ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
U5L0N4 | LLKSLPVGVGQIYGCDDPWTGGIFLGAILLSSPLMCLHAAIGSLLGMAAGLSLSAPFENIYFGLWGFNSSLTCIAIGGMFMALTWQTHLLALAC | Catalytic Activity: urea(in) = urea(out)
Subcellular Location: Cell membrane
Sequence Length: 94
Sequence Mass (Da): 9792
Location Topology: Multi-pass membrane protein
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A0A316US15 | MSSWWGSDPFVDLVAKATSELLPAGQEDIALNLEICDKVRAKQVPPKAAMQAIKKRISDANPNVVLLALGLTDICIKNGGDHFLEEVASREFMDNLTSILKRPAGVNHDVKAKALRLIQDWAQVAEAKPAQMGYITQVYRSLKLEGFDFPATSGQASAAFVETLTAPEWVDGDVCMRCRTAFTTFNRKHHCRNCGNVFCQQCSSHNMSLPWYGVGQDVRVCDGCFNKRAPPKIPAGGNKLQRSSTTTVVPTGRGGAAAQRSNTTGAKASSSRRNKREDDDLALAIKLSLQDAPSGSRAGAASYSEPSQPRATRQPNGRML... | Function: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane.
Subcellular Location: Endosome membrane
Sequence Length: 787
Sequence Mass (Da): 84055
Location Topology: Peripheral membrane protein... |
A0A316UUZ1 | MNRARSQTHQFPWLTDSGEGTTGASRSPGAPDWRRILYREQSSYPDNYLPPQAWLTRRQKTRLEAPPTHLGILIALLPLVQGLNVILVFLAVFQRLEQGKLFPVVLTAQCFAALAVASLVGWLHRRRWSSQDSAHQIRSASPARASSPSLIISFGIVLLLLYALSPVLKTLTEATSGDTIYPLAFLLFALHIALADNTLPSPPSRTAKERRAVESRSQELAGQDVGKEQESRKKQRKANSSARSPTDLSSALSLNAATSASLVLASRLPSNEHVFALLFLAVLCFGLLPRVTSWLLLGYAAPRDEPRRTRAPPLLLVIWS... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Membrane
Sequence Length: 394
Sequence Mass (Da): 43288
Location Topology: Multi-pass membrane protein
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A0A524HWN5 | MTDTTDKTRRHRTILQLLAATPIASQDDLAAKLAAGGIRVTQSTLSRDLKELRVTRVSTGVSYRYLPSGGNGGPHTATPPEELRRLAASEVTGIDANEVAVAVHTLSGRAQGVAVYIDSLAIPEILATLAGDDTVIVYPNRIKQTARLRQRLASLLSVA | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 159
Sequence Mass (Da): 16924
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A0A1F5VKP2 | MKFSIIKSIAQKDILLEYRSREALNSVIFFSLLVLAIASFALEPGSEAIKELSGGVLWISYFFSGMIILNRSFALEQDENAIQSLLLAPIKKSHIFWGKFVTNFIYIVFIEIIIFLIFVIFFNLQFHTKMIVLWLYIILIDAGFISVGTLFAAMLIRSKTREMLLPILLFPVSIPLVIASVKATSYLIQNVSYVYIIPYFKIIIAFDLIYMFAVSLLAEFVIGE | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 224
Sequence Mass (Da): 25565
Location Topology: Multi-pass membrane protein
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A0A1H0P7N7 | MFGIVEAITPVIGWAAGVAASGFVQAIDHWIAFGLLGAVGFRMLYAAMSRKAQTEERVGNSAYMLLATAVGTSLDAMAVGVSLAFLNVNILVIALAIGIATFLMSSGGMLIGRLIGERFGRAAEVVAGFALIILGSSILIEHLTA | Function: Probably functions as a manganese efflux pump.
Subcellular Location: Cell membrane
Sequence Length: 145
Sequence Mass (Da): 14957
Location Topology: Multi-pass membrane protein
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A0A103Y5Y6 | MPNFTRKMLITPLQKSHFLLLDCDALPPPPPPPPPPLRHSSLSPLIVIMLCTAATTFSFLCYILIIKACRTFQKRFRTRTHGRNINTNETHQDFVDREHGSIVFHPIWLINTIGLDQSVIDSLGVSVYKKGHGFINSDCAVCLGEFQDEENLRILPQCNHAFHVFCIDTWLRSHKNCPVCRASVTNNTKIELNPIESNSQEEIPIGDLRNETQEIDKCLFGGIRVQSDLIDHRRRQEPEPEPETMRRSVSMNMIQLSAGNGDQEPKKANMLQKTTENRSFQIRGDIKSESL | 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: ... |
A0A316UUL5 | MDEIRKVPPITRFLIGSTLVTSLPCILSLLNPYHLLLWYPAILRNYEIWRPLTCFFLTGLGQNGGLQMVFDLFLLGRNTLDLETSGQGFARRTSQFAWALLMMGFVILGTNYPLGSTVLFNPMLSALNYLWARHNPNARVSLFGLVTLPANLLPYAYLGFDVLRGGLPLAMQSATGLLAGHAWWVLAEAAQGDHPGGAARRLATPPGWLQALLPDSVAPEDVAAQAARDAPGGAGGRVASRAWGGTAFAPRGRNFGDGQGVGAWASGGGAAGQTIGGSGVGAATRGGSSWLPSFLGGGGGGGSTASTSTSATPAHRRDAL... | Function: May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 459
Sequence Mass (Da): 46845
Location Topology: Multi-pass membrane protein
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A0A7S4BTC3 | EAAHPGRWAGRKSKAEPAAVAEEKKTEPSTACPVKSGVVVGDDLLALFKWAKEQSFAIPAVNYVASSSVNAVLESAAKSENPVIVQVSQGCGAFYCGKGIKDDGYKATIAGSIALAKHVRAVAPMYDVPVVIHSDHCAKNWSTRRTLRPAKST | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
Function: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeoge... |
A0A7C9E9Q6 | MGNLPIILVPAMCKERSSPFGAPEVCEKYGLAYASLSMAIGGVYLWLYVYNIVRISSTEAGLIPDSKDSNIDAQEPLLLTSVDQLSSSSKSGNSMSHRISRFFKGLSKKINLKAVFAPSTIGAIIGFAVGIIAPLRHLLIGTGA | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Subcellular Location: Membrane
Sequence Length: 144
Sequence Mass (Da): 15303
Location Topology: Multi-pass me... |
A0A7S4BGH9 | MAAVRWMVIMAALYHSAVLAAMCRPTEFLQLVPHLTPQVQSVLQDRGISSPTPIQRAALPRVLNGESVVLHAETGSGKSLAFLLPAILRLGEGEKMLVVAPTRELAVQLANEAAGLVTDPSEVQIIAIGATPLPQALLDARVICCTAPEMVALIDLSAETEGVLTEVLSRLRVVVLDELDSLLPIETVYGPRAAERKRSANKQRPEPPAQQLLRAVFESNMEPQLQLVAASATVSRPSRLKLERVLRRDPLGRWFTSSLPIVRPAEIANLDLSTISRAVVIPSGVRHYYVRMPARVPSAGGGNAASRLAASGKGRVTLKQ... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 618
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): 66117
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A0A7C9ASL8 | MESFDAGNSKDGQIVVEEHNLVRILVLNRPKHLNALSPYMVSRLLKLFFAYKNDPNVELIILKGNGRAFCAGGDISAVVQDIKKDWRSGANFLRKQYGLYYV | Pathway: Amino-acid degradation; L-valine degradation.
Function: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism.
