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O66129 | MIALSYKAFLNPYIIEVEKRLYECIQSDSETINKAAHHILSSGGKRVRPMFVLLSGFLNDTQKDDLIRTAVSLELVHMASLVHDDYIDNSDMRRGNTSVHIAFDKDTAIRTGHFLLARALQNIATINNSKFHQIFSKTILEVCFGEFDQMADRFNYPVSFTAYLRRINRKTAILIEASCHLGALSSQLDEQSTYHIKQFGHCIGMSYQIIDDILDYTSDEATLGKPVGSDIRNGHITYPLMAAIANLKEQDDDKLEAVVKHLTSTSDDEVYQYIVSQVKQYGIEPAELLSRKYGDKAKYHLSQLQDSNIKDYLEEIHEKMLKRVY | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the condensation of three molecules of isopentenyl diphosphate with farnesyl diphosphate (FPP) to yield (all-E)-hexaprenyl diphosphate (HexPP; C30), the precursor of the prenyl side chain of menaquinone-6. Large subunit Hexs-B catalyzes the condensation reaction and the final product chain length is cooperatively regulated by both the Hexs-A and Hexs-B subunits using the whole size of the hydrophobic cleft as a ruler.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate = all-trans-hexaprenyl diphosphate + 3 diphosphate
Sequence Mass (Da): 37083
Sequence Length: 325
EC: 2.5.1.83
|
P20060 | MPQSPRSAPGLLLLQALVSLVSLALVAPARLQPALWPFPRSVQMFPRLLYISAEDFSIDHSPNSTAGPSCSLLQEAFRRYYNYVFGFYKRHHGPARFRAEPQLQKLLVSITLESECESFPSLSSDETYSLLVQEPVAVLKANSVWGALRGLETFSQLVYQDSFGTFTINESSIADSPRFPHRGILIDTSRHFLPVKTILKTLDAMAFNKFNVLHWHIVDDQSFPYQSTTFPELSNKGSYSLSHVYTPNDVRMVLEYARLRGIRVIPEFDTPGHTQSWGKGQKNLLTPCYNQKTKTQVFGPVDPTVNTTYAFFNTFFKEISSVFPDQFIHLGGDEVEFQCWASNPNIQGFMKRKGFGSDFRRLESFYIKKILEIISSLKKNSIVWQEVFDDKVELQPGTVVEVWKSEHYSYELKQVTGSGFPAILSAPWYLDLISYGQDWKNYYKVEPLNFEGSEKQKQLVIGGEACLWGEFVDATNLTPRLWPRASAVGERLWSPKTVTDLENAYKRLAVHRCRMVSRGIAAQPLYTGYCNYENKI | Function: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides. The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide. Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A. During fertilization is responsible, at least in part, for the zona block to polyspermy. Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and inactivates the sperm galactosyltransferase-binding site, accounting for the block in sperm binding to the zona pellucida .
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 61116
Sequence Length: 536
Subcellular Location: Lysosome
EC: 3.2.1.52
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Q8X736 | MAKNYYDITLALAGICQSARLVQQLAHQGHCDADALHVSLNSIIDMNPSSTLAVFGGSEANLRVGLETLLGVLNASSRQGLNAELTRYTLSLMVLKRKLSSAKGALDTLGNRINGLQRQLEHFDLQSETLMSAMAAIYVDVISPLGPRIQVTGSPAVLQSPQVQAKVRATLLAGIRAAVLWHQVGGGRLQLMFSRNRLTTQAKQILAHLTPEL | Function: Negative regulator of phage lambda lysogenization. Contributes to the degradation of the phage regulatory protein CII. Acts probably by holding CII on the membrane surface, away from the target promoters, but close to the FtsH protease.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22947
Sequence Length: 213
Subcellular Location: Cytoplasm
|
P42665 | MFYSIFFIHILRIVLVDCNEYSEENVDDRHKWAVLVAGSNGFENYRHQADVCHAYHVLLSKGVKPEHIITFMYDDIAHNKENPFPGKIFNDYRHKDYYKGVVIDYKGKKVNPKTFLQVLKGDKRAGGKVLKSGKNDDVFIYFTDHGAPGILAFPDDDLHAKPFINTLKYLRQHRRYSKLVIYVEACESGSMFAGLLPTDINIYATTAARPDESSYATFCDDPRISSCLADLYSYDWIVDSEKHQLTQRTLDQQYKEVKFETNLSHVQRYGDKKMGKLYLSEFQGSRKKASTEHDEPPMKPKDSIPSRDIPLHTLHRRIMMANNMNDKTLLMKILGLKLKRRDLIKDTMEVIDQFMFNVKQPNSNATIDETMDCIEVVYKEFQSKCFKIQQAPEITGYLSTLYNYCQKGYSAENINGVIRKVCG | Function: This protease is used by the parasite for degradation of the host globin.
Catalytic Activity: Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.
Sequence Mass (Da): 48938
Sequence Length: 423
EC: 3.4.22.34
|
Q9LMJ7 | MISLHSSAIKASLYGSFPSSLRSTLSVSFSAGSLIRLPSVGKRNLSVVVSSGRDSSMSSNNVSRGSSSKVAAESFFRSVLGQMETVYLNRNPTPKSVLELVRSVDDQQLCYDHLAFRTFGIGGYGIDSLASFFLDYGYTPMDELKFPAKKLRALWFAPPNASAVPGGSGVNGPLPRVFISELLVDQMSSQTQDVIRKYTEASPNGKKYAGLSSALGTLTWEKPLSSEFEQLARESEYAAWTLVNGYALNHVTISVHRLKSHLNKIKKLNQFLEEKGIKLNSEGGVLKVSPDGGLQQSSTVADSISFKFADGVTKSIPCSYIEFAERLVLPQYQNIPESEIQESHRRDGFEVGNADKIFESTFQEQLSRRTG | Function: Catalyzes the decarboxylation and hydroxylation of 2-oxoadipate (2OA) to form D-2-hydroxyglutarate (D-2-HGA) . Is involved in a D-lysine catabolic pathway .
Catalytic Activity: 2-oxoadipate + O2 = (R)-2-hydroxyglutarate + CO2
Sequence Mass (Da): 40638
Sequence Length: 371
Pathway: Amino-acid degradation.
Subcellular Location: Plastid
EC: 1.13.11.93
|
P65066 | MSRSKRLQTGQLRARFAAGLSAMYAAEVPAYGTLVEVCAQVNSDYLTRHRRAERLGSLQRVTAERHGAIRVGNPAELAAVADLFAAFGMLPVGYYDLRTAESPIPVVSTAFRPIDANELAHNPFRVFTSMLAIEDRRYFDADLRTRVQTFLARRQLFDPALLAQARAIAADGGCDADDAPAFVAAAVAAFALSREPVEKSWYDELSRVSAVAADIAGVGSTHINHLTPRVLDIDDLYRRMTERGITMIDTIQGPPRTDGPDVLLRQTSFRALAEPRMFRDEDGTVTPGILRVRFGEVEARGVALTPRGRERYEAAMAAADPAAVWATHFPSTDAEMAAQGLAYYRGGDPSAPIVYEDFLPASAAGIFRSNLDRDSQTGDGPDDAGYNVDWLAGAIGRHIHDPYALYDALAQEERR | Function: Catalyzes the decarboxylation and hydroxylation of 2-oxoadipate (2OA) to form D-2-hydroxyglutarate (D-2-HGA).
Catalytic Activity: 2-oxoadipate + O2 = (R)-2-hydroxyglutarate + CO2
Sequence Mass (Da): 45332
Sequence Length: 415
EC: 1.13.11.93
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Q337M4 | MAVALAGARSPGAGAILSLRRLAPAAAAPVRLGGSGTPGTRRRRGIAMAAAASAPPAPADALPKGADSFFRTVISNMEKVYLSRNPTAKTILELVRSYDGDHICYDHFAFRTFGVDGYGIKSLAEFFTDFGYVPREELRFPAKKLRALWFSPPTNDGYTGTGVYGPLPRIFISELLVDELSPQSQDIIQKYIRTSGKGNKHATLASTSGELTWEKPIYSDFQVLSRESEYAAWTLVNGYALNHTTISTHRLISDIRSINKFNKFVEDNGFKLNSEGGILKVSPDGLLQQSSTVADSALFTFADGITESIPRSYIEFAERLVLPQFKDLPNDEVNEHHRRDGFEVGNADKIFESTSNDQLTRRSA | Function: Catalyzes the decarboxylation and hydroxylation of 2-oxoadipate (2OA) to form D-2-hydroxyglutarate (D-2-HGA) . Is involved in a D-lysine catabolic pathway . Involved in the regulation of starch synthesis and amyloplast development within the peripheral endosperm during the grain-filling stage .
Catalytic Activity: 2-oxoadipate + O2 = (R)-2-hydroxyglutarate + CO2
Sequence Mass (Da): 39934
Sequence Length: 364
Pathway: Amino-acid degradation.
