHKIPAAEYAVFDDARSAIDYIRAAEMPIVIKADGLASGKGVTVADSVEKAEAAIRAAMIENTFGLAGQRVVVEACLVGEEASILVFCDGKTFKPLASSQDHKREFDQDQGRNTGGMGAYSPAPIITDAMMDRINREILEPCLRGMEEEGMPYTGILYAGLMITKEGPKVIEFNVRFGDPETQAILPRMDTDIVPILKACCTGTLAE... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Len... |
A0A660TR58 | MMNMSLKLNSEIRYIKGVGPSTAEKLNRLGIEIVEDLIYYFPRDYEDRRNLKTLAETDEGEKATFHFKVIDQGYIRFNGRNHPKIKVTDKTGIAYLYCFNRNYLKDILVPGTSFYLIGKYSLKGRYPIFSSFNYELDDNNAKLGIIPVYRLTSGISQNLLRKIIKTVLDSLSDKLKEEIPEFIRKGYKIPPRGEIIKRIHFPPSQRELRRMREAYSYQEFFKYQLIVAMAKSKNKEIKKNRIKSSGELREKFLKKLPFKLTNAQNRVLSEIDRDLDSPAPMNRLIQGDVGSGKTIVSVFAALKALERNEQVAFMAPTEIL... | Function: Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA).
EC: 3.6.4.12
Catalytic Activity: ATP + ... |
A0A7V0SDR8 | MGSGGSRGLQNRRPQSIAAAGSIPAPSALIKKMDTADEIFRKVPQVEKLLQSEGVRDYTPVLGRDVVVGIIRDETRHFRDLLKKNADTPVESLTDAIVQRCRAKKLEKLQRVINGTGIIIHTNLGRSPLAEDILENLKQIAGGYCNLELYLPLKKRGRRGGFAEELLCLLTSAEDALIVNNNAASVFLILREFGAGREVVVSRGELVQIGGGFRIPDIMNQTGACLVEVGTTNITTVEDYRRALTERTAMVFSAHRSNFRMEGFTASPELKELAALKEESLLFVRDLGSGNLVRDGRLPRDFEPTAGYELSQGADLVCFS... | Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1.
Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosph... |
A0A7V1EAG7 | MRTFLAADIDNKVNEKIKDFMDRCRLMDRSVKWGKADTSHVTIYFFGEVEEKNIKVLEGTVSEALKQIVPFEASAARISAFPSMKGPRVFWIGIENRTHELEKIYESIKTDLPGKKIKVNIESKDYTPHLTIGRVKGRCDPETIRRMSACSETEFGSFVIDKIILYQSILRKEGPMYSPLKVFQL | Function: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
EC: 3.1.4.58
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-end 2'-phospho-ribonucleotide-RNA + H(+)
Sequence Length: 185
Sequence Mass (Da): 21269
|
A0A918YSE4 | MDETLSLGRIAGVRVGLHWSVLVIVALVTVALANGRFPAAHPGHSPFAYWALAVLTALVFLVSLLAHELAHAVVARRDGVQVEGITLGMLGGAVRLRGEAPSPAAECRIAGVGPLTSLLTGAALTGLAMGLAALRVSGLVVEAVAWVGAINVLLAVFNALPAAPLDGGRLLRAYLWHRTGDRLRATRGASAAGRVLGWCMVLSGFADVLFAGHLTGLWPALIGWFLITAASGEARQAQILGMLDGVPVRRVMTPHPAPCRRRRRSPTSWPKGPSAATGTLRSRSWRQTVRSPGCSPCGGWRRHHRRSARARRSAR | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 315
Sequence Mass (Da): 33300
Location Topology: Multi-pass membrane protein
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A0A6L7U3N8 | MTFSATGPIPRRVVITGLGALTPMGLSAVETWDNVLAGRSGIGPMTRFDPSEIKSKIAAEVKGFDPLNFMSRKESRSLDTYSRFGVAAVQEAIKDAGLEFSREDIQRVGVTISSCVGGIEDYTNSVKTLLKRGMQRVSPFLVPRMLVDSLASRIAVRYGLQGPTMGVTTACSTGLTALCQAFDQVRFGSVDIAICGSSEAAIVPPMVAGFDAMGVLSANNDMPEEAAKPFDNERDGFVIGEGCGIMIMETLEHARARGARIYAEVAGGGMSNDGNDMVAMEKNGIGIQNAMRVALYHAKQLLGIDASDVDYINPHGSGTK... | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Involved in the type II fatty acid elongation cycle. Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor. Can efficiently catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-AC... |