EC: 3.1.2.4
Catalytic Activity: 3-hydroxy-2-methylpropanoyl-CoA + H... |
A0A1E3QIR0 | MSLKFRGASEAIDEQVETIIAKTSGLDIGEGLDEVEPEPYYYDGMNEDTEYELALLAAQTNYSKLFIPLLIFLASFLVRAYKIGLSKLVVWDEAHFGKFGAYYLKREFYFDVHPPLGKMLVAFSGWLANFSGEFEFDSGSSFPDHVDFRSMRLFQAVVGGLVPMFAYLTMENLQLASGKWASWLVVIMTCFETLSVQLSKFVLLDALLLAFTVSTFFCMTQVHRLRASGKEFTFSWYAWLVLSGVSIGCVCSVKWVGLFVTATYGCYVLYDLGRKHFDLGLSRARYYSHWAIRVATLIVIPLVVYLISFKLHFMILNKSG... | 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... |
A0A6P7GEE6 | MTHTHIFAGNSAPTSYVSNVFIGFSTSMTFWGRSFNTLMYMFETTFNYFVADPMQEAVKKKYFPNYPDLDSINKNISLFLINNHESINSPIPSVPNMINILGFHLKEENTLPKNLQDYIDSAHEGVILFSFGSFVNPSQLSPRVKQAFVKALGKLKQKVLWKSDEDSFLGKPNNIKLSKWLPQEDILAHPNCKLFITHAGFLSTIETIYHGVPVLTFPLTGDQDLNAFRAVEIDMGHTAVLRDITEEKLDYFLDQLLHNDK | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 261
Sequence Mass (Da): 29714
Location Topology: Single-pass membrane protein
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A0A118JSB9 | MSTSSSFYGNGITLGSSTPTFKNLLSSRHPNQIQVSSYPFAFLPLRLSKTSIFVRKRPNLITASALTTPESPLKSSFRDKNPKEINVLVVGSTGYIGNFVVKELVHRGFNVIAVCRENSGIRGRNSKEETLNKLNGANVCFSDVTQLDLLQKSLQNLGVSIDVVVSCLASRSGGVKDSWKIDYEATKNSLLAGRKFGAQHFVLLSAICVQKPLLEFQRAKLKFESELVKEAEEDDGFSYSIVRPTAFFKSLGGQVELVKDGKPYVMFGDGKLCACKPISEPDLASFIADCVCGEDAELREGYIGRILQEGSGGRDEWARA... | Pathway: Porphyrin-containing compound metabolism; chlorophyll biosynthesis.
Catalytic Activity: NADP(+) + protochlorophyllide a = 3,8-divinyl protochlorophyllide a + H(+) + NADPH
EC: 1.3.1.75
Subcellular Location: Plastid
Sequence Length: 914
Sequence Mass (Da): 100395
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A0A1X0RSP6 | MTNERKRSPIESDEPSKRVKTLMGHDHISSSSSSSSSNSDNSSSRISISSSSHSSHNRVNQQEEESFNNDNNNNETIDNSCSNHDDDKARREIPPPQIIDTPEPNVNKLIYGKYEIEAWYYSPYPTEFGSKIDRLYVCEYCLRYMNKETQLESHKAICKEKKPPGRMIYANGKIKVYEVDGQEHKLYCQSLCLLAKLFLDNKTLYYDVEGFKFYVLAEQNSKFKSYEELIGFFSKEKLSYDNYNLACIMTLPSHQRKGFGTLLIELSYELSKHEGKVGSPEKPLSYLGALGYQSYWASAILATLLHFRGDVTIEQISKET... | Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
EC: 2.3.1.48
Subcellular Location: Nucleus
Sequence Length: 379
Sequence Mass (Da): 43827
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A0A7J4UTW7 | MKKQKSSGGLQSSAGLVRYFDAESKNAIHMDPKTALAICIVFGLGILVLNWTI | Function: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex.
Subcellular Location: Cell membrane
Sequence Length: 53
Sequence Mass (Da): 5723
Location Topology: Single-pass membrane protein
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A0A1D1ZHD7 | GGDFSIQVLQKALEVWDLHVIPLDAPVAEPTKHDPEMENAYICHLQDHWFCIRKVNGEWYNFNSLYAVPEHLTKFYLSAYLDSLKSGGWSIFLVRGNFPKECPISSSEASNGFGQWLTPEDAEKIIKACNQKRVDSQKGEVLRSSNPIDYASDGDEISVQEAADLNAAIEASLMDSAAYNADDGLSQYKSSLVGSTLIGGVSGSPLDSSVGAEFDKCKGSSSETDPYLALGQQSIPPTSKWTLKPCNQKEVATCRSNTSVPSSPAQPAGTEVAGYEEDEASLLNAAVQASLVNPAAFSSKDACTKQGESTCKEFSGAGAE... | Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
EC: 3.4.19.12
Subcellular Location: Nucleus
Sequence Length: 359
Sequence Mass (Da): 38678
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A0A1D1XD15 | MYSFVLVYIFPSYSLQINLSVAPASADPYGFWSACKKNHAHCNADEMTVLQGLRNQVLKAVGSFSMSRQNGLFINSCFTHCQSESQTTWFAENSPALGNTRIAVAVGDWFFDRSAFKARDCAYPCDKTCHHSN | Function: Hydrolyzes acetyl esters in homogalacturonan regions of pectin. In type I primary cell wall, galacturonic acid residues of pectin can be acetylated at the O-2 and O-3 positions. Decreasing the degree of acetylation of pectin gels in vitro alters their physical properties.
EC: 3.1.1.-
Subcellular Location: Sec... |
D8U4E7 | NQSMSFQDLGLDPRLLRALGKRGFTKPTPVQLEAIPRTLEGKDVVARARTGSGKTMAYLLPLLHKLLSTDNISGSFRAIVLVPTRELCQQVGLLSFRPPAPPTTNVRDSQHPLHSPPSTHDSMRVPRSCQCILMSATVSEEVERLQKLVLHNPITLNLAGGPGGTGAPGAAEGGGEGRGGLASGSGVSADIQHFYIQCPRPDKLLHVLALLRLGLVPKKVLIFVNTVYEGVRLRLFLEAFGVRPALLNSELPLNSRSHILASFNKGLFDYLIATDDDAAAGGKKGRKKQKVLLGKAGKAARGGENGGARKDAEFGVTRGI... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 358
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): 38265
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A0A316V3S7 | MPSSAEASSSRSPPTSPKRAPVPRSISYGSSTRSPPSSSRPLNPPQYSYAGDGEGAHASSSYNASGSLATRTRSRSVGSKSRDAAVVPLEEHAQIGHALDRGPGTPDFTLGAAAAAGSPSSSPTRNPTKGKGRLQDIMRDGGDGGGPSAPVPETARRPRLTTRLRSFFTSSPDTSTPLADSDAGPPKARTSNEYERNNGAPLLRPSPLVVPSARQAGIQPFGLHGLNDDSPPLTPTSDEGYEGRAKGHGKWPSWAPQGNSSSEQMLTPPLTASMPATSRTDSPALYASSAMSLGTGGALASDGLLPRNIASHGVSTTPRR... | Function: Golgi membrane protein involved in vesicular trafficking and spindle migration.
Subcellular Location: Membrane
Sequence Length: 965
Sequence Mass (Da): 101339
Location Topology: Multi-pass membrane protein
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A0A2W5JH53 | MSASAGPRLHGYRLPAATMANLRATTTATVADDAFRALMRMRRQPALRIAPSFPDHPAYIRALADSVRQALAGLERPPQMLLASFHGLPRSYVEKGDPYLAECERTMRALRRALGLSEAEFP | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
EC: 4.98.1.1
Subcellular Location: Cytoplasm
Sequence Length: 122
Sequ... |
A0A1E3QQJ7 | MKLAHLAKITGLFLLVKVSQTLILINVPTRFDTSSQIIFGNAVVQQHKETSILLQLSQPFLQILSELLPKLVTWDTVYLSSFFANGLKYEHEFVFAPLWWRLIKSLPEIIPGTLPSVNFYDQLLIGTLVANASHYLACLVLYGLTNLVFSSNTLKARSESHNVALRAAMLYAISPAGIFLTAPYAESICALSSFVALYLREVSFDRRFLMKPTLKSAPLFQAAYILSGAFVATAFGFRSNAVLLGYLYLSDLYVFLRARSYKSALIPLLAGSQLFAAVLYLGYLPYSLLCPQRGEWCLNTVPSLFTHAQARWSNGFLSYW... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 433
Sequence Mass (Da): 48192
Location Topology: Multi-pass me... |
A0A2P4T8R0 | QAGYRAPSSSRAAASPSSAAPRSGGPGDESERSAGGLPAPSGLRPGREDVMVGDDPYSPYKYTDDNPYYNYYDTYERPRQGSRYRPGYGTGYFQYGLPDLVPDPYYIQASTYVQRMSMYNLRCAAEENCLAR | PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.