Subcellular Location: Plastid
EC: 1.13.11.93
|
Q88CC1 | MPANDFVSPDSIRAQFSAAMSLMYKQEVPLYGTLLELVSEINQQVMAQQPEVAEALRWTGEIERLDQERHGAIRVGTAEELATIARLFAVMGMQPVGYYDLSSAGVPVHSTAFRAVHEQSLHVSPFRVFTSLLRLELIDNPQLRELAQSILAKRQIFTSRALELIAQCEREGGLDAADAETFVQEALHTFRWHQDATVTAEQYQQLHDQHRLIADVVAFKGPHINHLTPRTLDIDAIQLGMPAKGIPPKAVVEGPPTRRHPILLRQTSFKALQETVAFRDQQGREGSHTARFGEIEQRGAALTPKGRQLYDKLLDATRVALGGAPAEANAERYMALLQANFAEFPDDLAQMREQGLAYFRYFATEKGLAARDQEGRPTTLQGLIDAGHVHFEALVYEDFLPVSAAGIFQSNLGDDAQAEYGSNANREAFEAALGLQVQDELALYAQSERRSLQACAQALNLGSM | Function: Catalyzes the decarboxylation and hydroxylation of 2-oxoadipate (2OA) to form D-2-hydroxyglutarate (D-2-HGA) . Is specific for 2-oxoadipate . Is involved in a D-lysine catabolic pathway .
Catalytic Activity: 2-oxoadipate + O2 = (R)-2-hydroxyglutarate + CO2
Sequence Mass (Da): 51372
Sequence Length: 464
Pathway: Amino-acid degradation.
EC: 1.13.11.93
|
O59394 | MYKVAVIKGDGIGPEVIDAAIRVVKSVTDKIKFYEFEGGLSVFKKYGVPIREEDLEEIRKMDAILFGATTTPFDVPRYKSLIITLRKELDLYANLRIIPNFKLRKEIIIVRENSEGLYSGEGAYDSNKVVDFRIITRKGAERIAKFAVKLAKDRSTFLTFVHKANILESDRFFRKIVLDIARKEDVKVREEIVDSFTIKLVKDPWNLGIILSENMFGDILSDLATIHAGSIGIVPSGNYGEDIALFEPIHGSAPDIAGKGIANPIGAILSAAMMLDYLGLDGSIIWKAVGRYVRRGNLTPDMEGRATTLEVTNGIISEIYRLDEYEIDEVWRDEVRLGRILLEIS | Function: Catalyzes the NAD(+)-dependent oxidative decarboxylation of homoisocitrate to 2-oxoadipate (alpha-ketoadipate), and of isocitrate to 2-oxoglutarate, at near equal efficiency. May thus play a dual role in glutamate and lysine biosynthesis in vivo. Preferentially uses NAD over NADP.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 38735
Sequence Length: 345
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 4/5.
EC: 1.1.1.286
|
Q72IW9 | MAYRICLIEGDGIGHEVIPAARRVLEATGLPLEFVEAEAGWETFERRGTSVPEETVEKILSCHATLFGAATSPTRKVPGFFGAIRYLRRRLDLYANVRPAKSRPVPGSRPGVDLVIVRENTEGLYVEQERRYLDVAIADAVISKKASERIGRAALRIAEGRPRKTLHIAHKANVLPLTQGLFLDTVKEVAKDFPLVNVQDIIVDNCAMQLVMRPERFDVIVTTNLLGDILSDLAAGLVGGLGLAPSGNIGDTTAVFEPVHGSAPDIAGKGIANPTAAILSAAMMLDYLGEKEAAKRVEKAVDLVLERGPRTPDLGGDATTEAFTEAVVEALKSL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the NAD(+)-dependent oxidative decarboxylation of homoisocitrate to 2-oxoadipate (alpha-ketoadipate), a reaction involved in lysine biosynthesis through the alpha-aminoadipate pathway. In addition, has high activity with isocitrate, but is inactive with 3-isopropylmalate.
Catalytic Activity: (2R,3S)-homoisocitrate + NAD(+) = 2-oxoadipate + CO2 + NADH
Sequence Mass (Da): 35922
Sequence Length: 334
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 4/5.
EC: 1.1.1.286
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Q8IV36 | MGSTDSKLNFRKAVIQLTTKTQPVEATDDAFWDQFWADTATSVQDVFALVPAAEIRAVREESPSNLATLCYKAVEKLVQGAESGCHSEKEKQIVLNCSRLLTRVLPYIFEDPDWRGFFWSTVPGAGRGGQGEEDDEHARPLAESLLLAIADLLFCPDFTVQSHRRSTVDSAEDVHSLDSCEYIWEAGVGFAHSPQPNYIHDMNRMELLKLLLTCFSEAMYLPPAPESGSTNPWVQFFCSTENRHALPLFTSLLNTVCAYDPVGYGIPYNHLLFSDYREPLVEEAAQVLIVTLDHDSASSASPTVDGTTTGTAMDDADPPGPENLFVNYLSRIHREEDFQFILKGIARLLSNPLLQTYLPNSTKKIQFHQELLVLFWKLCDFNKKFLFFVLKSSDVLDILVPILFFLNDARADQSRVGLMHIGVFILLLLSGERNFGVRLNKPYSIRVPMDIPVFTGTHADLLIVVFHKIITSGHQRLQPLFDCLLTIVVNVSPYLKSLSMVTANKLLHLLEAFSTTWFLFSAAQNHHLVFFLLEVFNNIIQYQFDGNSNLVYAIIRKRSIFHQLANLPTDPPTIHKALQRRRRTPEPLSRTGSQEGTSMEGSRPAAPAEPGTLKTSLVATPGIDKLTEKSQVSEDGTLRSLEPEPQQSLEDGSPAKGEPSQAWREQRRPSTSSASGQWSPTPEWVLSWKSKLPLQTIMRLLQVLVPQVEKICIDKGLTDESEILRFLQHGTLVGLLPVPHPILIRKYQANSGTAMWFRTYMWGVIYLRNVDPPVWYDTDVKLFEIQRV | Function: May play an important role in the development of cancers in a broad range of tissues.
Location Topology: Lipid-anchor
Sequence Mass (Da): 88745
Sequence Length: 788
Subcellular Location: Cytoplasm
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Q5NUF3 | MAKEIVKELLPLIRVYKDGSVERLLSSENVAASPEDPQTGVSSKDIVIADNPYVSARIFLPKSHHTNNKLPIFLYFHGGAFCVESAFSFFVHRYLNILASEANIIAISVDFRLLPHHPIPAAYEDGWTTLKWIASHANNTNTTNPEPWLLNHADFTKVYVGGETSGANIAHNLLLRAGNESLPGDLKILGGLLCCPFFWGSKPIGSEAVEGHEQSLAMKVWNFACPDAPGGIDNPWINPCVPGAPSLATLACSKLLVTITGKDEFRDRDILYHHTVEQSGWQGELQLFDAGDEEHAFQLFKPETHLAKAMIKRLASFLV | Function: Dehydratase that mediates the biosynthesis of isoflavonoids. Can use both 4'-hydroxylated and 4'-methoxylated 2-hydroxyisoflavanones as substrates. Has also a slight carboxylesterase activity toward p-nitrophenyl butyrate.
Catalytic Activity: (2R,3S)-2,4',7-trihydroxyisoflavanone = daidzein + H(+) + H2O
Sequence Mass (Da): 35138
Sequence Length: 319
Pathway: Secondary metabolite biosynthesis; flavonoid biosynthesis.
EC: 3.1.1.1
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Q28BZ2 | MSAEAGATVEQNHSYDMSCIFCRIANKQESGAELLHSDDDLVCFKDIRPAVTHHYLVVPKKHVGTCKTLTKDHVQLIKTMMEVGKSTLQKNNVTDLEDIRLGFHYPPFCSISHLHLHVLAPASQLGFLSRMIYRVNSYWFITADELIDQLQAS | Function: Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (By similarity). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase (By similarity).
Catalytic Activity: adenosine 5'-phosphoramidate + H2O = AMP + NH4(+)
Sequence Mass (Da): 17316
Sequence Length: 153
Subcellular Location: Cytoplasm
EC: 3.9.1.-
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Q84VV6 | MAGVNQACIFCEIVRNPTTTRLLHTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDLQRRDEDYSLVRHMLSVGQQLLQKDAPQSIHRFGFHQPPFNSVDHLHLHCFALPYVPRWKAIKYKSLGPLGGFIEAETLLEKIRPLLSKV | Function: Possesses adenylylsulfatase activity in vitro, releasing AMP and sulfate from adenylyl sulfate. Possesses also adenosine 5'-phosphosulfate (APS) phosphorylase activity in vitro. Catalyzes the phosphorolysis of APS, leading to ADP and sulfate.
Catalytic Activity: ADP + H(+) + sulfate = adenosine 5'-phosphosulfate + phosphate
Sequence Mass (Da): 16798
Sequence Length: 146
Subcellular Location: Peroxisome
EC: 2.7.7.5
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Q9VUW9 | MYQSACQAATTGSCVPGTGQQPDNERQSALIAQQPPTAPVEPDYSGFDIVKATQYGAIARVRELVESGWDVNQPDSETVTLLHWAAINNRRDIIRYFLEKGATVDAVGGELNATPLHWATRQGHLGAVVLLMAAGADPRIRDAEGCSCIHIAAQFAHTALVAYFIAKGVDPDLQDRGGMTALMWAAWKVCALDPVRLLLTLGANPAMVDYTHGNTALHWAILARNATAISTLVLKSKASLDVPNLRGETPLSMLESQTGAIWIGAKVMDRVKEAALTSQQRRSLLSKLRHDKRLRWWSMVACPFTAFYLAGIVFTVNTLYIIKFFLLGCLYSIFHTIGKALFDEHLMALLPLSVYLATKAWFYVTWLMYIDDAVSFTATVCFLISSLLLWVCFLKSWKGDPGIIRPTREQRFKTIIELSERGGIGFEPASFCSGCLVRRPIRSKHCSVCDRCVARFDHHCPWVGNCIGLKNHSYFMGFLWMLLIMCAWMLYGGSKYYVNQCNVRFDDFLGAMRAIGNCDAWVGWVMGNALLHMSWVILLTICQTYQVICLGMTTNERMNRGRYRHFQAKGGHSPFTRGPIQNLVDFLECSCFGLVQPKRVDWMNYYDYDAQTHQTIEKEPLLSVDCPDGMAGDHQYV | Function: Probable palmitoyltransferase which is required for photoreceptor synaptic transmission and for the correct expression and localization of palmitoylated protein Csp and synaptosomal-associated protein Snap25 . Probably palmitoylates Csp . Probably also palmitoylates the dorsal-ventral patterning protein Sog and promotes its secretion and activity and the stabilization of the membrane-bound form . Required for synaptic vesicle exocytosis .
