ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q93Z96 | MASHSSTLFTSPSSFILFSSHRLKSSPNYFTYHFPRSVKRPHFDLRCSVSIEKEVPETERPFTFLRVSDGDQTQSSSYSVRARFEKMIRTAQDKVCEAIEAVEEGPKFKEDVWSRPGGGGGISRILQDGNVWEKAGVNVSVIYGVMPPEAYRAAKAATSEQKPGPIPFFAAGTSSVLHPQNPFAPTLHFNYRYFETDAPKDVPGAPRQWWFGGGTDFTPAYIFEEDVKHFHSV | Function: Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III (By similarity).
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX
Sequence Mass (Da): 26134
Sequence Length: 233
Pat... |
Q83QN1 | MKPDAHQVKQFLLNLQDTICQQLTAVDGAEFVEDSWQREAGGGGRSRVLRNGGVFEQAGVNFSHVHGEAMPASATAHRPELAGRSFEAMGVSLVVHPHNPYVPTSHANVRFFIAEKPGAEPVWWFGGGFDLTPFYGFEEDAIHWHRTARDLCQPFGEDVYPRYKKWCDDYFYLKHRNEQRGIGGLFFDDLNTPDFDHCFAFMQAVGKGYTDAYLPIVERRKAMAYGERERNFQLYRRGRYVEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDYQPKDGSPEAALSEFIKVRDWG | Function: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX
Sequence Mass ... |
P35055 | MMHCASIVSAPSYAFPFRSGSASTTPTAISLTKRSWKPPPSMAKGPVRATVSIEKETPEANRPETFLRGVDEAQSSTSVRARFEKMIREAQDTVCSALEAADGGAQFKEDVWSRPGGGGGISRVLQDGAVWEKAGVNVSVVYGVMPPDAYRAAKGVPTDQKPGPVPFFAAGISSVLHPKNPFAPTLHFNYRYFETDAPKDAPGAPRQWWFGGGTDLTPAYIFEEDVKHFHSIQKQACDKFEPTFYPRFKKWCDDYFYIKHRGERRGLGGIFFDDLNDYDQEMLLSFATECANSVIPAYLPIIEKRKDLPFNDHQKAWQQL... | Function: Involved in the heme and chlorophyll biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX (By similarity).
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + prot... |
P72848 | MTVSPTTQPQTNHSLPPADAKQRVSQFMQTLQDEICQGLEALDGKGKFQEDSWQREEGGGGRSRVLADGDFLEQGGVNFSEVWGKSLPPSILKQRPEAEGHEFYATGTSMVLHPKNPYIPTVHLNYRYFEAGPVWWFGGGADLTPYYPFAEDAAHFHHTLKNACDQTHGEFYPVFKRWCDEYFYLKHRQEMRGIGGIFFDYQDGNAPLYRGPDPNGPAAQYSNQLAPIEPLGWEDLFSFAQRCGRAFLPAYSPIVEKRRNTEYGDRQRQFQLYRRGRYVEFNLVYDRGTIFGLQTNGRTESILMSLPPLVRWQYCYSPEA... | Function: Involved in the heme and chlorophyll biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen I... |
Q6APB0 | MQNIPTGVILLNMGGPTQTKDVRPFLYNLFSDREIIPLGPRLMQKPLAWLIAKRRAPKSAATYERIGGGSPLKQITEAQAEALEKSLQAHGNFTVTYAMRYWPPYCDEALDYLLSKGVERLVALSLYPHYSKATTGSSLTQLHKTLKKKNISLPLTEIPSWPKQRDYIAAIAANIKKGLATFHGEKTEIVYSAHSLPTSFIEAGDPYVEHTKQSIGAIEEITGKRGRLCFQSKSGPVEWLEPSTPDVLIQLAQEGVKNILMVPISFVSDHVETLYEIDILYKKQAKKLGMRLTSCPSLNTQEQFITGLRQLVLESSVNSD | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 35657
Sequence Length: 320
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
Q54IA8 | MISRKIISTINSKTFYNKSLSYCTVNNNKNTTININNNNEKPKIKTGILMLNLGGPSKLEEVEPFLTRLFTDKEIFKLPFQKYTGTLIAKRRSNAVMKLYEAIGGGSPIRKWTEKQGELLSSMMDKISPETAPHKHYIGFRYSDPLIADTLDQMENDNVERVVAFSQYPQYSCTTTGSSLNNLWKTLEEKQMQSKFKWSVIDRWQDHKGFIDATIHKIKKAYNQFNSKLRELDIDDVDANNNNNNNKPVLVFSAHSLPMSTVEKGDPYPQEVAETVCRVMDGLGIRDEETGKPLEYILAWQSKVGPLPWLSPKTSFVIEQ... | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 47990
Sequence Length: 423
Pathway: Porphyrin-containing compound metabolism; protohem... |
Q9V9S8 | MFLHNTKFCRLASGLAGGVRNLSGQKPKTAILMLNMGGPTHTDQVHDYLLRIMTDRDMIQLPVQSRLGPWIAQRRTPEVQKKYKEIGGGSPILKWTELQGQLMCEQLDRISPETAPHKHYVGFRYVNPLTENTLAEIEKDKPERVVLFSQYPQYSCATSGSSFNSIFTHYRSNNLPSDIKWSIIDRWGTHPLLIKTFAQRIRDELAKFVETKRNDVVILFTAHSLPLKAVNRGDAYPSEIGASVHMVMQELGQTNPYSLAWQSKVGPLPWLAPATDDAIKGYVKQGLKNFILVPIAFVNEHIETLHELDIEYCDELAKEV... | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Catalyzes the ferrous insertion into protoporphyrin IX . Terminal enzyme in heme biosynthesis . Contains four conserved cysteines that function as cluster ligands and play a crucial role in maintaining protein structure .