Function: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (a... |
H6N6W7 | MENKLKVVLEISKNSRLKYEVDKESGKLVLDRVLFGSNVYPQNYGYIEKTLDHDGDPLDVLIISNESLLPGSVIPTRILGAMKMIDSGDRDTKLIGVVDVDVRYKSFQKLADIPEALLNEIKDFFSNYKKLENKEVEVQEFVDLEEAMKILAECKDLFKKSHY | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
EC: 3.6.1.1
Subcellular Location: Cytoplasm
Sequence Length: 163
Sequence Mass (Da): 18676
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A0A7U8PFR1 | MRLTLSRWKASATTCLSAVMDHPRFREGALTTAFIAEEYPDGFSGVKCSEDDARTLAAVAAEINLVAQRRDTQISGRLSPQKHSIANDWVVTLDGYSLPVRIAEGEGGTTINFIDGGSLPIASDWHPGSQLGSFTVGGKPIAVKVSRSGTGWRLRWRGMDVVAHVRKPRVAELAKLMPVKLPPDTSKMLLCPMPGVITSILVKDGETVEAGQPLATVEAMKMENVLRAERRATVKRITAEAGSSLAVDELIMEFE | Pathway: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3.
EC: 6.4.1.3
Catalytic Activity: ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-CoA + ADP + H(+) + phosphate
Sequence Length: 255
Sequence Mass (Da): 27584
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A0A261B2K5 | MRLLLLFSFTILLSSAFFTIPAYDSGILEILIESEAPIHAGFVVTYKNKSHVTWRHLKPNIPELLIFEGFDLFPGMNQALMNVTIHDNITSNSVVFQPANKPVYDINKLPLPYTGLQMKFKCAEDWYGILCHQHCFVKNERWRCDENGNPACAQGYCGWNCLKSGSDCPVFANCSCQNGGECYNPLSESSTKCHCPAGYLGDDCGFFHIIESKLDLMTNFGANLTVQNKFSNRADIYQLFEKNDEKLRASRHQDAQKYQSFETFAAICVLIWLVATTGYCIIKCCGKSEKDEKKIVETFGDEKKKTSEEEKKCILIEMNN... | Function: Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Location: Membrane
Sequence Length: 321
Sequence Mass (Da): 36415
Location Topology: Single-pass type I membrane protein
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A0A8H6YIF0 | MVCTDAAGMGCNIPNIDVVVQWKLPASVSIFVQRAGRAARLHGRTGVAILLVEPSAYAVDLFEELAKEQTGQGKKKRQAKEKETDAEKRKRAQEKKTYAKSRGLLRGAADVEHDEILVKDTPLLDPEAANEGLYVLVQAGTCRRAILTKIYNNASAAPTVACCDICCPELLNVARPGNPQKVIRQSAVKRGEVVKDLQVVLNEWRTSIKKRDYPSPLFAASAILRDETIALLSSVGPIKSRKHLQKVLAGQWTWW | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 255
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): 28081
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A0A524ITV7 | LAGADSAEFEPTAPHRVISLLDSQLKVTDKGGTMRLGAYPCRLEPESRVREFYGESKVSERHRHRYELNNDYRDRLTEAGIRLSGTSPDGGLVEIIEISNHPFFIATQFHPELKSRPTRPHPLFAAFIGAAIQRRDARGTHSRESSESAELIERQPAGKQ | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2.
EC: 6.3.4.2
Catalytic Activity: ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate
Sequence Length: 160
Sequence Mass (Da): 17963
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A0A7W1PLL0 | MSTDLSLPDALIIGYFALLGAVLGSFLNVCILRWGVEPKQSVMYPPSRCPSCGHAIRWYENIPVVSWLVLRARCSGCGVRISALYPAIEVTTALLWAGSVALLGLGVPAVKLAVAATLLLGIAVSDARAFIIPHELSLGGTAIALAFAAWPESGGVPDAIRGALFGAGLVLLVGEITELVLGQEAMGGGDCALMGMIGAFFGWESVWPVVALGAFISILLHVAAALRRSAPAVEGTGGAPSPGLRWGKLIQLLAGGLVLMGLVGVAARAGVMGSLLRTAFSGVVGAGAAYYVSFLLPRRMPIGPLTQVWGLIGAAIGIAI... | Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to rel... |
A0A524KTR5 | MTALTISRDGTTAVLTLDLPGEPVNKLNAQVKTEFEAALTDLRDDPAVRALVIISGKPDTFIAGADIEEFTRLSTQEEFTRLSREGQEMLQRLDDFPKPVVCAIHGACLGGGFELALACDWRIATDHPKTQLGLPEVQLGLLPGAGGCQRLPRLIGLSAALSIIMPGKTEAGSKAFRLGMVDELVPKSILLDAALKAADRLVGTGVPVRPTRGGLMGAIFDRTGLGRRFVYWKARKDTLAKTGGRYPAPIAALEAVRAGLEQDGSAGYAVEHRLFGELAATDVSRKLIGIFFATNALKKDDGLPPGGTTAKPRTIERLGV... | 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: 563
Sequence Mass (Da): 59968
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A0A1S2ZKF8 | MAPGNASLVTEFILVGLAELPDTQLSLFFFFLVVYMVTVLGNLSLITLIGLNSHLHTPMYFFLFNLSTIDLCYSTVFTPKMLNHLIFKKNIISYHGCMTQLFFFCFFGISEGYVLTVMAYDRYVAICNPLMYNSVMSPKVCSSLMFGSYLVAFSGAVAHTGCMLRLTFCDADTINHYLCDILPLLQLSCTSTYVNEMVVFVVVGINITVPSVTIFVSYGFIISSILRISSKEGRAKVSL | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 239
Sequence Mass (Da): 26619
Location Topology: Multi-pass membrane protein
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A0A7C9EW97 | MGLLHLFLAASMAVVKVFLVVSVGFFLALDRVDVLGSTACKLMNKVVFFVFCPSLVGSSLAKTITVKGFLTLWFMPVNIFFTFIFGSVLGWILVKITRTPKHLKGLIIGSCSGGNLGFIVVIIIPAICKEKASPLGAPDVCQTYGLSYSLLSLAFGSVFLWVYVYNIVRIYSKEIVERTAAVDVPPGANDVESNINGDHISVISTEPQLPSLDNPPMSPVT | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Subcellular Location: Membrane
Sequence Length: 221
Sequence Mass (Da): 23849
Location Topology: Multi-pass me... |
A0A1S3A8P2 | NQRVTAMNITDKMEQLYQPYTFEQTLDISPFLEQYWSSSFLITGVYLLLIVVGQNFMKSRKSFDLQVPLTLWSFFLAVFSIVGTLRTWGYMGMLILMDGPKHTLCFTIFCKNTVISFWSSLFLLSKVIELGDTVFIILRKRPLIFVHWYHHSTVLLYTSFAFKIKMPSGGLFMAMNFGVHAIMYTYYTLKAAKVECPRKFSMLVTSLQILQMVLGTIFSILAYIWRQDFGCHTTEKDLLWSMTLYVTYFILFAKFFLETYILPKVKDKTKIQ | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 272
Sequence Mass (Da): 31848
Location Topology: Multi-pass membrane protein
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A0A6P7G2K7 | MMEKKLPVKEMPARKDTELLDLAFKVGKLVGLYPQTFENNFRFKFHIFLYGIFTAFIIAFDLYNDVLDVLYPEERGNGIAVIVLTSLVVWYTQIINFLNLFKRQTWSSLFTKLSTLDSNLGIYPINDKRRILTIICAVLFCSGYTAYEIFLCWPASNDYSYNLMLLFTSLVISFNMFLVIFTFHQVTTVIERRIKMIKQIVKHSVHTKTLTLTFVKIKMNYSIVYDLVNDLNDIFGYYILTIVFNFFYYSLDYFNVSMRYVLHDDNSNGMFVSYGPHLAVLLIYIVNVAFSSDKISRAADNLIKTCFLLHPDVQDQVLTE... | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 369
Sequence Mass (Da): 42967
Location Topology: Multi-pass membrane protein
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A0A1D1XVI8 | MRRSFVYIAALSWQIFLLLLFAIVSAQEAGERSFVITDMKLAVTTSDSVRKLTESITYPSSLDKPIELAQGDNLKVIFSIHDKETKKGIQPHQSMLILSSKQAGIQIPIIVTVREKGKARAELNMKSAPKDLLSSPGNYSLSLIIGTFSHNNPINYHIGTVIIDIPYTPSVPVPVKYGPKPEIYHTFKPDQKLPSIYISYTFMMIVLSPWLFLIGAWIHLGVNVSFLTSEPGSLPAIISFLFTLLAIEILFYNYWIHLNIFQTLSWLSGLSILAFLLGQKALSDVQGWRLKGLR | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus m... |
W3WWE1 | MKLSTILSAGLLAVYASATPIVTTGTSYNIPDGVSIQEMVARGEDNLVRRQANDTGDSSFTANDFLDAGCKDVVLVYARGSTQDGNIGDQPGPQLASSLQTSLGADRVAVQGVDYPAGLAQNLIPGGTNPDDAADMADLIANISSTCPDSQIVLSGYSQGAAMVHRATEQIDDETVLGQIAAAVTFGDTQKDQDDDQVPNVDTAKTLILCNDGDLVCDGTLIVTKAHLDYTGKVQQASDFVTGLIQ | Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle.