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71299
Sequence Length: 637
Domain: The DHHC domain is required for palmitoyltransferase activity.
Subcellular Location: Golgi apparatus membrane
EC: 2.3.1.225
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P46586 | MDLVNHLPDRLLFAVPKKGRLYEKCCNLLSGADIQFRRSNRLDIALSTNLPIALIFLPAADIPVFVGEGNCDLGITGLDQIKEAEQFDNIEDLLDLKFGSCKLQIQVPADGEYEKPEQLVGKKIVSSFTKLSTDYFKQLSDKPTNIRYVGGSVEASCALGVADAIVDLVESGETMKAAGLKAIETILETSAHLISSKKSKFPEMVNIIVQRLQGVLAAQEYVLCNYNAPKSIQAKCLTITPGRRAATVSTLDKHSDDEEDWVAISSMVNRKEIGNVMDELKKAGATDILVLEISNCRV | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of the enzymatic activity (By similarity).
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 32605
Sequence Length: 298
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
EC: 2.4.2.17
|
Q3AD54 | MKNGLTFALPKGTLFPDTVRLLYKAGFLKKEEVLLESRKLVIKDGPYTFIICRPTDIPTFVEHGAADLGIVGKDVIEEQRREIFELLDLKYGKCHFAVAAPRDNPKVHDLGKLTEVRAASKFPEVTRRFFKGLGVRAEVIKMHGNVELAPLVGLADVIVDLVSTGRTLRENNLIEITKIMDITARLVANRVAARVYDREIKAIVKKFKNLVGGEKNEVNLK | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 24764
Sequence Length: 221
Domain: Lacks the C-terminal regulatory region which is replaced by HisZ.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
EC: 2.4.2.17
|
Q9A2P5 | MSTPMIFAIPSKGRLKDQVEAWLADCGFKLEMTGGARGYSAELSGLPGVSVRLLSAGDIAAGLDSGDLHLGVTGEDLLRERGDDMDSRVMLLRALGFGRADLVVTAPKNWLDVDTMADVDEVGHAHLARTGRRLRVATKYVTQTRAFFARHGVADYRIVESSGATEGAPAAGAAELVVDITTTGATLAANGLKILSDGVILKSQAQLTASLTAGWNGEQLDALRRLLSVVEAKGRAGKLATLVWPAEQDRAAQDAVAAFIARGGSRRANGALLATADLFDAAAALAEAGVEPVTVSRPDYVFESRSAVLDRFAEALKSKI | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity).
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 33587
Sequence Length: 320
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
EC: 2.4.2.17
|
Q8KB10 | MSNNKVLKLGLPKGSLQDSTLELFANAGFHFSVQSRSYFPSIDDDELEAILIRAQEMGRYVSLGAFDAGLTGKDWIIETDADVVEVADLVYSKASMRPVRWVLAVPESSPIKTVKDLEGKHIATEVVNITKKYLAENGVNASVEFSWGATEVKPPELADAIVEVTETGSSLRANKLRIVETVLQSNTQLIANKAAWADPWKRKKIENMAMLLQGAINAQGKVGLKMNAPKAALDKIMSGIPALRQPTVSDLADKEWVALEVIVSEKIVRTLIPELKRAGAEGIFEYNINKLID | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 32103
Sequence Length: 293
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
EC: 2.4.2.17
|
Q2YAU4 | MTSITIALSKGRIFDDTAPLLKAAGIIPLDDPETSRKLILATNRDDVRLIIVRASDVPTYVQYGAADMGIAGKDVLLEHGGAGLYQPLDLNIARCRMMVAVRSDFDYESAVRRGARVRVATKYLQTAREHFAEKGMHVDLIKLYGSMELAPLVGLADAIVDLVSSGNTLKANNLKAVEEIMPISSRLIINQAALKLKRRAIQPMLEAFSAAITPLTPLSPYPLGATP | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 24596
Sequence Length: 227
Domain: Lacks the C-terminal regulatory region which is replaced by HisZ.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
EC: 2.4.2.17
|
A6Q469 | MLTIALPKGRIGEDSLALFEKIFDTKFEFGKRKLILEAGGFRFMKVRNQDVPTYVYHQAADLGIVGLDVLEEKRLDIMRLLDLGFGRCDICIGIKAEESLDFSKPSYKVATKMENITRDFFSKKAIPVEIIKLYGSIELAPLVGLADMIVDIVETGETMRQNGLKPALKIMESSAFLIANKNSFYQKKAQILHLREQMSKVLYGS | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 23131
Sequence Length: 205
Domain: Lacks the C-terminal regulatory region which is replaced by HisZ.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
EC: 2.4.2.17
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Q8ESR7 | MQPVTIALAKGRPAKQTIKLLQAAGLTFEELDATSRKLVFYNEDRTARVIFLKGMDVPIYVEKGAADIGIVGKDNIIESQAEVYELLDLGIGKCKFSIAAKQGVTLSSDNEITIATKYPIVAKRYFSKRNQSIDVVKLNGSVELAPLIGLADYIVDIVETGNTLRENGLEILEDIETISTKAIVNKASFATRSAEIQSIINRLSTVVG | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 22633
Sequence Length: 208
Domain: Lacks the C-terminal regulatory region which is replaced by HisZ.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
EC: 2.4.2.17
|
Q67KH5 | MSPITIALPKGRPYAATVRFLREAGLAGPELEPEEGRSLYVECPAQGTRFIIARDSDVPTYVEYGAADLGIVGKNVLMELEPQVYELLDLGYSQCRFVLAAPAGVDPRQLLSGRSRQRVATKYPRMTEAYFNSRGLQVETIFLHGSIEVAPKVGLADLIVDIVETGRTLRENNLVVVEELWTSSMRLIANRAAYRLRAERIGPMVQRLRELVSRRAVAANA | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 24515
Sequence Length: 221
Domain: Lacks the C-terminal regulatory region which is replaced by HisZ.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
EC: 2.4.2.17
|
Q9Z471 | MKTFDSLYEELLNRAQTRPEGSGTVAALDKGIHHLGKKVIEEAGEVWIAAEYETDEELAGEISQLIYWTQVIMVARGLKPEDIYKNL | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 9822
Sequence Length: 87
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
EC: 3.6.1.31
|
Q1LIB4 | MSDNLSQADILARVAATLESRKPENGGDPEKSYVAKLFKKGDDAILKKIGEEATETVMAAKDARAADLADEAVSKVVYEVADLWFHTMVLLARIGRTPEDVVNELARREGLSGLVEKASRKE | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 13301
Sequence Length: 122
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
EC: 3.6.1.31
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Q0K695 | MSDNQLSSNDVLARLAEVLESRKPANGGDPDKSYVARLFSKGDDAILKKIGEEATETVMAAKDARAAGQTGAEAGKVVYEVADLWFHSMVLLANFGLTPADVVNELARREGLSGLEEKARRKD | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 13235
Sequence Length: 123
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
EC: 3.6.1.31
|
Q9RWD6 | MTDLSELNFDPSGLIPVVTQDARSGAVLMQAYADRAAVERTLDTREATYYSRSRGEQWVKGQTSGHTQRVVSVHVDCDGDSLLYRVEQTGPACHTGEYSCFYRPLLEDDAPDTGLDGTLERVYATITERLATLPEGSYVARLHAGGLDRVLKKISEEAGEVLLAAKNADRAELATETADLLFHTLFALAEVGVSPADVAAVLQGREGKSGLKGPKEVG | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 23484
Sequence Length: 218
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
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Q9S5G3 | MLTEQQRRELDWEKTDGLMPVIVQHAVSGEVLMLGYMNPEALDKTIESGKVTFFSRTKQRLWTKGETSGNFLNVVNIAPDCDNDTLLVLANPIGPTCHKGTSSCFGDTAHQWLFLYQLEQLLAERKSADPETSYTAKLYASGTKRIAQKVGEEGVETALAATVHDRFELTNEASDLMYHLLVLLQDQDLDLTTVIENLRKRHQ | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 22841
Sequence Length: 203
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
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P06989 | MLTEQQRRELDWEKTDGLMPVIVQHAVSGEVLMLGYMNPEALDKTLESGKVTFFSRTKQRLWTKGETSGNFLNVVSIAPDCDNDTLLVLANPIGPTCHKGTSSCFGDTAHQWLFLYQLEQLLAERKSADPETSYTAKLYASGTKRIAQKVGEEGVETALAATVHDRFELTNEASDLMYHLLVLLQDQGLDLTTVIENLRKRHQ | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 22756
Sequence Length: 203
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
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Q2N8I9 | MNTLQRLEATIAARRNADPDSSYVARLNAKGLPKMAEKVGEEATETVIAALTGSDEELVGEGADLIFHLLVLLQARGVSLDQVLAELDRREGLSGLDEKAKRGD | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 11174
Sequence Length: 104
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
EC: 3.6.1.31
|