A0A0W0SMR6 | MGKESTPKSSLHPQLQAFLLLSEDCIIVLDANYRILEFNEASTSLLGWKDKEMLGQPFASIYFQLGHKIPFPFYQYELILQNEHGEFEGMLYKNNTKRYFTWKFKRQSNQIILLGKDNTDTKRLALQNVTIFDQIKKISACVPGNFYWKNKDEEYLGCNKILLKTLGLNSMNDFVGKTDLDLWPEHAEELRKNDQRVIKGKKPVLFEETVTLNGKKMYFTVIKMPLIDDEGNIIGILGNSSDITELKRTQADLKIAKEAAEKASQAKTEFLANMSHDIRTPLTGIIGMTKMLEETARSEEERQYASWVNESGEQLLKLLN... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 798
Sequence Mass (Da): 90084
Location Topology: Multi-pass membrane protein
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A0A1B1YU95 | METVRLVLVTLLLVITFFIYQAWQAQRPQPVQPPSIEQGTLPTPAVSQSAPVPGAPAAAAGPVAPPAARPSGTPVAVSTDVMNVQIDTAGGDITRLDLTAYRAHAGPDAPPYSILDVAPPRLFESQTGLLSAEAGRAPDHQATFTAAANSYQLAPGADTLEVPLSWTDAGSGIEVRKVYRFARGRYDIGLRYEVRNTGSQPWQAQPYTQLMRRKGADAQGSIFMPASFQGAVYYSAADKYRKIGYDDMLKAPLATTLSDGWVGLSEHYFLAAFLLTQGQAQNCYTKALADERFLAGCIAGPLSVEPGQTASWETRLYAGP... | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
W4ERQ8 | MTLNPVTTIVLVSPKGNAEDIFARIKIPYEVEYHHVAIDYPSTTSPLDFTVYCSFVTLWRQFMVEHNKAYISTKRTVSINGEIMSPPTTRQAAYRYLAKLSNRQHIVTTAIAVRYLGQLTMVVVESKVTMKKLSQKIIEHYVETGEPFEHDIGYNIQGLGANLSESIEGDFDNVAGLPIDSLQEHLINKKILDVKEGEIVDVY | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+)
EC: 3.6... |
A0A3B9UHJ9 | MRARGHRAGAARPRHLEFTGTPKLVKKLPYALRGQLVLGSASPRRRELLAVLGIPYSVRTSDADESAPEVLNDVETVRYVARLKAEALVPELSHGEVLLTADTEVWFEGRRFGKPRDLDHAVEMLQTLRGQTHKVITAVCATDGHQWSQAESIAEVTFHRVDDAFIRYYVETFQPLDKAGAYGAQEWFGQLAIERIHGTFDNVKGLPLDTVVEVLGPWLENA | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
A0A972R4H9 | MMKIPFTKAQAALNDFVIVDDREGSIPVEARKAFAREACLRRKGIGGDGVIFIEKNNLVEFTMAFYNPDGTDGSMCGNGGRCAALFAYRKGIAGSEMGFEVMNQYYKALILDDGVRLFFPPPKTIRLNFKLRLRDKTVTAHYVHNGAPHVVVFIDDFESASYLSLDDIPVRSLGQEIRLHGDFRPVGVNANFVSIDTDQHVHIRTFEKGVEAETASCGTGAIAAAIVSHAVRNIEPPVTLHTFGGDCLTVGFRPLSEADRVEIIPFIESDIRSAGIGNDLYLEGPAHLVFEGVTCFDEEHLLLVWPEEDRGQVRSR | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacte... |
A0A9E7E7M5 | MPEPADPLRISDQQQVLQTMETMDEGCRGVGVEECLMRRTLAAHTDYIYTQGNKH | PTM: PSK-alpha is produced by endopeptidase digestion. PSK-beta is produced from PSK-alpha by exopeptidase digestion.