Catalytic Activity: cutin + H2O = cutin monomers.
EC: 3.1.1.74
Subcellular Location: Secreted
Sequence Length: 246
Sequence Mass (Da): 2555... |
A0A1D1Z6E6 | QKMKNIQNILSLFFLTVLLFAPLLAFGAENEEVKVFQSPNTVEITGGFPGNPFSQIVNGQKNTVKFTFDNKGQSNYTIDLITGELVNKDDPSEIYRNLTGYRYNVAAPSMDNIDIIYNFYAEYPPQELGLLLYVFFTDENSKRYRGVGFNGTVTVVEPEGSIFDLQAIFMYLILIGFFSGIGYLIFQTFFGGTKTKKGKKRVVKPEDNAAESSDKIDESWIPEHHLKPQTRSSARLKKRNEAKKD | Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facil... |
A0A2N5YZS6 | MYLKEEECKIEQVRIFGDFFSKRPMSEIEEKLIGCNLRKKSVISALSSLDFNNYMSGIELEEFAATFEKND | Pathway: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
EC: 6.3.1.20
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+)
Sequence Length: 71
Sequence M... |
A0A1E3QQT8 | MKPKTLTKTSVFPFWLCNYNLLSGFLWGLLLIQTSYLQFKPLGGQPRLFQATYSNLLVIETLALVELYNAAAGIVKSSVFTTFIQLYARFSIIWGLLYPFSDSDFNNSTSCYYYMVVAWSVTEVIRYNYYAANMIFQGEPGKVLTWLRYNTFLVMYPLGLFCEVSILLGNFPDFVAALGGSRAAELFFYTLLLLYIPGFSLLYGHMLKQRKKIMRKF | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzy... |
A0A1D1Z6F3 | MAVLAPLSFLFFSLCLSIRGSSAEEGHATFYGGGDASGTMGGACGYGNLYSQGYGTNTAALSTALFNDGLSCGSCYELSCNDDPRWCLPGSIIVTATNFCPPNFALANDNGGWCNPPLQHFDLAEPAFLQIAQYRAGIVPVSYR | Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found.
Subcellular Location: Secreted
Sequence Length: 144
Sequence Mass (Da): 15128
Location Topology: Peripheral membrane protein
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A0A6P7HF91 | MTINHNKPRTGGVESLYGKMIETCLFKCINRFDGCRELLTYSQVLDHEKVCVGKIHKCPICNEEVTSFLMVRHFISNHKDAILDCPAFVFNMNNYLEMPGTYLYQEEDNLFFLYISYSQSENAIRLELVYMGSDKMATSITHQFTVTSENKEFDINLNSKPSRANEVSVVDASNMSHLINVKFKLFFQNVQFFTISENVHSSSIQNSSSGIENSSEKPKPNQWKLQFCDKSPLDYTTKIVEFPSEYNPQCFN | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 252
Sequence Mass (Da): 29052
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A0A2M9W5X5 | MVHKMEKSTLKLKFRELLQAANFTSQNEIVNYLIEQGYEKVNQSKVSRMLTKFGAIRRRNAKGDLVYSIPTELNVLKISSNINNFIQSVNYNNILVVVNTSPGAAPLVARMLDSFGKAEGIMGTIAGDDTIFIAPCLDITVNALFMNINNLLDIEVR | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis [regulation].
Function: Regulates arginine biosynthesis genes.
Subcellular Location: Cytoplasm
Sequence Length: 157
Sequence Mass (Da): 17510
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A0A1F5VHF7 | MLKEITIAHSSDADDAFMFYALSSNKVPSGNLIIHHHITEIEELNREAFTERYEITAISFHSFSKVMDKYDLMPCGASFGLEYGPIVVAREPHTPDQLKNILIAVPGCGTSAFLILSHYLGDFTYEITAFDTILPNVINGKYEAGLIIHEGQITYTEHHLHNVXXXGALWFRDTHLPLPLGGLAIRKNLAIEDKIFLVELIKESLAYSLNNFDEAFLYASKYSRNAPAETIKKFIKMYVNDLTMDYGEQGIQALKIFSQKFQLPDISQSLITL | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Function: Catalyzes the conversion of cyclic dehypoxanthine futalosine (cyclic DHFL) into 1,4-dihydroxy-6-naphthoate, a step in the biosynthesis of menaquinone (MK, vitamin K2).
EC: 4.1.-.-
Sequence Length: 273
Sequence Mass (Da): 30800
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A0A7Y2JUS9 | MTNPLVELGRIGQSVWYDFITRDLMASGKLHRLIEQDGLSGMTSNPTIFEQAISSSSDYDADIRRLATAGHSAEDIFVALTVADVRAACDAFRPVYDATGGVDGLV | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic... |
A0A7W9KPT8 | MSVTPLAPYHFPGKAQRTRCVTIGSSDSSAGAGIQGDLKAFSSVGAYGASVVVGVTAQNTTGVSASAAIDPKLVESQLKAVLDDVGADGVKVGTSWNAPLVWTLVDRLVWLDDIPVVVDPVMETAAGSALGGSEESVVAIREGLLPLAWVVTPNVREARRITRLDEDAPPEQLAEELVQLGAQAALITDAFPDDPEVCDWLFDGEKHHEIRGPRASTRCDHGAGCAHSALLTVFLARGVDLVGAAHQAHEAVSLAIQRGAADIGAGRHPVDLLAGSVDW | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3.
Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Catalytic Activity: 4-amino-2-meth... |
A0A1E3QPN6 | MKFESRTLDVGYPIYGAGFISDAMLAVAGGGGEGAHGIPNKLSAVTIDFSADEPLKVQSEVKLSDEEDSAMSLAAGGDTVLLGVNQSSKSITRGENKHVRMYSYTKDQWVFGLALQVSESKDSSEYQKHTVVSLDGVYAAICMSDESGIVTFLKSTERGFTKTYEYKAESDVKDISFGPDGKSVAIVTSKTLTIVAASIGKPTFKLENFGKDSLTKVRFIDDEMLLVGASAKNNGGVLLFQISIPQESVLRRLVVSKKVRGLTSMAVSLDEGLVAFSGSDSSVFLLDVTTLRTIHLFKTVHAFAITKVVFSPSGQYLAST... | Function: Guanine nucleotide-exchange factor (GEF) required for the formation or budding of transport vesicles from the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 326
Sequence Mass (Da): 34849
Location Topology: Single-pass type II membrane protein
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A0A645AWP1 | MKKIFLLTLLLGLFNTGLVGQTKTDIFDQLQENVWYLPTSDASTRLYITSIGVGDTIVTLHGGPGNDFNYLVDALKENSEKNTFILFDQRGSLLSPVADSLIASLTLDVIVEDLETLRKSLNQDKMLLFGHSFGSLAVMFYYMKYPEHVKGIILSATMPPYINEDKPFNEILKEIHKRCLDLRNRPEITTELVKADLMDDSVLTPRQRSDKFKILGLASFNMINIANWKKFQGGRIYYNSLVDNAIGGSIPNTYDIRSTLNTYPIPITIIQGEKDYIDPSAYYWTSVFSDYEFVKLIVVKNASHYIWLDDKLKFDESLRS... | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 327
Sequence Mass (Da): 37312
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A0A261AU50 | MTELSKNEGSGKSGKGVSEVVDTVLYYVVDLKKQPPMAQLGVGAGFGTVTGYFVTKGGRLVAATVGISFLLAQFAIHKGYITLNESKIERDIKNLQKVSKRDTINIPSSFITENRWILGGFAAGMLIGFSKNYIMGSSQSTPKVQDKVLNDTDRIRQAQHNMAAAGGGSQCPLTPEQQQKHQAVSGESCGSASGGCPVGADKGGINPLNNELEHPNQKPAPDQPFPLPTKRVQSTIPKAGTEKDTWVYPSPQMFWNAMLKKGWRWQDDGLSQKDMENIISIHNANNEEAWKEVLKWENLLHPECAEPKLKSFKGDAKNIS... | Catalytic Activity: holo-[cytochrome c] = apo-[cytochrome c] + heme b
EC: 4.4.1.17
Subcellular Location: Membrane
Sequence Length: 785
Sequence Mass (Da): 87953
Location Topology: Multi-pass membrane protein
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A0A0C9TWY2 | MDPQMMFGFKAFSALLLAVPAFAHVRMTSISVNGGAPVTDSVRLPPSNSPVTDVTSDDLICNVNGANPMPGITSIPAGATIGAQWDQGAHPGPNLVYMAKVDNATTSTITGLSWTKISQQGIVNSALVANAGGWSSPLPTGLYEFTIPSEIPSGQYLLRVETIGLHVASTYPGAQFYIGCVQIQVTNGGSGTPTGVSFPGAYAGSDPGITIDIYYPVPTTYTFPGGPVWPDGSTQNDNDAGDWSS | 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... |
A0A0F3IPA8 | MPLHRSRPWALPESAATPESLFLNRRSLLQVMGTLPLLAGAGALIAGEATAAGYPYPRSSVYPPERAETPEKLATTYNNFYEFGTSKSVASAAEALKPSPWKVTFDGMVEKPQSFDAEELIARMPLEERVYRLRCVEAWSAVIPWTGFPLAALVKLAQPTAGAKYVRFETFLDSGMAFGQRQFWQPWPYVEGVTISEAMNDLAFIATGAYGKPLPKQMGAPIRLVLPWKYGFKSIKSIVKVTFTDKRPVSYWEQLQASEYGFWANVNPAVAHPRWSQASERTLTGERIPTQLFNGYGPWVADLYKGLEAEKLYM | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Cofactor: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O... |
A0A7C9AXJ0 | MATIRRAYFIVLLVAIALLWSEMAPRRASAGQAMVKRSAWKRIMKVDKSGKGGYVKIQDAIDAVPSNNIDPVFIRVEPGVYKEKITVPSDKPFITLSGWKANTTIITWDDSGDIFKSPTVSVLASDFVGRYLTVQNEHGSGAKAVALRVAGDRAAFYACRILS | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) ... |
A0A316UNA6 | TTISPYPPGPEQWPGVLRNIVPNSFYEASLQAWVPIVFSIVYYIVAHGANHAFFFSQKSKDLTKANSPLAALLRWGIVAHNAFLAVYSGWTFYHVVPVVMRFFYVGARAAGLDGVKLSLCSMPTNTVTLAPYAWLFYISKYYEVVDSIILVLKGKKVSNLQSYHHAGALLAMWIAYRYQSQAVWVFVAFNSGVHTAMYSYYFCSTMKLPFPRTLKRNLTTLQIAQITSGVVLTNLYWITKLDPTRVAAGLVKLGFRSSTGSASASDASWAAGSELLTLATARAAKVGRHSDQCLESSGASLALHFNTAYLVPLVVLFARF... | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 326
Sequence Mass (Da): 36089
Location Topology: Multi-pass membrane protein
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A0A3G3M3T6 | LSFWLGPVALLFMTMSMLIGLGAGTGWTVYPPLSNSVYHFGGSVDFAIFSLHVAGVSSILGGINFITTCMKGKVSYVMSFEFLTLFVWAMIVTSFLLVLSLPVLAGGITMLLLDRNFGSSFFDPSGWGNPILYQHLFWF | 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... |
A0A7C9EGL0 | TELSKWIFHERGHLKAVKIRHHKVGETDEPSIYRINDELEFSVEIYEWAGTSWEPYVGDDVQLQFFMMSPYVLKTLANDKKGLYSTSFRVPDVYGVFQFKIEYQRLGYSSLS | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus m... |
A0A7C9ERR3 | LSFVWLGLLPFLPIQGLRESAMATQSRLGNAIAFSLLVSLLILALSTFVASNQDLQIASAERRIDLSSHIVKVFLTLKVENTGTTPASEVLLAFPPTQVDHLALLKAALVAGRKKKRTYTSLDVKSKLPDGPNGTKYFSITLLHPLIVGEAVTLEVLYILTHSLEPFPLEISQSESQLVYYRDTAIILSPYHIKQQTTFIRTPTTKVESFTNVEPTSRTGLELKYGPYTDQPPHSFSPIIVHFENNKPFAVVEELVREVEISHWGSIQVREHYKLAHAGARLKGVFSRVDYQSRLSVSGAASFKQLLARLPPRVHSVYYR... | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus m... |
A0A524QSF8 | MNTIGSELRLTIFGASHGPCVGAVLDGVPPGMQIDIGRIQNEVDLRRPSAGIGTPRAEEDRVEVISGIVNDRSTGAPITLMVVNQDTDSGKYEKFKKVPRPGHADLTARSKYSECVDLRGGGQFSGRMTVGLVAAGAIAKMLLEERGIRVAAYVRQIGSVRDDVERDVTEALLSRSNEIRAADPEMVERMREEIMRAKEE | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 200
Sequence Mass (Da): 21749
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A0A7C9CNT9 | SASNLVQAGVRNILDIGCGYGTFGAHLFANGLLTMCIAPYEASGSQVQLTLERGLPAMIGSFTAKQLPYPSLSYDMVHCARCGIDWDEKDGLYLVEVDRVLRPGGYFVWTSPLTNARNKVNQKRWNLIHDFAESLCWELLSQQDETVVWKKTPKRGCHFSRKTDSSPVICSRSGDVESPYYQPLQTCIGGIHSHRWIPIEERSTWPSRIRLNAKELQAYRLHLEDLEEDSAKWNSAIRDYWSLLSPLIFSDHPKRPTEEDPSPPFNMLRNVLDMNARLGGFNAALLETGKYAWVMNVVPTNGPNYLPLILDRGFVGVLHD... | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 420
Sequence Mass (Da): 48020
Location Topology: Single-pass type II membrane protein
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A0A1S3AKM3 | MGGAACALTSVMAGAARALTRRGPVASIPVAREQLCLRDRPALDRSCHCGSRHVCEPTRLRRLATGRRPPPSQPRSARKRPAHPAADYKPHGAPRALLAAAQHTPRRTTSPMVPRAPSSPPPPSGDPAAQRARPPGRDPGALLATGRGERRPSFPASAPRSAAASSPRPLGTVPGREPAAVGFGPARTPGPLSLLRLGGRRAHTLTVLFILTCVLGYVTLLEETPQDTAYNTKRGIVASILVFLCFGVTQAKDGPFSRPHPAYWRFWLCVSVVYELFLIFILFQTVQDGRQFLKYVDPKLGVPLPERDYGGNCLLYDPDN... | Pathway: Lipid metabolism.
Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) is replaced by L-serine.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
EC: 2.7.8.29
Subcellula... |
A0A7S4AZA4 | APSAALSDCGRCGGARSSSHATPPRGRPYGQTISRNGLYAPDHQHFFVARLDMAVDGVRNRVVEVESRKLAAHARAADAHGGAFSRVRTVLGSEARAAREAQPHVG | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 106
Sequence Mass (Da): 11184
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A0A6P7GAB9 | IKHLGTTPIVKPAWITDSIDFGKLLDYRRYLLYNNQSKSQPKIGFPVIEKVSASASISENNSANVESDTVVAETSELIQNSIAQIKSDKLSSTNQINRFPTKTASDPNFLEEFYNNSRLHLISTLGAEFKHLVGQMRELSDGKFPGLEKLISCKVPEGAILVPSTVIMHIDMDCFFVSVSLRNHPELKGKPVAITHARNGQLSNVRPDQRSAREQEFSLYSERLPVGVTSRVDQIDIQSSMSEIASCSYEARKFGIKNGTFLGQAIKMCPELKTLPYDFEGIKEVSHTLYRTVASYTLDIEAVSCDEMYVDVTKILRKTG... | Function: Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by p... |
A0A8H6XX59 | MDAICDRLQALAAEGGSSSRLLMYSHDNYGLGHLRRCRAIAHTLVERFHNIRVLIVSGSAIGNAFDFRDRVEYLQIPSVVRLMNDDHAAIIRLMSGLYMPPKHTELYEVLQCRVDTLLNAAKLFRPSIFYSDYSPLGLRGELIPALEYLKTQDAMLVLGFRDVLDSPTKLKSEWGHLNDLARAAELYDAVWVFGPEDFYDPLVDLEAPKALHDRLVYTGFLHREIPSPLPGGDGSRLFHQVIEAYASDPSLTKQAILVLGPLMHPSKREEIHRKAAAHSAFHVIDFEAHLEPIMQSAAGVVSMGGYNTFCEILSFDKRAI... | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway.