P60536 | MNERDDILQAVYEVILDRKGALPESSYTASLFHKGIDKILKKVGEEATEVIIAGKGGKREEIVYETADLLFHTLVLLGHYDIAPADVYNELRRRFGTSGHAEKASRNE | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 12103
Sequence Length: 108
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
EC: 3.6.1.31
|
Q7NLB5 | MAPHQFKSKGAPTLVHVREAARFDRDGLIPAVVQDVLDGTVLMVAWMNREALERTLETGESWFWSRSRQELWHKGATSGHRQKIKALRYDCDSDVLLLTVEQQGDIACHLGERSCFHRDEAGDYDLPPADTLSQVFRVVEERKAHPHPDSYTSRLLEAGSNKILKKIGEEATEVVMAAKDGERVAEEVADLWYHTLVLLAHADVDILDVYRALQQRRR | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 24795
Sequence Length: 218
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
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Q5FTN2 | MGKPATKPAPKPSKQQDDKKSDLQQELVLQRLYDTVQSRRGTDPSLSHSARLMARGRNKIAQKFGEEAVECLIEAVNGNRKELIGESADVLYHLIVMWVDAGVSPEDVWTELKRREGTSGIAEKAARPKEKLG | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 14781
Sequence Length: 133
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
EC: 3.6.1.31
|
Q0BPX5 | MMVKAVKKKTVTKINKKTSAPAAVKIKSRRLSPLADIDPDNAVQVLNRLWEVVMQRRDADPAVSHSARLLSRGIGKVAQKFGEEAVECLIEAVSGDKEALIGESADVLYHLLVLWVAVGVEPAEVWRELTKREGISGIAEKASRAKILPRAAGLKTTKIP | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 17413
Sequence Length: 160
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplasm
EC: 3.6.1.31
|
Q4K3E4 | MIRRPPLSLLDLEAAPLGSRWALTAVLDALPWNSDGLIAAIAQQHDSGEVLMLAWMNRQALGETLASGQACYWSRSRRCLWRKGESSGHRQRLIEARLDCDGDAVLLLVDQQGPACHTGRPNCFYNAIRDGAVEVISSPLKDSRHDS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 16205
Sequence Length: 147
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
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A0LTT2 | MTRRPSNLDPAIAARLKRDEHGLFPAVAQQYDTGEVLMVGWMDDEALHRTLTTGRCTYWSRSRQEYWVKGETSGHQQWVKSVALDCDGDTVLVKVDQIGAACHTGDRTCFDAGQLPAVVGEPPTPVGAGERQPASGTADAAP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 15380
Sequence Length: 142
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
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Q21U90 | MNWLDELKWDSQGLMPAIAQEQGSNDVLMLAWMNREALQKTAELGRAVYFSRSRNKLWFKGEESGHVQIVHEIRIDCDQDVILLKVTQTGHTPGIACHTGRHSCFYRVYENGEWKVTDPVLKDPQTIYK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 14919
Sequence Length: 129
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
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Q0VML6 | MFKHNEQQPEGFQISLKEALDNLAFNDAGLVAAIAQQHDSGEVLMMAWMNREAIEETLATGRVCYFSRSRGKLWRKGESSGQVQTLKELRIDCDGDALLVKVDQTGSACHTGRRDCFYWKADANNVTIDKAPIKDPKELYGK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 15938
Sequence Length: 142
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
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O82782 | MRTLSSQLYSNGGLTWFQKKNQSSLFIKHLRVSKPSRVQLISAVQFRPCIDIHKGKVKQIVGSTLRDLKEDGSVLVTNFESDKSAEEYAKMYKEDGLTGGHVIMLGADPLSQAAAIGALHAYPGGLQVGGGINSENCMSYIEEGASHVIVTSYVFNNGKIDLERLKDIVSIVGKQRLILDLSCRKKDGRYAIVTDRWQKFSDVILDEKSLEFLGGFSDEFLVHGVDVEGKKLGIDEELVALLGNYSPIPVTYAGGVTVMDDVERIKDAGKGRVDVTVGSALDIFGGNLPYKDVVAWHHKQHSLH | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 33365
Sequence Length: 304
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
Subcellular Location: Plastid
EC: 5.3.1.16
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O28329 | MELQFDEKGLIPVITQDVKTKEVLMLAYANEEAIKLTLKTGFAHYWSRSRKKLWKKGETSGNVQRVVEIRYDCDCDALLYLVEQKGNACHTGNYSCFYRRLEGDEVRC | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 12557
Sequence Length: 108
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
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A0JVK7 | MSEQPAPAPVPVLPAEVADALKRDAAGLVAAVVQQFDTNEVLMLGWMDDEALRRTMTSGRVTFYSRSRQEYWRKGDTSGHVQWVKSVALDCDGDALLVRVDQVGAACHTGTRTCFDGRGLPVVAGDAGAAGNAS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 14234
Sequence Length: 134
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
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A0PP21 | MTLDPNVAARLKRNADGLFTAVVQERGSGDVLMVAWMDDDALDRTLKTREATYYSRSRGEQWVKGATSGHTQYVHSVRLDCDGDTVLLTVDQVGGACHTGDHTCFDATVLL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 12146
Sequence Length: 111
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
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A1T8W8 | MSALDPAVASRLKRNADGLFTAVVQERATGQVLMVAWMDDDALARTLETREATYFSRSRGEQWVKGLTSGHTQRVHSVRLDCDGDTVLLEVDQVGGACHTGDHTCFDADLLLGPDL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 12631
Sequence Length: 116
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
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Q9K0H5 | MDKNLLEAVKFDEKGLVCAIAQDAETKRILMVAWMNAEALQKTVETGFAHYYSRSRQKQWMKGEESGHTQKVRALRLDCDGDAIVMLIAQNGGIACHTGRESCFYKVWRGSAWETADAVLKDEKEIYGSTH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 14787
Sequence Length: 131
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
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A9A5W9 | MDKTIDDIDFEKSGGLVPVIVQDANTKEVLTLAYSNRESLELAKKTRKSWFYSRSRNKLWMKGEESGNTQEIKEILVDCDSDAIIYLVEPSGPACHTGERVCFHNELK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 12282
Sequence Length: 108
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
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Q2YAV1 | MSDTWLNKVNWSADGLVPVVTQDAISNKVLMVAWMNPEALRLTAQTGEAHYWSRSRKKLWHKGEESGHVQKVKEIRLDCDEDVLLLVVEQVGGVACHTGRHHCFFKKLEQDQWLVTEPVIKNPEEIYGQR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 14963
Sequence Length: 130
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
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Q3J6Q0 | MSLGWLEDVAWNKEGLIPAIAQEDRTGQVLMLAWMNREALETTVQSGYAVYWSRSRKRLWRKGEQSGHEQIIKAIHLDCDSDAVLLLVEQKGGMACHTGRHRCFFKRLEKGNWASVEPVLKSPDSIYNNSDE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 15089
Sequence Length: 132
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
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A1R5S3 | MSEQSAPSPTPAAELSSDPASPLPQEIASALKRDSSGLVAAIVQQHDTNEVLMLGWMDDEALHRTMTSGRVTFYSRSRQEYWRKGDTSGHVQFVKSVALDCDGDALLIRVDQIGAACHTGTRTCFDGRDFTVVTGHRE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Sequence Mass (Da): 15052
Sequence Length: 138
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular Location: Cytoplasm
EC: 3.5.4.19
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P59520 | MIIPSIDLIEGNIVRLYQGNYDTKTFYQNNIYDIALKYYNQGAKIVHLVDLDGALCPNNKQTSLIKNLLNYFNFHIQVGGGIRSYKDVETLLLNGAKRVVIGSSAINNITEVEKWLLEFGYKSIVLALDVYVRNNGYKEVVINGWKNRSNVSLESVLERFSTLGIKYVLCTDVKKDGTCLGPNFTLYKNISKLFKNVCFQLSGGIGTISDVISAKKSGIKDIIIGRALLENKFSLLEAIRC | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 27005
Sequence Length: 241
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
Subcellular Location: Cytoplasm
EC: 5.3.1.16