Function: Promotes plant cell differentiation, organogenesis and somatic embryogenesis as well as cell proliferation.
Subcellular Location: Secreted
Sequence Length: 55
Sequence Mass (Da): 6265
|
A0A7V1EAU7 | MRYQVTDLSPADLVIRAALSEDLCVNFGKGLDAFLRGETPDFIDVTTDAVFSAEEKEAHLMAKSSGIISGAVVFKKVYGLIDPGLAVTFYKKDGEGFKKQEKIASLKGRMRSILAGERTALNFLGHLSGIATETGRLTGLLSGTGIRILDTRKTLPGLRELEKTAVVHGGGVNHRMGLYDMVLIKDNHIDGAGSIAGAVNRVRTRHSDKYKIEVECRSLEEVREALSLGVDRIMLDNMTRSTVKKAVKIVNRKTEIEVSGNMNRRRIKKLRKVHVDYISAGCITYAAGNSDFSMKIKPDP | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1.
Function: Involved in the catabolism of quinolinic acid (QA).
EC: 2.4.2.19
Sequence Length: 300
Sequence Mass (Da): 32910
|
A0A9E5XS57 | MKWLAVDYGRKRTGLAETDDLRLVASPLTTVETAGLWSFLDDYLRHNRVERLIVGEPLREDGTHNPLEADIRGFIKKFRKRYPGIAVEREDERYTSKMAFDAMIAGGLGRKKRRDKALVDKISAALILQAYMDRAGR | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 137
Sequence Mass (Da): 15681
|
A0A1I7YCZ6 | MSGKEKSQSTSCDNSHQSQRSKRGKWNSNVQFILTCVGYSVGLGNVWRFPLKAYENGGGAFLIPYLFCSMVIGFPVLFLEMSLGQFTSSGPGTIFRKLCPLMQGIGWGQAAMSFVVSIYYNVIVAWTLLYMGYIVIGKWKTFATCDNDHNTECEWPSSYNDPDTKFLLYRVRANLLVVDGRMLFRNCYSNLQKESIWPDDPVDYQFYYNRQNYSYADTKNVTLSLAVLRKALNHTEPTATAAEEFFNYNILRQSPGMEYVGDFNYKLLIALAIAWLITALCLIKGVKWIGRIALVTATVPYIIICILFFRSVTLEGARKG... | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.33
Subcellular Location: ... |
A0A9E7JLS8 | MGVRVALHLKGVVDYDFLQERLGEKSQLLLESNPVYKKIPVLIHNHNPVCESMIIVEYADEAWAASGRAIRTADPYDRALHRFWAACIDDEVRVAPRRPTFFCLGWSQCPRHHAAAVGSHR | Function: Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
EC: 2.5.1.18
Subcellular Location: Cytoplasm
Sequence Length: 121
Sequence Mass (Da): 13763
|
A0A5C9CXE0 | MIFEAGEIGGMIGAVCKGNLQAKVSSVSLDSRDCGPGALFVALKGERADGHDFALKALENGATCVLAEKDKAHLLLASIPPAMLKDACLVFLDKSLEGLQRLAKEHVRRIKGLLRIGVTGSSGKTTTKECIGAVLRAAYPSDTVAVGKGNLNSDSGLPLALFSLEPFHKAAVFEMGMNRRGEMDELARLFEPDIGVITNIGTAHIGLIGSRMGIAEEKKKIFSRFTGTQKGFVWEDDDFKAFLSLGVKGSVQEFGPRSTQGFEGARSQGLAGWIISWKGLEIAFPLPGKHNLLDALAALSVAHELGLDPAKCALGLSSVK... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-d... |
A0A7C2KJ69 | MFFSIIRRLKSVWFKVFFLRELKIILASSSPRRIELLQEMGIPFDAVHPNVNESIINMDSKQKDVQQVAIDLSMLKALAVARDYPRRLVLGADTLVSVDGEILGKPKDIEDGRRFLKLLSGRKHQVITGISWVYQLKNYSFSEYALTHVYVHRLSDREIEDYLESEAVLDAAGAYKIQGAFFKYIKKLDGFYHNVVGLPMSLVYQSYYRLCGESDKNV | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