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP
EC: 2.4.1.141
Subcellular Location... |
A0A2H0V9K5 | MQYFSIVIFSVVQAITEFVPISSSGHLVILHNILPQISINDLAFDVFLHAGTISSVIIFFAADIKKMIKAFYQSLIGHGLNEDGRLAWLIVLATVPAAVAGYFFGDLIEYRLRSIMVVAVMLILVGLFFLVVEKFAKQTDDLRNLNWRSSL | Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Membrane
Sequence Length: 151
Sequence Mass (Da): 16879
Location Topology: Multi-pass membrane protein
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A0A7W0YQE7 | LFSVERYAGVIEAFLSGMERRLERGLPLEAVSSVASFFVSRVDGKVDALLDRAGANDPSPLRGQIAIANAAAAYRLFEWSLGTPRWDRLAKAGARPQRPLWASTSTKDPRYPDTYYVEALVAPRTVNTLPPETFTAYRDHGRPAVRIRDGIAKAPAQMKALATAGIDLAAITRELEDDGVAKFAASYRSLLSGIEAKAGELVGR | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic... |
A0A0F3IKM6 | MNKARSSPLTPVLMHLALGLYTLICLAPVVLVIMNSMKSRSAIFAAPMALPTPKTFDLIGFTTVLSKGDFVGYFGNSLIITCGALFCVLLFGAMAAFALSEYKFRGNTLLGLYLALGIMIPIRLGTIGILNIMVATDLVNTHLGLILVYT | Function: Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 150
Sequence Mass (Da): 16061
Location Topology: Multi-pass membrane protein... |
A0A7J4URR4 | MEFEAWEGIYEKIRMEFGFQKENDEHARDVLNNIEPEYRIEELTKFESAKVMIAGGSKCIEQELDLVEKVDRVIAVSTAADVLLEKDIKIDMMVTDLDKNPGTAVRLSKMKIPVAVAAHGDNIGDLKEWVPRCDLNYVMGTTQVEPIGNIVNYGGFTDGDRAAFLGDAMGASEMIFIGWDFDDESVGIEKRHKLKWAEFLLLLLEGQRGQKFNVLEGRREKIREMI | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of diphosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin (6-HMD), leading to 6-hydroxymethyl-7,8-dihydr... |
A0A1E3QRR0 | YGHNPNQFIDQSQQQFYPNQQQNQPQPQQQQQGLPGNPQFSNFFNDPAASMGMQFTQSAFQSSNQYISSNFNLYIARSHLESYFKISTNYVLRKIFLVLFPYRHKSWSRAVETSSSNDQSTAAFAPPLTDTNAPDLYIPLMGFVTYVLFGAVTAGARGKFHPEILGYNATSTLAFAVIDLLLLKLGIYLLADPSSSTPGVTYGALWDLVALTNYKYVSLIAISILHKVLGLDNKFFAKWAVFGIVFVGWALFLLRSLRDVVLPPSSTGATMYGNGFGNSSSKGRKVKVQFLFVYCFVGEFFIFWFL | Function: Has a role in transport between endoplasmic reticulum and Golgi.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 306
Sequence Mass (Da): 34296
Location Topology: Multi-pass membrane protein
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A0A1D1YGJ0 | DFMIQGGDFDRGNGTGGRSIYGPSFDDESFALKHVGPGVLSMANAGPNTNGSQFFLCTVKTPWLDKRHVVFGHVVEGLDVVRKLESQETSRSDVPRLPCRIVNCGELPMVG | 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: 111
Sequence Mass (Da): 12025
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A0A0C9W1X3 | RATARTTNFTVIIVGAGLSALLAYALATELFARNSPTVLYNDACEKIKASPAVHAHLRPPFIFHNHPPLTHRPRHRNRSVNSLLTVDSSGREHLLLNFFIEGSDPSTSSLPVNTDEPLMDRLSSWAQDKTHALSGLTADDALNWSKAKVHEGWRRTKTAFAYLTGAPVPPAPQPTTQTIEVVRDSGREKEGWSLTGAFGRMIGRRSSGRESRTDLARVGIWTTGEVHADLIKDEDGKFVYRYLLINLPDSNSRNAQRIFVERMDGVPEHESILRWSSH | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Location: Membrane
Sequence Length: 278
Sequence Mass (Da): 30967
Location Topology: Single-pass membrane protein
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A0A976MFB3 | MESRSPSDELDTSKSLRKRHMIKIDSHYTQSQNSQSDDDESRYKQSPNQQSDQSPVFHSPSENHLDPEATNEETHTNPSPYNHFHTASMDIPEFDHELLQSEYMSQNIFDQDDHGSVHSDARDDCEIVNIVQSGSSNNSSITVDALSRFNMLSSQNGSTSDPILVDDSVNSSVEDTNHEHNTNEPSNYNNEVYEVVIATDTSTQNRTNILSQPNFTNTPRRSINTAESREQDSDDCIMGPIHWGNKRPPMFPLDYYRTHRNFSNAYKFLDTERPSELRSLDDIEFLFKCPICYSTITRLRSGKVPNENDKVIYSTKCGHL... | 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: 3... |
A0A7C1GUX1 | MPNARRKKQPVRVDPQLRRRWLRRAGVLVMLLAFVVMVWAGIERLRDPQTLPVRQVRIEGELTYLDRAELERVAAPLVSGGFFTIDLRRVEAAVEALPWVYDVSLRRQWPDTLELRVTEQVAIARWGDEALLNQYGELFSPPVESFPGGLAVLHGPVGQQRELIARFIKVSELLKGAGLRPRALVEDERRAWRLTLDSGVEMLLGREEMLARLERFVTVYPQTLARKAEALARVDLRYTNGFAVAWRAETQPAAQ | 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: 255
Se... |
A0A7V9T2M8 | MLLVLDIGNTEITTGLFHGDSLSSHWRLTTNPDRTPDEW | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
EC: 2.7.1.33
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Length: 39
Sequence Mass (Da): 4440
|
F0WVD2 | MGKQRNPQSVSGRKKHNCRPLTRGDEESELSFSRRSFPVKLFMWDYEQCDAKRCTGRKLCRLQYMRSMRPGQSFRGLVLSPNTKTVLSAADRNLVESTGISVIDCSWAKLSELPPNHFKKSGVHRLLPFLVAANSVNYGKATKLSCVEAVAATLYIVGLKEEAIQLINEFSWGNEFLKINQDCLEAYAACNSSDEVVKAQSKYLEGCRKEQEERLNRFALPKYESSDESEQEIDPDLLTETVAHDTVVTESVVKDLETIETVAQDPEITATVAQDTDITETDQTFPPIKETLERALPAVQTTQNLRKMSHAAKCDSNAET... | Function: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
EC: 2.5.1.-
Catalytic Activity: an N(1)-methylpseudouridine in 16S/18S... |
A0A7S4B2H6 | LADSGAKPRLANSRRDVAWRDQHMASHTSSTSTKHETKPLRSKAQKLHSSASKKALAKGLLTGVKKKTVMHKQQGLKAKSRSSTPNTNNNGRRTLGTRVGDNGGGNEAQGLCGTAPKSCHRDGGRSESADRRVASSATAATASSTTAHVTPTAAPAAAAGGASRLCPFESLQPPLKPPTLRALHSMGFATATPVQAAAIPRLLRHQDVAVQACTGSGKTLAFLVPLYELIARRADALKKHQVGAIVIEPTRELATQVHSVAQKLCAEWSGTTLALLVGGTNIHADMARLREEGAHVLVGTPGRLEDLLERLRELSVKELE... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 786
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): 84879
|
A0A2P2E7X5 | MESVDPASNRVKPANRRRQDLSEAARISVTDMGAYVLAVILTFIGLLFAVSGGDIVGPASNWILALLIISGLVIGYLSVRVGSRLLALRKAGQKAQSGARLHLRFVMLFAANGVIPVILISLFSALTIGQGIQAWFSSQVRDAVQATRILGNQAVEKTAEATKVDIAAMAVDLNASAIQLKVDPDAYRQYLAVQADRRGFVAAYVLNAQGTKLAQAQRPQGVPQFILPDPDDFATAQAGDVSINIDRSAVVRALYRLDAFSNSYLAVVRLPEPGQLSLFEKATAAVYAYQLIEERQGLLQLLFALAYLEIVLLVLIGSVW... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell membrane