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Q058A3 | MIIPSLDFIHGKIVRLYQGNYNNKISYKKDIFKQIEKYIYQGATYIHLVDLDGCNNPENRQKSMFNIFSNFKNVSFQVGGGIRSKRDIENLFHAGVSKIVIGTSAILYPNKFKKWLKNYGSKNFVLSVDININTKKENKIAIQGWKKTTEINLDDAIKQFIPYGLKNILCTDISRDGTFSGPNISLYKYLKNKFPNIVLQSSGGINSISDIYNLKKNNVEHVIVGRALLENKFTFLEASKCWLKE | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 28078
Sequence Length: 245
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
Subcellular Location: Cytoplasm
EC: 5.3.1.16
|
P62354 | MIVIPAIDLFDNCAVRLFKGNYEEKKIYSSEPWKLAESFAKNGATLLHLVDLNGARNQLGVNEDSILKIRETTSLKVQLGGGIRDKEKLAYYDKIGINRFILGTAAVTNPDLLKYALDNYGKERVVVAVDARDGIVKIAGWEKDSGIHYRDLLERLVKAGIEHIVFTDIAQDGTLAGPNLEAYREILNSYPFQVIASGGIASLKDLMDLSSLKTKISLYGVITGKALYEGKLDLAKAISSI | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 26492
Sequence Length: 241
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
Subcellular Location: Cytoplasm
EC: 5.3.1.16
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Q8Y9G4 | MQIFPAIDLKNGQCVRLFQGDFSKKTVVNEDPIAQAKAFATDGATYLHIVDLDGALEGRPINLEVIQKMKITAKIPVQVGGGIRSMAQVDYYLESGIDRVIIGSAALTDPDFLRAAVQKYGAKIAAGIDAKNGFVATRGWLDVSQVSYLDLAKRMEKVGVETIIYTDISRDGTLTGPNLEQMANLKEHVKVNLIASGGVSSRADLEALAQLGLYGAIAGKALYNHHISMSDIVEVEQIAY | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 25883
Sequence Length: 240
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
Subcellular Location: Cytoplasm
EC: 5.3.1.16
|
Q0AP83 | MILYPAIDLLDGRVVRLHKGAFDAVTDYGDDPMRVAEQFGEAGAVWVHIVDLSGARDGARRQGALIRSLCETGLRVQTGGGVRSAEDIEDLLAAGVERVIIGSLAVTDTNRVAGWLQNYGGDRITLALDVRQIGGQYRPALKGWTDMADTTLDDVISAYEGTGLAHALVTDIGRDGDLSGPNIALYKRLATDYPNIDWQASGGVSSLDDLRAARAAGAAGAITGKALYEGRFTVGEAIACLRDA | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 25788
Sequence Length: 244
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
Subcellular Location: Cytoplasm
EC: 5.3.1.16
|
Q8TU55 | MAFEVIPAVDMRGGKCVQLVQGVPGSEIVSLNDPLAVALDWIGKGAKTLHLVDLDGAIEGERKNAPIIEKIVQACREKGVSIQVGGGIRSFEDAASLLELGVSRIILGTAALQNPELVKQLSDAFGSSCVNVALDAKNGKISIKGWTEECAQTPVEMGREFEELGAGSLLFTNIDTEGLMQGVNPGPTRELVESVSIPVIASGGVSSLEDLKVLKQTGASGVVVGSALYTGRFTLEAAIETIRND | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 25614
Sequence Length: 245
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
Subcellular Location: Cytoplasm
EC: 5.3.1.16
|
Q0W0J3 | MSFNVIPAIDLKGGKCVQLVQGVPGTEMVSIDDAVEVAAGWVGQGAKTLHIIDLDGAFSGSRKNAYIMEDIVSKFDVDVQVGGGIRDYETAKYLLSLGIDRVILGTAAIKNPDLVRQLADEFGSETVMVSLDSKQGEVVIEGWTESSGKTTNEMGKFFSEIGAGSILYTNVDVEGLLKGVNEDPVRSLVNSVTIPVIASGGVAKIDDLVKIKNTGAAGVVVGSALYKGLFTLREAIDKVS | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 25255
Sequence Length: 240
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
Subcellular Location: Cytoplasm
EC: 5.3.1.16
|
A9GB86 | MQLIPAIDLLGGQAVRLHQGRYDQVTVYDQDPAALAARLRRACARLHVVDLEGARAGLPVQADAVRAVIAAFGAEGGSVQVGGGIRSAAAAESYLALGADRIVLGTAAVNDPALVRDLAGRFPGRVVVAVDAKDGRVAVQGWEQVSSVTALDVARALAGAPVAALLYTDVSRDGTQVGPNLEATRELAASCGFPVLASGGVGSLAHLRALAQIPGVSGVIVGRALYEGAFTLAEAIEAASA | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 24377
Sequence Length: 241
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
Subcellular Location: Cytoplasm
EC: 5.3.1.16
|
Q8KF56 | MVFIADYGAGNLRSVHKAFDYLGIEAVVSDKASEMSRYDKVLIPGVGAFGPAMEALNRQGFDEAIREHIDKGRSVLGICLGMQLFLSESEEMGAYKGLDIVPGKVLRFTSSTDKIPQIGWNSVDYCKDSVLFRNVPDQSYFYFVHSYYCAPDEPESVAATTFFAGKKFCSAIEKNGIFAVQFHPEKSSEAGLQVLKNFAEF | Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
Sequence Mass (Da): 22259
Sequence Length: 201
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Subcellular Location: Cytoplasm
EC: 4.3.2.10
|
Q97KI0 | MNKKIAIIDYDMGNLLSVKKAFDYIGANSFITSDSKEIEKSDAIILPGVGAFPDAMSSLKENGIDKTIINEAKNGKPFAGICLGMQLLFDESEEVTNTKGLGLIGGKIRKMKTEFKIPHMGWNSLNIPRECNILKGVSKGSYVYFVHSYYAELADKNNLNAYCDYGTKLPAVVSYKNIFGIQFHPEKSGEIGLTILKNFWELI | Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
Sequence Mass (Da): 22518
Sequence Length: 203
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Subcellular Location: Cytoplasm
EC: 4.3.2.10
|
Q6A8L2 | MSDPVRVGIIDHGSGNLHSARRALRQVGAEVIVSNDPSALLDTDALVLPGVGALAVCMTGLRAMGGARLVRQWVDEGRPLLGICVGHQMLFERGRERDVDVKCLGVLPGVVEELPAERLPHMGWNTVTPATDSALFQGVQERFYFVHSYGVVVTGPHDHFTTATHQGATFVAAAEYGPVTSTQFHPEKSGIAGLALLTRWLNQLS | Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
Sequence Mass (Da): 22013
Sequence Length: 205
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Subcellular Location: Cytoplasm
EC: 4.3.2.10
|
Q9TLQ8 | MKNIGIINCGMGNLHSVSNAISNIGFNPVIINASKDLVSFACSALVLPGVGSFDLAIDRLEKKNLIEPVKLWIQEDRPFVGICLGLQLLFEGSDEGSKPGLKIFNGYVSQFKHSLVKKVPHMGWNKLYFNRFNTIDNLVPHYFHYDLQPWAYFVHSYYIEPKDCYTFNTTSLTFYGKQKIVSSISYNNILATQFHPEKSGLFGLFILKRFLSSY | Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF (By similarity).
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
Sequence Mass (Da): 24305
Sequence Length: 214
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Subcellular Location: Plastid
EC: 4.3.2.10
|
Q85FY4 | MKVGLVDYSMGNMHSVSRAIQQANQQVCVVRSESELAQVHILVVPGVGHFDLAMKKLEQKGLRTGIAKWIAKGNPYIGICLGMHILFETSEEGKEEGLGVYKEQVKRLPVKVIPHMGWNRLECQNSECQNSEWVNWKAWPNAWAYFVHSYGVMASSQACATTTYEKIQMVAAIEKDNCFAMQFHPEKSGEFGLWLWREVMKKAASL | Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
Sequence Mass (Da): 23294
Sequence Length: 206
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Subcellular Location: Plastid
EC: 4.3.2.10
|
P48262 | MINSKNNSPIEISIIDYQMGNLYSVCKGIERSGGIPKIINSAEEIKKATALILPGVGSFDPAMKQLKKQDLINPIKDAISEKKPFLGICLGLHLLFEESEEGIESGLGILSGSVKRIKNEPEITIPHMGWNQLQLTNPKCYLWDGLTKYPWVYFVHSYFAQPKNPNVIAAAVTHGTQQVTAAIQYENISAVQFHPEKSASIGLHMLNNFVQQSCN | Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF (By similarity).
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
Sequence Mass (Da): 23795
Sequence Length: 215
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Subcellular Location: Plastid
EC: 4.3.2.10
|
Q3Z7F2 | MIALVDYGGGNLKSVANAIHALGYEFKLTSSPEEILSAEAVILPGVGAAADTMAGLQSKGLDKAIKELVARDIPLLAICVGMQVLFDYTAEGDNTKCLGILKGDVKRLPEGLKIPQMGWNQLKQRVSHPIFEGIPDGIDFYFVHSYYASPADPGIIGATTDYGVDFCSLVISKRLIATQFHPEKSGSYGLKLYQNFFKMALGDKK | Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF.
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
Sequence Mass (Da): 22132
Sequence Length: 205
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Subcellular Location: Cytoplasm
EC: 4.3.2.10
|
Q7MPK7 | MRVYRMLRSRVIPVLLMREKGLVKTVKFKEGKYVGDPLNAVKIFNEQEADELTLLDIDASRLGHEPDYVLIERIASECRMPLCYGGGIKTVEQAERILKLGVEKVSLSSAVFENPKIITQLAERVGRQSIVVCLDVKKRLFGSKFDCFTINGTKKQSVDTIEFVKQIQTLGAGEIVLNFIDNDGVMKGYDLDAVSKFKALVKVPLTVVGGAGCVDDIAKLVQQEKLVGAAAGSLFVFKGKYKAVLINYPSPSEKKKALEL | Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit (By similarity).