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + proto... |
Q8XD39 | MRQTKTGILLANLGTPDAPTPEAVKRYLKQFLSDRRVVDTSRLLWWPLLRGVILPLRSPRVAKLYASVWMEGGSPLMVYSRQQQQALAQRLPETPVALGMSYGSPSLESAVDELLAEHVDHIVVLPLYPQFSCSTVGAVWDELARILARKRSIPGISFIRDYADNHDYINALANSVRASFAKHGEPDLLLLSYHGIPQRYADEGDDYPQRCRTTTRELASALGMAPEKVMMTFQSRFGREPWLMPYTDETLKMLGEKGVGHIQVMCPGFAADCLETLEEIAEQNREVFLGAGGKKYEYIPALNATPEHIEMMANLVAAYR | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 35854
Sequence Length: 320
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
Q8D226 | MKNNIGIIISNVGTPSHPNKKSVKKYLSEFLSDKRVIDISRFFWIPYLHLYFLPLKSYKSVNLYKKIWEKDGSPLMINSLNQRNYLINKFPNFKIELGMRYGDPSICVAIKKMIKIYNVNKLIILPMYPQYSCTTTASVLDSVCEVIKKYRNIPSIIFIRDYADNINYINAITNSIKKSFNKNGIPEMLIMSFHGIPKKYIKDGDDYLKRCNVTKKLVLSKLNFSRKKVIMSFQSKFGNIPWITPITSEVISFLPKKGIKNIQVICPGFSSDCLETLEEIKIQNKKIFKDNGGKKFHYIPALNYSKIHIECLANIIRTHL... | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 37214
Sequence Length: 321
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
B3CLU1 | MKKAVILFNLGGPDSLSAVRPFLFNLFYDKRIINLPNPFRFLLAKFISKRRESTAQEIYEHIGGKSPILENTKAQADALELKLNENGNHVYKIFICMRYWHPFADEVVKSVKQFDPDEIILLPLYPQYSTTTTLSSIENWQKNAKLECNTKTIHHYYDNEDFIEAHVNLTSKYYKLASKIGKPRVLFSAHSLPLSIIKKGDPYASQIEKTVKLIVKKLNIEDLDWGICYQSKVGPVKWLEPSTESELSRAKDDNIPVVLSPISFVSEHSETLVELDIEYKAIIKDGYYFRVPTLSTDLLFIKCLADLCLDHSQSTDL | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 36383
Sequence Length: 317
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
Q7M7P9 | MKKAVILLNMGGPSSLLEVDMFLKNMFNDPRILPIKSPFFRSLVASFIANRRSETAKANYRKIGGKSPLIGHTFNLIQKLQSLDPSRFYTYAMRYTPPMTDMAVRELAQKEIEEVTLFSLYPQYSTTTTLSSIEEFHKQCALLSYFPKTKEIDRYFEDSNYNEAIIDRILEALGGDNPEEFTLIFSAHGLPQSVIDAGDPYEKEVHANIQALTKLLEERGITFKKITHAYQSKVGPMKWLEPSLDEVLKLHAKEKILLYPIAFTLDNSETDFELRIEYQEKATHLGITDYRVASCLNDSTRFAHAIIKLISQGEIS | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 36077
Sequence Length: 316
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
Q5GRR7 | MKKAVVLLNLGGPDSLSAVRPFLFNLFYDKRIINLPNPFRFFLAKFISAKRENNARKIYEQIGGKSPILENTKMQAEALERELNRSVFCHPSSVTLGPRKENWIPVSRIGMTSKLTKVFICMRYWHPFANEVVKSVKQFDPDEVILLPLYPQYSTTTTLSSIENWQKNAKQYGIKCNTKIIRHHYDNQDFIEAHANLITKHYKLASEVGKPRVLFSAHSLPLSVIKKGDPYALQVEETVKLIVKKLHIKDLDWSICYQSKIGPVKWLEPSTESELLRAKADGVPVVLLPISFVSEHSETLVELDMEYKTIIKDGYYFRIP... | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 38928