Sequence Length: 757
Sequence Mass (Da): 81039
Location Topology: Multi-pass membrane protein
|
A0A081BLM6 | MPTPNILQKILAQKTLEIAAAKNTISAQELQARIALMGPARSLRDALQRNGLSVIAEIKKASPSAGVIRENFNPPEIARSYINASADAISMLTDEKFFHGSLAYIPQIRPFTPIPILRKDFIIDRYQLLEARAAGADAVLLIVAALEKAQLRDLLRQTRELGMEALVETHTAAEMDIALDAGADIIGINNRSLETFQIDLATTEQLALLAPESVVIVAESGLHTRDDVQRMIAAGVDAILVGTHFMKSPDPGAALQAFLSGRGEC | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 265
Sequence Mass (Da): 28613
|
A0A2J6I203 | MMLHYILWNADPEIFELFGRGVRWYGLLFAGSFYLAALMLRRILLKKDMKDEQISKLIIFLIVGCLVGLRLGHCLFYEPGYYLSNPVEILKIWKGGLASHGAAIGILIALYLFIRKTNFSYLWLLDRIVIVVLFIAPFIRTGNLMNSEIIGDKTNMSHAFIFVKGIDDELVRKNGKYIDKTTINQIGKDTVVDNIHYSKLNLEVYFNKNIPKNRIGDFLHQLFIQQIENDSDLKQNIKLFIDKPSIEIIEQGGKYKATMTLYGIPRHPSQVYEALAYLSFFLIFIIYYIRQKGMIREGFLFGMFLILVFGFRFFVEFLKE... | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,... |
A0A6N9T5E4 | MKDIVLACSRKADVFAKMAEYLSWLVLLVWVGLIAVGVVMRYVFAAPLIFQGDLVSALLVVFASLSFASLLVREQHIRVDLLTRHFSLKAQYYLTAFSYLVTLLLSALMITASKNLIFLSYMMNSRFDVSGIIAWPFQAVFSFGFLLLGTVSLLRFLEMVVDPNGRLSPGQSR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 173
Sequence Mass (Da): 19383
Location Topology: Multi-pass membrane protein
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A0A2M9W6C1 | MIATKTGFTLAALVMLTALAVLFSHWTAFLAWSLQTQIQLHRLLVTHLLQINSGQYSAGLWLIGVTFIYGILHAVGPGHGKFIVTTWLTTHQPPRGVALTVPFLGSLVQGLSAIAFVFILAVGFNLTTGDLSTSRWYLEKASSLFIAALGVMMMVQAWRSRSQYQHHNLNHNHGHGHGHGYDQEHEHEHEQHHHGCGHHHGITAESVDNWKAWIGIIIATGVRPCSGALTVLLFASVIGITRWGMFAVMTMALGTGMALVALALFVRHFRHRAGELWLAESSPRSQQILGILRIAGGALLMLFALVLFLTVVPISANGDY... | Function: Efflux system for nickel and cobalt.
Subcellular Location: Cell membrane
Sequence Length: 325
Sequence Mass (Da): 35435
Location Topology: Multi-pass membrane protein
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A0A096XUH1 | IWGGFSVDNATLTRFLAFTSLCPLAVVAATILHALFLHETGSNNPMGLNSDSDKIPFHPYFSYKDFLGFITLLTLPPSLALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLFSILVLMLIPLLHTSKQRGLTFRPLSQTLFWVLVADVMILTWIGGMPV | 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... |
G2T049 | MLSAVAFILMFLDFSVPFMPAFIKMDLSELPALIGAFSMGPVCGILICLIKNVLHLFITTTGGVGELSNFLLGVAFVLPAGLIYRHKKSRRSALIGSLFGAVIMGVFSVVSNYFLVYPVYYNFMPEEAVLGAYQVIVPSMKSILQCLVCFNMPFTIVKGLFSVVITFLVYKHISPILKGANR | Function: Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex.
Subcellular Location: Cell membrane
Sequence Length: 182
Sequence Mass (Da): 19960
Location Topology: Multi-pass membrane protein
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A0A316UZ43 | MSLARTFRLIREGGVSIACGYRGRESYTTRYWSAHTVPPAMSFSSHPLPILVPPTTFNTNTRLIPPLPQLGRYWRNMQSLGDAKAGTYMGTDRAGNKYYEDLNEIPGRHRWVEYAQNNEVNASQIDPAWHGWLHHTHKMPPEQNPNMGRPTWESVSRAPLEAVMPS | 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.
... |
A0A2H9HZZ0 | EQGLIEHPPTYRSHTYFDEIYYVRTAENYLHGEEPYEWTHPPLGKFFIALSILSLGFSPFAWRFAGVAIASLMVPAIYILAKMMFRTRVAALLSASILSLDFLHFTMGRIATVDTFAVFFILTSYLFLFLCYRRLTEGEGLNGRYFLAGAVTFSLAFSTKWYALYGFVGQVILIIAVLLWNLKTSRCEFKGFSRSLMIIVCSMVLAVLVYFCSFIPYMMLGHSIQDVINRQWEMYRYHSTLKATHPFSSPWWSWPLITRPVWLDVQYLPDGMVSTIVAMGNPGIWWMSLPFLTATALKAMKDRDRNSLYIVWLFLFQWLP... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Location: Membrane
Sequence Length: 400
Sequence Mass (Da): 46684
Location Topology: Multi... |
A0A8H6Y8N2 | MPLPVPPLLQTLPRRTKRAKVESSATPDGPSVSGEASKSPLKRASKSPQKSTSYKKALATADPEPPRWREVYACIKKMRDTNKAPVDTMGCHMAQQHETDPKNKRFVTLVSLMLSPQTKDQVTDAAVSKLRTALGGSVSLDAVLAADKETISGAINKVGFWPRKTEYIKRAAEKLRDEFDSDVPKTIEGMVSLPGVGPKIGFLALQHAWGINIGIGVDVHVLRITRLLGWHKADNPEDARISLESWLPTELQVEINPLLVGFGQTICPANTPHCGECDLSALGLCPSAKLKAPKKKKPVAVPDW | Function: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glyco... |
A0A7J4SN47 | MTKTKICGITNEDDLVASIGCGANYVGFIVDISVESHRKISPEFANELVSKVPSGVTTTMVTILEDADRTLDFFEQVGADALQIHGDLTLDVIQKVSDSIDGKLIVSVDPNATISNQLEGIANAALCDSQREKGAGGTGKVTDWESVRKFREKTKLPVILAGGLTPQNVSHAIRLVKPFAVDVASGVEGPNGLKDHSAIREFITNVHKVEGGKL | 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: 214
Sequence Mass (Da): 22782
|
A0A261BWT0 | MRKLAIEAITCNFVDNLDLQSPNGRIKARGWIARIKFSRFLSGQCISIFHSFTKLLYCINVLSDIWAGRPWTETGHFPRVTLCDFEVRYLANLNRYTVQCALLINIINEKVFAFLWCWYMILAIITTCSFIYWLANSFIHSEKVDYVMKFIQIAESSEFKKLQKFEKDATVERLYTVIAFAPHLLDSFVSDFLKSDGRRMGVVCDIS | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 207
Sequence Mass (Da): 24099
Location Topology: Multi-pass membrane protein
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A0A656GK25 | NHATLAGHSFHHEIATAVSLGIFGSIDANRGDPQNGWDTDQFPNSVEEMTLAHLRDSQGRWFHQWRLQFRFQGPSSEPRRSRPVPRPRCR | Catalytic Activity: alpha-D-xylose = alpha-D-xylulofuranose
EC: 5.3.1.5
Subcellular Location: Cytoplasm
Sequence Length: 90
Sequence Mass (Da): 10361
|
A0A2N5Z4I6 | MRLGVSLAVSFSAITGYIVAASSIDINILYIFLGVFLLSGGASALNQFQERNVDALMFRTKSRPIPSKLISAGLGLFIAILLCSAGFILLYLKVGTLPAMLGLLNLIWYNGFYTFLKKKTVFAVVPGSLTGVTPLLIGWSAVNNYLLDPQIVFISFFIYMW | Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o
EC: 2.5.1.141
Subcellular Location: Membrane
Sequence Length: 161
Sequence Mass (Da): 17599