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
Sequence Mass (Da): 28730
Sequence Length: 260
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Subcellular Location: Cytoplasm
EC: 4.3.2.10
|
B9DHD3 | MGVINVQGSPSFSIHSSESNLRKSRALKKPFCSIRNRVYCAQSSSAAVDESKNITMGDSFIRPHLRQLAAYQPILPFEVLSAQLGRKPEDIVKLDANENPYGPPPEVFEALGNMKFPYVYPDPQSRRLRDALAQDSGLESEYILVGCGADELIDLIMRCVLDPGEKIIDCPPTFSMYVFDAAVNGAGVIKVPRNPDFSLNVDRIAEVVELEKPKCIFLTSPNNPDGSIISEDDLLKILEMPILVVLDEAYIEFSGVESRMKWVKKYENLIVLRTFSKRAGLAGLRVGYGAFPLSIIEYLWRAKQPYNVSVAGEVAALAALSNGKYLEDVRDALVRERERLFGLLKEVPFLNPYPSYSNFILCEVTSGMDAKKLKEDLAKMGVMVRHYNSQELKGYVRVSAGKPEHTDVLMECLKQFY | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 46635
Sequence Length: 417
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
Subcellular Location: Plastid
EC: 2.6.1.9
|
A1TL06 | MLAKRIIPCLDVTGGRVVKGVNFLELRDAGDPVEIAARYNGQGADELTFLDITATSDGRDLILPIIEAVASQVFIPLTVGGGVRTVEDVRRLLNAGADKTSFNSAAIANPEVIDAASAKYGAQCIVVAIDAKRRTPEEAARPGPDGAPRGEGWDVYSHGGRKNTGLDAVQWAAEMARRGAGEILLTSMDRDGTKSGFDLALTRAVSDAVSVPVIASGGVGGLDDLADGVQQGGADAVLAASIFHYGEYTVAQAKERMAARGIPVRL | Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
Sequence Mass (Da): 27684
Sequence Length: 266
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Subcellular Location: Cytoplasm
EC: 4.3.2.10
|
Q6F799 | MLAKRIIPCLDVDNGRVVKGVQFLDIRDAGDPVEVARRYNEQGADEITFLDITATHHGRDTTYRTVERMAESVFVPLTVGGGVRKVEDIRLLLNAGADKVSINSAAVFNPEFVQEASQRFGAQCIVVAIDAKKTGDNTWEIFTHGGRKPTGIDALEWSVKMAEYGAGELLVTSMDADGTKAGYDIALMREINNRVSIPTIASGGVGNLQHMADGILKGGADAVLAASIFHFGQHTIPEAKQFLAAQGIEMRL | Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
Sequence Mass (Da): 27183
Sequence Length: 252
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Subcellular Location: Cytoplasm
EC: 4.3.2.10
|
B2UL23 | MRNASCKRVTGETDISMELNLDGTGCAAVATGHAFFDHMLDLLARHSLMDLTLQARGDLEVDAHHTVEDVGIVLGECIKNALGDKKGIVRYGCSYLPMDETLTRVVMDLSNRPYVAFRIPEGGLPDAPNFPLTLCEEFCRALANNLRCNLHVEVLYGRDGHHIAESVFKGIAHALRQAAAIDPRAAGTLPSTKGML | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21299
Sequence Length: 196
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplasm
EC: 4.2.1.19
|
Q5WDH9 | MARSYELTRTTGETDISLRLNLDGEGKADIETGVPFMEHMLDLFAKHGQFDLFVKASGDIEVDAHHTTEDLGICIGQAVKEALGTKEGIKRYGNAFVPMDETLAQVVVDLSNRPHLEFRADFPSQKVGTFDTELVHEFFWKLALEARMNLHIIVHYGHNTHHIIEAIFKACARALDEATAIDPRIKGILSTKGLL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21756
Sequence Length: 195
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplasm
EC: 4.2.1.19
|
A6TKT3 | MTRSYRGDRRTKETDIELILNLDGKGQGKIATGIGFFDHMLEQIMKHGQLDLELKAVGDIEVDFHHTVEDVGILMGKAIAEALGDKKGIVRYATAFIPMDEALSMVSMDISGRPFLQYGVNYSGEFVGQFEVQLVEEFFRALAFNSGITLHIQTQYGRNNHHIVESIFKAFAKALREAITIDPRIEGVLSTKGSL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21736
Sequence Length: 195
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplasm
EC: 4.2.1.19
|
Q2INV5 | MTRRAAVKAPRAGAAARRGSVARRTKETDVAVDLRLEPGEASISTGLPFFDHMLDQISRHGGMALTVRAEGDLQVDAHHTVEDVGIGLGEALRQALEDKAGLARYGHAVVPLDEALVEAVVDLSGRPHLTFNAKLPSGKKFIGGYDVDLTQDFLQALVNHARICVHVNVRYGRNLHHVVEAIFKATARALRAATAREGTALPSTKGTL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 22307
Sequence Length: 208
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplasm
EC: 4.2.1.19
|
Q2VYI7 | MRKAAITRNTNETSIKVAVDLDGSGKYAVSTGVGFLDHMLEQLSRHSLMDLEVDAKGDLHIDAHHTTEDVGIAIGQAVNQALGDRKGICRYGSAYVPMDEALTRVALDLSNRPYLIWKVAFGRDKLGTMDTELFKEWFQAFAQAAGATLHVESLYGDNDHHIVESCFKALARALREAVEIDPRKADAVPSTKGTLGGSL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21670
Sequence Length: 199
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplasm
EC: 4.2.1.19
|
P58878 | MRTGRISRKTKETDIQLELNLDGKGVADISTGLGFFDHMLASFSRHSEFDLKVRAEGDLYVDEHHLVEDVGIVLGRALAEVLGDMSGIARFGEARIPMDEALAEVALDVGGRNYLVLKAEFASPQVGQFSTQLVRHFFETLASNAKITMHASVYGDNDHHKIEALFKAFAYAMKRAVKIEGKEVKSTKGTL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21069
Sequence Length: 191
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplasm
EC: 4.2.1.19
|
A7I774 | MNVSLARETKETKIALTFDPEGTGKVAVETGIPFFDHMLTGMARHGGFDLTCTVTGDLGVDSHHTIEDTGIVLGDAIKAAIGEGRGIRRFAHAIIPMDESLAQVALDCGGRGYLVYTGTFGARTLGNIPPDLFEHFFYTLCIHAGITAHIRFTGRNDHHQCEAMFKAFGIALGEALAKSGKTKEIPSTKGTF | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 20597
Sequence Length: 192
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplasm
EC: 4.2.1.19
|
Q12WC5 | MRNAKITRKTKETDIQMELELDGTGSSNIDTGIGFFDHMLTSFAKHGNLDLIIEATGDLIVDEHHLIEDTAIVLGQALSEALGDKDGIARFGDARIPMDEALADVVLDLGGRTYLVMKAEFEAPRVGEMNTQLVRHFFESLTDNSKMNLHIAVTGYNDHHKIEALFKAFAYALRRAVKIEGEGIKSTKGVL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21072
Sequence Length: 191
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplasm
EC: 4.2.1.19
|
Q1AX09 | MARVGELERKTGETFVRVRLEVDGEGRADVSTGVGFLDHLLHLLAHHSGMDLEVRAEGDTWVDDHHTVEDTGLVLGRALDQALGDRSDLVRFADASVPLIEALSTAAVDLGGRSHLTCNTGPLPEKIGTFDTELFPEFLRAFTQYGRFTLHLNCHYGHNAHHKVESGVKALAVALRAAVSRRSSGTASTKGVVD | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 20990
Sequence Length: 194
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplasm
EC: 4.2.1.19
|
Q1GF01 | MRTAQVSRSTAETEISVSVNLDGSGTYDNQTGVGFFDHMLDQLSRHSLIDMTIRAKGDYHIDDHHTVEDTGIALGQALVQALGDKKGINRYGECHLPMDDAQVRAALDLSARPFLVWNVDLPTQKIGSFDTELVREFFQALATHGGITLHIDQIHGVNSHHIAEAAFKAVARALRTAVEVDPRKADAVPSTKGAL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21238
Sequence Length: 195
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplasm
EC: 4.2.1.19
|
O33773 | MSRSANITRETKETKIEVLLDIDRKGEVKVSTPIPFFNHMLITLLTYMNSTAIVSATDKLPYDDHHIVEDVAITLGLAIKTALGDKRGIKRFSHQIIPMDDALVLVSLDISNRGMAFVNLNLKRSEIGGLATENVPHFFQSFAYNSGITLHISQLSGYNTHHIIEASFKALGLALYEATRIVDNEIRSTKGII | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21437
Sequence Length: 193
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplasm
EC: 4.2.1.19
|
A4X9Q4 | MSRTARVERVTKETKVLVEIDLDGSGKADIETGVGFYDHMLHQIARHGGFDLTVHTVGDLHIDAHHTMEDTALALGSAVDRALGDRAGIRRYGSATVPMDEVLVRAAVDISGRPYVVHDEPPLAPYIGPVYPTSMTRHVWESFGQSARVTLHVDVLRAARPGGHPDAHHVVEAQFKAVSRALREATAVDPRFTGVVPSTKGTL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 22010