Sequence Length: 340
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
Q8P3H6 | MNTTSDTALLVVNLGTPESPTVPAVRRYLAEFLSDRRVVAIPPLFWKPLLYGVILPIRGPKSAEKYAKVWLPDGSPLAVYTRRLTEGLQQVMPDWHVTWAMRYGAPALRKALDGLRARGIKRIVVLPLYPQYSTTTTASIQDVVDAWRPSAPEIAVEVIQDYCEDAGWVAAIADSIRTHWQVHGRSEKLMFSFHGLPQRVANAGDPYPQQCERSAQAIVTALGLGPDAWQMGYQSRFGAERWLQPYAEPTLWALAEGGVRSFDLVCPGFATDCLETLEEVALGFAETLAERGATLSYIPCLNDSTTHAQALAAVARRA | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 35064
Sequence Length: 318
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
O57478 | MAAFRAAHRLLGHILRNESSAGLVTQRWSSSAAVASVPKSSDPKPHAQPDKRKPKTGILMLNMGGPETLDDVHGFLLRLFLDKDLMTLPAQSKLAPFIAKRRTPKIQEQYSKIGGGSPIKKWTEQQGEGMVKLLDELSPATAPHKYYIGFRYVRPLTEAAIEEMERDGVERAIAFTQYPQYSCSTTGSSLNAIYRYYNAKGTQPKMKWSVIDRWPTHPLLIQCFADHIQKELNMFPADKRGEVVILFSAHSLPMSVVNRGDPYPQEVGATVQKVMERLGFSNPYRLVWQSKVGPMAWLGPQTDESIKGLCQRGKKNILLV... | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 46039
Sequence Length: 411
Pathway: Porphyrin-containing compound metabolism; protohem... |
P16622 | MLSRTIRTQGSFLRRSQLTITRSFSVTFNMQNAQKRSPTGIVLMNMGGPSKVEETYDFLYQLFADNDLIPISAKYQKTIAKYIAKFRTPKIEKQYREIGGGSPIRKWSEYQATEVCKILDKTCPETAPHKPYVAFRYAKPLTAETYKQMLKDGVKKAVAFSQYPHFSYSTTGSSINELWRQIKALDSERSISWSVIDRWPTNEGLIKAFSENITKKLQEFPQPVRDKVVLLFSAHSLPMDVVNTGDAYPAEVAATVYNIMQKLKFKNPYRLVWQSQVGPKPWLGAQTAEIAEFLGPKVDGLMFIPIAFTSDHIETLHEID... | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
PTM: The leader peptide may be processed in two proteolytic steps, first between Ser-23 and Phe-24, second and by a different protease, to yield the mature protein.
Location Topology: Peripheral membrane protein
Catalytic Activity: 2 H(+) + heme b = Fe(2... |
Q58824 | MYVMKVVGKTTTTHFTFESLEKIRFGEYVIAKNVDGRDVLGVIKNVVADVEKFVGEVKVIGVLDGNKIIPNRTPILPNSEVRLCDDEILNNIYLTPDGLNIGHLLTRDNVRVYLDTNKLVSRHFAILSITGGGKSNTASVLCRELAKKNGTVIMIDPHGEYISLYHEDMEGKIKVINPIINPVLLAPSEFANLIGIGDNEIEKRVYVEFAYHTVKHECPDAKGIEFIEKIENLLYEWSKIASVGWEIKYYNPLRRNYDRRKLEKEDFVILMSLIDTISKFKLDYALNIGDRDVIEEFEIGKINIVNLSGLEIPQMVTFVG... | Function: Involved in DNA double-strand break (DSB) repair (By similarity). Acts probably with NurA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Exhibits DNA-dependent ATPase activity and DNA helicase activity (By similarity).