Location Topology: Multi-pass membrane protein
|
A0A349G6F3 | GILVSKTGKILSNETTIDMKMSPDMMNESWYIDVMEKGSMPVLTSIRRQAFTMDKSQWVISIGQEIVDEEGAHVGLFILDFSYEVIERFLLNLSLGSEGFAFILSDLDELVYHKDVSFFESRENLTELTAIQKMVSGYDKTMGKLTHQVDIEGTDWCLVGVSSLDHLSAARRQLFEVITLVALLLTAIAIGSGVLIASRISKPIRSLEEAMNHLSSELVDAVEVPNSCYEVDNLRLRFNEMRIQIEALLAGIKEKEYYLRESEIRALYSQINPHFLYNTLDTIIWMAEFKDTEKVVAITKALAQFFRISLSHGDALIPLS... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 476
Sequence Mass (Da): 53502
Location Topology: Multi-pass membrane protein
|
A0A6P7FQV3 | MRLNQVLKIALLALFCNITFCDSFNILAITPHVGKSHQLVFEPLFKKLVSVGHSVTLITRYPMNVDSPKWRDIPIGPEDTNTTELFDFSLLTGTRFDRYACPLVLAEAARISCSEGLPHPNLQRFLKEDNHFDVVLMEVFNTNCYMGIATKYNVPVIGVHSAGWMPWMYQWFGVPYHPGFVTDHFLGNSQPMDFLARLENTIVHIYNNAIYTVTMGWYGSYLSNKYVGADLYENGDVMKNMSLLLINTHFSLNLPLPLGPNVVEVGGLHLESKPNKKLPQDLEKFITDSKHGVIYMCMGSTIRGASFPESKKQAFMKAFS... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 519
Sequence Mass (Da): 59271
Location Topology: Single-pass membrane protein
|
A0A6P7GP80 | MMNYGKNDTAVLPENHVYITPTKQVKNMGDMQHWEKSEAYHEYLGFVCALNEAIKCKTNSAGSANASEEINKICSLLNSLDTWIDEIPPIQQPQRFGNQAFKQWFAKVKDLKILQQVDMHTCFNHLRYPFVEVIGR | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 136
Sequence Mass ... |
A0A7S4BMS5 | MAAASRRCTREGVRLVNVSLLSTASRRFSLASCSKLPLSSLRTRLAVPALLAEFRVLNLSQFMRCHSTPAGNGPSDKSPDKAEPAKSPGENATPQEGPDGKSKTGTGQAASDASSAQPKSGEAGAGQAAPEVSTSSTQPPSGGAASNASAPGEASSDDMIHVGKGEKAPGGLTVHDDESEENLPPLAFEPGAAGVAQKGISAVIIAFGAVAFGACAWGISEALFPSASSTQVIFNEAFDQVRLDGDILYALGTPLKAFGADHGSERGRRNAIDRWEVEEGGEELSVIRFHVAGPNGAGLVLVQVPRKRRRGEFRYVIFEH... | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Location: Membrane
Sequence Length: 347
Sequence Mass (Da): 35895
Location Topology: Single-pass membrane protein
|
A0A1S3W8E5 | MAAGIVSFVLFSFFWGICDAVTGSRVYPANEVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEASQNNWLRTDWITREGAQRVYIEIKFTLRDCNSLPGVMGTCKETFNLYYYESDNDKERFIRESQFGKIDTIAADESFTQVDIGDRIMKLNTEIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKKCPLTVRNLAQFPDTITGADTSSLVEVRGSCVNNSEEKDVPKMYCGADGEWLVPIGNCLCNAGHEERNGECQACKIGYYKALSTDATCAKCPPHSYSVWEGATSCTCDRGFFRADSD... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
EC: 2.7.10.1
Subcellular Location: Early endosome
Sequence Length: 986
Sequence Mass (Da): 109611
Location Topology: Single-pass type I membrane protein
|
A0A261BKG4 | MFASRKLVEKALGEVKKKFVGVVSAKLPADGMEYDLVQYRCRNIQSFYLIADDIMDNSETRRGKQCWFRREGVGMSAINDAFIMDSFVEDILRLALPGHVNLDRLCEAYRKSKQKTLIGQFLDTSSVNQIASFTWDRYELMVENKTSHYTVFHPLQMALIISDVLAYHGAVKKAAYQIGFLFQSQDDFLDVYGDPTITGKIGTDIQDGKCTWLAVRALQKMHSTPQKSAHLITDFKQSFGTSDPEKIEKIKKIYDELQLREEFRRTNIEMPTSLQHSKPRVSYYYDGDFGNFYYGQGHPMKPHRVRMTHSLIVNYGLYRA... | Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
EC: 3.5.1.98
Subcellular Location: Nucleus
Sequence Length: 875
Sequence Mass (Da): 100260
|
A0A7S4C389 | RLIDSKGMADEELSASPQNTLASNQQLLDAFPPVAFAFAYGSAVYPQRGYSRADLNSAMTDLIFAVDDPLQWHALNMERNSSHYSLLGALGPSTVAAVQEHVGAGIYYNALIPVRGRMVKYGVMSTSRLADDLRNWSTLYVSGRMHKPIQVLLPDEKMHRAQACNLHSALSAALILQPSRMNERALFKSICGLSYGGDVRLRLVENRKVADIVDAQLALLRAIYADPMQALISQGHLHARPAKGSAATDTDSLSNHSRRVKAGEDVYYEQDESWEGRERLLSRLPRNAKSELIRTLSGARTSADTPDEEVSARLNETARA... | Pathway: Lipid metabolism.
EC: 2.7.7.41
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 346
Sequence Mass (Da): 38030
Location Topology: Peripheral membrane protein
|
A0A124SHT9 | MLTVSDGGRANFTCISAQQPGLKDEDDTPRNNLKKALDSAPPSRDFRGVLKEIMKENNSIFSLKKALDNAPPSRDFRGALKVSYIRTGSPGLIAEVKKASPSRGVLREDFHAVEIAKAYESGGAACLSVLTDEEYFQGSFENLEDIRNSGVKEPLTLVKMQCPLLCKDFIVDVVQLYYARIKGADAVLLIAAILPDIDIKRMLKICKKIGLAALVEVHDENEMDRMLGIDGIELLGINNRDLETFEVDISITKKLLEGERGEKIQQKGIISIVKPKDPIQGIRKLFGKDISA | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 292
Sequence Mass (Da): 32187
|
A0A261C0T9 | MVSFVQLVVQIREIFGQKMVDVDEVKKLMGSYKSTPVTWWTSGMESTI | Cofactor: Binds 1 Fe cation per subunit.
Pathway: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.
EC: 1.13.11.20
Catalytic Activity: L-cysteine + O2 = 3-sulfino-L-alanine + H(+)
Sequence Length: 48
Sequence Mass (Da): 5510
|
A0A7W1QKI0 | MTLRFTTAGESHGKALVAIVEGLPAGLPVSAEWVDRELARRMQGYG | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 46
Sequence Mass (Da): 4943
|
A0A2J6HE15 | MRRKAKRSLKKTKMSRKFQKKLKVLKYVRLNELHYLLKMDTGGANAVFEPGQFVEVLVPGSKDAFLRRPISIHDVSNDNASFTMMIKIVGEGTRALSEVREGDELDIVFPLGHGFSINENHQKVLLVGGGCGVAPLLHLSKAAKEKGLQPHVVIGGKTADDILEADAYRKYAEVAVMTENAEIGDIGMVTDHAWLREKLKDFDFVYTCGPDPMMKAVAALAEEAGIECEVSLENLMACGIGACLCCTVHTHDGNVRACVEGPVFNASQIIGWNQNENCHV | Cofactor: Binds 1 FAD per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Function: Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate ... |
A0A261BZ85 | MNYRITAVLFGVVFLIVIFINEDDRALSKADRLCIQREWHQNPTIKATTSHGSSFFIAFGDVQKSVEWLYLPEIVTSEKSEILMIVQSRSENLGRRNVLRGTWMNENFSQMMRERRMKALFLVGIVEKDENVKKLLLEEAKLYGDLIVVDLIDNYVGLTYKTIASLLYATSKAPKFQLIGKIDEDVAFFPDRLINLLNDDVIDTNTSTLYGEIVREGGEVNHDKSKKW | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 228
Sequence Mass (Da): 26230
Location Topology: Single-pass type II membrane protein
|
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