K2DVM9 | MFLNLLLQYLLPQHILSRLIAKIANCRIRLIKNLFISQYCKFYRIDMTDMLEPNPLNYQTFNDFFSRALKPGARPVTDDKNVIISPVDGRVLQIGKVSANLLIGAKGKNFTLEQLLADNEDAVRFHNANFAVLYLSPSDYHRIHMPVRGKLCSMRYVPGRLFSVNPNVINQIHDVFARNERVIITFETVLGPMIMVLVGAIIVGSVETTWGGVVMPNSQNSVINWDYTKQEIIFERGAEIGGFKLGSTVILLFPEKTMEWNKLSQDAAIKMGQDLGTAL | PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme... |
A0A7C5MXD4 | MYTFLLVIFIIVILLLIPIILMQSGSGAQSGMLGSDFAFGVFGAKTNEVLVKITKWLIGIFMFLAFILGYIKVKEFNAYKARHVKETEEVNKVESQAASSVSETTSESQTNINLPLQGK | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 119
Sequence Mass (Da): 13138
Location Topology: Multi-pass membrane protein
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A0A9E0ECT3 | MKSANIFKYFILLILSIIFLPALPIFFLIDLSVNLTRKDLCKFLKERYGWLSWIKTYKSFLKSFNNKKDNKLILCLATSAGEIATLEALFEKYSKANFFILTTSITGRNRCCNFASNSKIQYMPIPNFLFTMTIFSLLKPDLFLVVESEFWISYFITSKILNIPIVAVQIRHTMFQKKITELYYYTFIRLCAWIILPEERDAYPDNFPFEKVKFFNTDLKLLKVRVKKANCRKVFCIFASTHKEEEVVFFECINKMIDSFEGIFVIAPRHPQRAKEISDFALKKDLCPIFLSEILDFLTKKVDNIEDTKNNIDNQEFILS... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A9E5XWB7 | MENHLFDFDKILLLGTRSPRRRELIERMDIPYRTIEIPFDESRAGAGTPLEMARAKMDAYKGELSSHEILLTADTMVFAGNRRLEKPRDTRQAMEMLESLSGRSHRVVTGVCMKDVLRQTCFDDTAYVYFRELSREEMCYYIHQYMPLDKAGAYGIQEWIGLTGITRLEGNFYTVMGLPAAKVWEEWLRFNGY | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
A0A6S4QPW5 | MNESNLSVTTSLTFAKRQGPLRPVKINAALLTGNASSSSELSVIRDALDIPALAVLGSKYVANRLIVLGLLSAGTSTFTGIPVNEDIEIALAGIKGLGAKFSYEEQGTILNITGTGGRINSSASALFLGDNGTFSRLVTPIAALSEKPIVLDASSQMKRRPMSPLFESLTTLGATIVRAHKSSLPSFPVTLSGPLQNNDLTLAGSISSQFISALLLVAPYLNALDKTSAARKPFTLKLTSPLVSRGYVHLTRRLMKEFGVIVDHEEHKGLDHFTVKAGQSYLARPYVVEGDVVAASYFWGLSLIKGESLAITNYPQDSFM... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-ph... |
A0A1A3GRT9 | MRRLSGEDNSFLAWESAVQPQHTIKAVVLDPAQGHEPITFEAVRAALPGLVDRVEPLQWQLMSPRFGAGRPWWITRARGDLNYHMKRATAAAPGTDRELGAEIAKLFEEPLDRNRPAWQMWYIDGLADGRVALVLKIHHAVADGMASLNLLEQFYSQDPADRLPEPSARPAPDEHRPPTAEWLPMVARQQVKSLTKFPKVLARTAKVTRTIQNRQKSGKPGYAEAFIPPALPFNEPLTARRGFAFVNVEMDQIKRVSKAFGVSVNDVFLAMCSTVLREYQASRGPVGDDTMTAVVPVSMRPQDGDRWGNKVARWNVELAT... | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 469
Sequence Mass (Da): 52163
|
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