Sequence Length: 203
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Subcellular Location: Cytoplasm
EC: 4.2.1.19
|
Q9PII2 | MKFNEFLNNLSNYEPGKDIEVIAKEYGVKEVIKLASNENPFGTPPKAIECLRQNANKAHLYPDDSMIELKSTLAQKYKVQNENIIIGAGSDQVIEFAIHSKLNSKNAFLQAGVTFAMYEIYAKQCGAKCYKTQSITHNLDEFKKLYETHKDEIKLIFLCLPNNPLGECLDASEATEFIKGVNEDCLVVIDAAYNEFASFKDSKKHLEPCELIKEFDNVLYLGTFSKLYGLGGLRIGYGIANANIISAFYKLRAPFNVSNLALKAAVAAMDDDEFTEKTLENNFSQMELYKEFAKKHNIKIIDSYTNFITYFFDEKNSTDLSEKLLKKGIIIRNLKSYGLNAIRITIGTSYENEKFFTEFDKILR | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 41368
Sequence Length: 364
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
B3PCJ2 | MSKFWSPVVRALEPYVPGEQPQIDGLIKLNTNESPYPPSPKVLELMTHDAIDRLRLYPDPDSKKLKATIASYHNISPEQVFVGNGSDEVLGLLFMAFFQQGKAVLFPDITYSFYPVYCKLFNIDYRTVPLNDNFDIDFNDYPQDNSGIIFPNPNAPTAIGKPLAEIEALLQRNSETVVVVDEAYIDFGGQTAIALIGKYPNLLVVQTLSKSRALAGMRVGFAAGHKDLIAGLDRVKNSFNSYPLDRLAEAAAVVAFEDDSYFKRCCNKVIATRDYTVRELEKLGYQVLPSQANFVFAAPPAGNAAEIAQYLRDHKILVRYFNKPRINQFLRITIGTDEQMQKMIEVLQQY | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39334
Sequence Length: 350
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q2SBJ7 | MSVKDRILQWVRPEVQALSAYHVADASGLIKLDAMENPFDFPAALKAELGVDLRDAAINRYPDPDAGAIRTALRELYSLPASADMLFGNGSDEIIQILAMAVAGPGRTILSVEPSFVMYKMIATFIGAEYVGVPLNDDFQIDAQTTLDAIKRHQPALVFIAQPNNPTGNLFDDETLRQIVAASPGLVVIDEAYTAFTNADYMSWVSEYDNVVVMRTFSKVGLAGLRFGMLFGAQEWIEQLNKVRLPYNINCLTQNAVLTAIRHFPEFVKQTEALREQRSWLSAQLDGVAGVTVYPSEANFILVRVDLPAKSVFSEMKRRGVLIKLLDGGHPKLAGCLRLTVGSHEENEAMLKALSGALAAVRG | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39773
Sequence Length: 363
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
B9LNJ8 | MQPRDLSDHSPYVPGRGVEEVARDRGLDPDDLIKLSSNENPHGPSPAAVDAIREHADRVHQYPKSSHTDLTAKLAEKWDVSTEQVWVSPGADGSIDYLSRAALEPGDEVLVPEPGFAYYAMSARYHHGEVSEYALSPDDGFAQDAETVLSAYGGERIVYLTSPHNPSGSVMPLDEVRAIADATAEETLVVVDEAYGEFAEVDSAIPLVDERDDVAVLRTFSKAYGLAGLRIGYSVVPEAWGEAYARVNTPFAANELACRAALAALDDEEHVAESVETARWAREYIADELDAPTVESAGNFVLAEVGDAERVAEEAQERGVIIRDCTSFGLPNHVRISTGTREGTREAVARLNETLADLGLGVRA | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39332
Sequence Length: 364
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
P17736 | MQPRDLSAHAPYVPGRGTEEVARELGMDPEDLTKLSSNENPHGPSPKAVAAIEDAAPTVSVYPKTAHTDLTERLADKWGLAPEQVWVSPGADGSIDYLTRAVLEPDDRILEPAPGFSYYSMSARYHHGDAVQYEVSKDDDFEQTADLVLDAYDGERMVYLTTPHNPTGSVLPREELVELAESVEEHTLLVVDEAYGEFAEEPSAIDLLSEYDNVAALRTFSKAYGLAGLRIGYACVPEAWADAYARVNTPFAASEVACRAALAALDDEEHVEKSVESARWSRDYLREHLDAPTWESEGNFVLVEVGDATAVTEAAQREGVIVRDCGSFGLPECIRVSCGTETQTKRAVDVLNRIVSEVPTA | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39418
Sequence Length: 361
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
B4U9L1 | MFSKRIKLLKAYKTETTPCHIKLSSNENPFDLEESVKLELLEVIKNIEFNRYPDPHATKLRQTLSKLYEVEPENIMVCNGSDEAIQYLMLGIGELDEGVLIPRPTFPMYEVIANALGKPIYDVDLDENFQMNKQTLQKALEKKPSIAFISNPNNPTGNLFRDEDIALIRKHTFTVVDEAYYDFCGKTYIKDAIKDDNMAVMRTLSKIGLASLRVGALIGTKEFIREISKLKMPFNVSYTSQAMADYIISNHIDNIKNQIKVLIDERHRLKEALSDIKGIKVYDSCANFFLIKVNDADFIHKSLIQKGILTRNISYLPNLENHIRISIGKKEENDALINALKEIAQQVYL | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39924
Sequence Length: 349
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q0C348 | MSKPISQIEPLPHIAATKPYVPGGKLHGAKGAVAMLASNENPFGPSPKAVEAAKAAAANVHVYPDPDYGPLRAAIAAAKGIADASRVVTSAGSDEIIHLLTQCYAGPGDEVLFTEHAFSMYRVSAGAHGATSVTVPETDMTAGVNAILGAVSPRTKILFLANPNNPTGTMLSVDELKALQDALPPHVLFVVDGAYSEYLGPDYEAQLRDLVDRRDNTVMMRTFSKIYGLAAMRLGWAYMPAGIAAIYQRIRGPFNVSSIAAAAGIACVGDEAFLKMSRDHNTHWRAIMTDALNAMGLPTPPSHANFIVTEFGSDERAAAANQHLKDNDILVRAIGGYGLPTKLRISVGSADDNQRFLDALKAFTASR | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 38865
Sequence Length: 367
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q02135 | MSWQNNLRSVSPYIAGEQPELTDIIKLNTNENPYPPTSVAQLFNERYKTKNLRLYPSTDAKSLRKKLADYHHLEVEQVIIGNGSDEVLSLSFLTFFNSQSPLLMPDITYSFYPIYCELYRIPFQKVPVDDDFKVLIKDYCIENGGIVIANPDAPTALALNLKDIEEILKKNQNSIVLINEAYIDFGGETCLPLLKKYDNLVVVQTFSKSRSLAGIRLGVAYGSAEAISHLYDVKNSFNSYPIDSLAQIIGEASLMDEHYFQKNIQKIIKTREVFKDNLVNLGFEVTDSKANFVFVHHPKVKAEELFKALYEAKIIVRHWNQPRIDDWLRITIGTNKEMNKVIEFLKGYLKKNEEIDEWKK | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 41401
Sequence Length: 360
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q88UE6 | MKASIEQLEPYVPEKPLATLQAELGLTELVRLSANENPYGTSPKVATAVKNWDFTQSNRYPDADAQELRQAVAQQQGIDPNSIVFSVGLDEMIVMLSRTFLATNDQVLVSAPTFSEYGLHAEIEGGQLISVPTLPNDHVNFEGLMKAITPHVKMVWLCNPNNPTGTVESLAAIEAFVQQVPPETMVLIDEAYIDFTPGAAQVTAMQLPAKYPNVVVMRTFSKAYGLANFRIGYAVFNTKYAATMQTIRLPYNVNSLAQVAALAAIDDPNFVKQTVQKNATERAKWMAFFDDQGVTYDQSGANFIFFKYPSATQLADYLVHHGYLIRTGLRPGWLRLTVGTANDNQQLQQLIREFKA | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39431
Sequence Length: 356
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q49VS0 | MKKQIEQLSAYEPGLSPRALKENYGIKGELHKLASNENLYGPSPKVKEAIQAHLDELQYYPETGSPLIKEAISKHLNIDPARILFGAGLDEVILMISRAVLTPGDKIVTSEMTFGQYYHNAIVESANVVQVPLQNGEFDLDGILSEIDNDTKLVWLCNPNNPTGRYFTHDALRNFLERVPSHIPVIVDEAYVEFATAKDFPDTLALQQEFENAFLLRTFSKAYGLAGMRIGYVIAAKEAIEKYNIIRPPFNVGRLSEYAALAALEDQEYLASIRERNAEEREKFFELSQSDHFYPSQTNFVFVKTDKPHELYEALLNVGCITREFPNGVRITIGFPEQNAKMREVLAQFTL | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39696
Sequence Length: 351
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q82AA5 | MSFGIDDLPVRDELRGKSPYGAPQLDVPVRLNTNENPYPLPEPLVERIAERVREAARHLNRYPDRDAVELRTELATYLTNTGKHPVGIENVWAANGSNEVIQQLLQTFGGPGRTAIGFEPSYSMHALIARGTGTAWISGPRGEDFTIDLAAARQAIAESRPDVVFITTPNNPTGTAVPPETVLALYEAAQAVKPSMVVVDEAYIEFSHGDSLLPLLEGRPHLVVSRTMSKAFGAAGLRLGYLAAHPAVVDAVQLVRLPYHLSAITQATALAALEHTDTLLGYVEQLKAERDRLVAELRAIGYDVTESDANFVQFGRFADAHEVWQQILDRGVLVRDNGVPGWLRVSAGTPEENDAFLDAVRELKKEQNA | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 40311
Sequence Length: 369
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q8DTQ4 | MIRGLRQIEPYVAGVQPAERKMIKLNTNENAYGASPKVREALANFDVDNLRKYSTLEQADLRAALANNLKVKPEQLMIANGSDDVLSIAFLAFFNNDEPVLFPDLTYGFYKVWADLYRVNYHEIPLAEDFTINTEDYLADNGGIILTNPNAPTGIYKPLNEIEKLLKANQDTVVIIDEAYISFGGQSALSLLNKYNNLVITRTFSKDAALAGLRVGYAIANEPLIAVMNAVKHSINPYSVDLLAERLATAAVEDWSYYQENAKKIQKTRAWFSEQLVKQGFDVLPSQANFVLTKPHDLATAKLFEELEARKIYVRYFPKVERIKDYLRISMGTQEEMEEVVKAIEEIRG | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39443
Sequence Length: 349
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q9RI00 | MSADFLALAVPGVQKLSPYVTGKPIDELARELGIEPARIVKLASNENPLGPNPRVLEAVRGELSELTRYPDGSGFRLKAKLAERFGLKSEQITLGNGSNDIIDLVARCCGAGPNAVFSAHAFAAYPLCTQAAGAESRVVPAVDYGHDLDGMLKAIDEQTAVIFIANPNNPTGNLVRAQALESFLDRVPERVLVVLDEAYIEFYRGTNCQRLNYLVRYPNLLVSRTLSKVYGLAGLRVGYSASSPQIADVLNRVRQPFNVNSLALVAACAGWMTSSIWLKGGGWIAPVWELEQGLAELRLKWIPSRGNFLAVDLGRDAAPINAGLLRDGVIVRPIAGYDCPTFLRVSIGTEQENARFLEALRVVLDQ | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39700
Sequence Length: 366
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q67KI2 | MSSVRTAVRRMKPYVPGKPVEDVQRELGLHDLVKLNQNENPLGPSPRAVAAARAAMAQVHTYPEGTARRLRERLAQMWNLPADWFLIGNGSDEVFRLLAEVYLEPGDRVVVPEPSFAAYRFVAELMGAEVVAVPLAGWTMDLPAMAEAAARGAKLLFLCRPNNPTGTVFAEADLRAALERVPPSTLVVVDEAYREFDETPFDSRALVQDYPNVVIARTFSKIYGMAGFRLGYGVMRPEVLAPLYTARDPFSVNGLAVAAGLAALDDVEHVERTRALTREGKAYLYAAFQRLGLGYVPSEANFVLFDAGRPAAEVFDALLRRGVLVRPCGSFGLPDHLRVTVGTPEQNRRFVEALKAALGEG | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39538
Sequence Length: 361
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q2LST8 | MNAKGESMLSRRLEALTPYVPGEQPRDRKYLKLNTNENPWPPSPRIEALLREYDPDQLRLYPDPWSLSLRQKIARKYSVDVDNIFVGNGSDEILSFVWYAFFDGLYGKLVFPQFTYSFYPVYCDFYEIPYRRIPLRPDFTLDLEAMIENGGEPSCGMAFPNPNAPTGIALTLKQIEDLLNRYPTDRVVVIDEAYIDFGGESAVGLIDRYANLLVARTFSKSFSLAGLRLGYALGSPELIRALFVTKDSFNSYTVGRLTQTIGEIAIEDEAWFAEKIARIIEARDFFSEELKGQGWQVLPSKANFVFVRKPGLTGQTIYETLKERGILVRYFNVEGIRDFVRVTIGKREDMARLLEELKRLF | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 41437
Sequence Length: 361
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
|
Q5NAY4 | MSLRPGRAHPLAASPLHTPLPARPRPQLRLSTSTSCAAMKSYRLSELSDAEVGGLKARPRIDFSSIFGTVNPIVEDVRMRGDAAVKDYTVKFDKVALDDVVVRVSDLPDVELDPAVKEAFDVAYDNIYAFHVSQKLPEKTVENMKGVRCKRITRCIGSVGLYVPGGTAVLPSTALMLAVPAQIAGCKTVVLATPPSRDGSICKEVLYCAKKAGVTHVLKAGGAQAISAMAWGTVSCPKVEKIFGPGNQYVTAAKMILQNSEAMVSIDMPAGPSEVLVIADKYANPVHVAADLLSQAEHGPDSQVVLVVAGDGVDLGAIEAEVSKQCSALPRGEFASKALGHSFTVFAKDMVEAISFSNMYAPEHLIINVKDAEQWEDLVENAGSVFLGQWTPESVGDYASGTNHVLPTYGYARMYSGVSLNSFLKYITVQSLSEEGLRSLGPHVAKMAEVEGLEAHRRAVTLRLQDIEATVTV | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Catalytic Activity: H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH
Sequence Mass (Da): 50566
Sequence Length: 473
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
Subcellular Location: Plastid
EC: 1.1.1.23
|
Q6D411 | MADNTNSTGSFSTLVDWQRCSVEEQRQLLTRPAISASDRITAVVSDILTNVKSRGDGALRDYSAQFDKVQVDAIRITDAEIAAASARLGDEVKQAMAIAVRNIETFHNAQKLPIVDIETQPGVRCQQITRPIATVGLYIPGGSAPLPSTVLMLGTPSRIAGCRRVVLCSPPPIADEILYAAQLCGIKEVFQLGGAQAIAAMAFGTDSVPKVDKIFGPGNAYVTEAKRQVSQQLDGAAIDMPAGPSEVLVIADSGATPAFVASDLLSQAEHGPDSQVILLTPDAVMAKAVADAVEEQLTQLSRADIARQALASSRVIVARDLAQCIEISNQYGPEHLIIQTRDAESLVDSITSAGSVFLGDWSPESAGDYASGTNHVLPTYGYTSTYSSLGLADFQKRMTVQQLTPQGLLQLAPTIEILAQAEQLTAHKNAVTLRVAALKEQA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Catalytic Activity: H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH
Sequence Mass (Da): 46850
Sequence Length: 442
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
EC: 1.1.1.23
|
Q4FNE2 | MIKILDSKNKNFDKTLDALLSKRKNKVQLNSVSVIKIIKDVKKNGDKAILKYEKRFNKNSIIAPSIKQINRAIQSLDQKVKKAIDLAYDRIYKFHSLQKFKNISYTDKLKNKLEYKYVPIESVAIYVPGSTASYPSSVLMNAVPAIVAGVKRLVMVNPGQKGKQNPAVLYAAKKCKIKEIYSIGGPSAIAAVAYGTKKIKKVDKIIGPGNSYVAAAKKEVFGDVGIEGMIAGPSEVTIVCDKFSNPEWIASDLIGQAEHDNLAQCILISKDKSIIKKVNYEIINQLKELPRAVIAKNSLLNNGILIYMPSDQKIINTVNKIAPEHLELNTKNYKKVVSKIKNAGSICLGKYAVMAMTDYNVGSNHVLPTNSSARYSSGVSVNEFYKRISYINLSKKGIETLGPSVITLANYEGLVGHAKSVEKRIRRK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Catalytic Activity: H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH
Sequence Mass (Da): 47310
Sequence Length: 428
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
EC: 1.1.1.23
|
Q7VA26 | MSERKQILNCIDDPQQALIMLKRISARTSLEVQENAISSVQNILTEVKQLGDEALFRLTEKFDGFIPKPLEITPEQTLEAWEKTPTPLQEALQLAKNRIEAFHKYQIPKDFLKEGIHGELLGKNWSPVEKAGIYIPGGRAAYPSTVLMNAVPALVAGVNEIIMVSPAGPNGQLNRTVLAAAYIAGIKKIFRIGGAQAIGALSYGTQTIPRVDVISGPGNLYVTLAKKLVYGQVGIDSLAGPSEVLIIADHSADVEQVATDLLAQAEHDPLAASILLTTESNLAKKINLEIENQLKDHPRSAICRKSLKDWGLIVICKDIKSCAALSNSFAPEHLELLIEKPFEFISQIKNAGAIFLGEWSPEATGDYLAGPNHTLPTSGTARFSSALSVETFMKSTSIINFNQAALNKTSAAIMELANSEGLHSHSRSIEIRRSKPSSDD | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Catalytic Activity: H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH
Sequence Mass (Da): 47721
Sequence Length: 440
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
EC: 1.1.1.23
|
Q9HVW9 | MTAPFAIRRLNAADPDFGRHLDHLLSWESVSDDSVNQRVLDIIAAVRSRGDAAVVEFTQRFDGLQAASMADLILPRERLELALTRITVAQREALEVAAERVRSYHEKQKQGSWRYTEADGTVLGQQVTPLDRAGLYVPGGKASYPSSVLMNAIPAKVAGVSEVVMVVPTPRGEINEIVLAAACIAGVDRVFTIGGAQAVAALAYGTESVPRVDKIVGPGNIYVATAKRHVFGQVGIDMIAGPSEILVVCDGQTDPDWIAMDLFSQAEHDEDAQSILVSPDAAFLDRVADSIARLLPTMERAEIIRTSLEGRGALIQVADQAQACAVANRIAPEHLELSVADPESWLPEIRHAGAIFMGRYTAEALGDYCAGPNHVLPTSGTARFSSPLGVYDFQKRSSIINCSAEGASVLGRTASVLARGESLTAHARSAEYRILDEKEA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Catalytic Activity: H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH
Sequence Mass (Da): 47179
Sequence Length: 440
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
EC: 1.1.1.23
|
Q8Y9F9 | MNLNKNLPTGTRDKLFREARAAYKIEQQVNHYFEKRGFKRIETPVIEFEDVFSSEHQADAKLYRFFDEKGRLTVLRPDMTLPIGRVVSTTGVMLPLKLSYSGKIFRANEDFGGEQNEQTQAGIEIIGYPSIKAEIECILIGIGVLNALEIPNFQIELGHAAIYRRVTNLLNLSETAEIDFRLLIQNKSLTGIKRFVADNPSTLDDFILALPRLFGPATAILKQAKNLTTDKGILTALREMETIVEAVSYTADISVDLGLVQDFHYYTGIIFRGYADLAADNFLSGGRYDHLLEQFTSASSPAVGLALNLDSLTTLQNRAGVIKKQVSTSLLIHYDLDAIQQAEKLMQETPNSELSFFETPTNAISFAKKWHIPAVIHVSRQGIQTIFQREADL | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity).
Sequence Mass (Da): 44034
Sequence Length: 393
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Subcellular Location: Cytoplasm
|
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