Catalytic... |
Q8U1P0 | MEEFVGIVRGEASFTSYEFSINPSANVSFGEFVVTKNRDGDLVLGTVRHVKNVNWLLSSVKSNFNSLALDIEEYGESLGENEEVVATVRILGKIEGNELVPNRVPIRNGEYVYKASDDLLQMIYGNDGIEIGTLLLRPNVRIKLDVNELVSRHFAVLAVTGAGKSNAVAVIIKGIVEDVGGTVVVLDPHGDYVNLRLPETGIDLVNIIDGKIRIEDLDPEELADLIGISSSAQIQRHFLSLAWETVKHKNQSLGGESLLEALLDLLNEWISRKTIKYWSEKEGRMKSEDLKSERIETIRGIIFRIRRFLRNYGNIVTSEN... | Function: Involved in DNA double-strand break (DSB) repair . Acts probably with NurA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading . Exhibits DNA-dependent ATPase activity and DNA helicase activity (By similarity) .
Catalytic Activity: ATP + H2O = ADP + ... |
Q97WG8 | MIIGYVIGQATTQEALILAERPVRLGTYVVLEYDNVKALGLITNVTRGSPMLDDNMNDIEIVQRLKQFNNSIPVYTKAKVKMLCDMNNHFLMPDIPPFAGTPAREAEDEELKSIYSQDGQIRIGSLIGKNVEVKLNINSFARHLAILAATGSGKSNTVAVLSQRISELGGSVLIFDYHGEYYDSDIKNLNRIEPKLNPLYMTPREFSTLLEIRENAIIQYRILRRAFIKVTNGIREKLKEGQIPFSTLNSQFYELMKDELETQGNSDKKSSAKDEVLNKFEEFMDRYSNVIDLTSSDIIEKVKRGKVNVVSLTQLDEDSM... | Function: Involved in DNA double-strand break (DSB) repair . Acts probably with NurA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Exhibits DNA-dependent ATPase activity and DNA helicase activity .
Catalytic Activity: ATP + H2O = ADP + H... |
Q8IVU3 | MYFCWGADSRELQRRRTAGSPGAELLQAASGERHSLLLLTNHRVLSCGDNSRGQLGRRGAQRGELPEPIQALETLIVDLVSCGKEHSLAVCHKGRVFAWGAGSEGQLGIGEFKEISFTPKKIMTLNDIKIIQVSCGHYHSLALSKDSQVFSWGKNSHGQLGLGKEFPSQASPQRVRSLEGIPLAQVAAGGAHSFALSLCGTSFGWGSNSAGQLALSGRNVPVQSNKPLSVGALKNLGVVYISCGDAHTAVLTQDGKVFTFGDNRSGQLGYSPTPEKRGPQLVERIDGLVSQIDCGSYHTLAYVHTTGQVVSFGHGPSDTS... | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-... |
Q9LX66 | MGIEKFETFILISTISILLCICHGFTPVDNYLINCGSPTNGTLMGRIFLSDKLSSKLLTSSKEILASVGGNSGSDIYHTARVFTEVSSYKFSVTRGRHWVRLYFNPFDYQNFKMGSAKFAVSSQSHVLLSDFTVTSSKVVKEYSLNVTTNDLVLTFTPSSGSFAFVNAIEVISIPDTLITGSPRFVGNPAQFPDMSMQGLETIHRVNMGGPLVASNNDTLTRTWVPDSEFLLEKNLAKSMSKFSTVNFVPGYATEDSAPRTVYGSCTEMNSADNPNSIFNVTWEFDVDPGFQYYFRFHFCDIVSLSLNQLYFNLYVDSMV... | Function: Receptor-like protein kinase required for cell elongation during vegetative growth, mostly in a brassinosteroid-(BR-) independent manner.
PTM: Autophosphorylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 91468
Sequence Length: 830
Subcellular Location: Cell membrane
EC: 2.7.1... |
Q15011 | MESETEPEPVTLLVKSPNQRHRDLELSGDRGWSVGHLKAHLSRVYPERPRPEDQRLIYSGKLLLDHQCLRDLLPKQEKRHVLHLVCNVKSPSKMPEINAKVAESTEEPAGSNRGQYPEDSSSDGLRQREVLRNLSSPGWENISRPEAAQQAFQGLGPGFSGYTPYGWLQLSWFQQIYARQYYMQYLAATAASGAFVPPPSAQEIPVVSAPAPAPIHNQFPAENQPANQNAAPQVVVNPGANQNLRMNAQGGPIVEEDDEINRDWLDWTYSAATFSVFLSILYFYSSLSRFLMVMGATVVMYLHHVGWFPFRPRPVQNFPN... | Function: Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins . Could enhance presenilin-mediated amyloid-beta protein 40 generation. Binds to ubiquilins and this interac... |
Q9KIV0 | MANFRLNVLAYSVMLGLTAGVAYAAQPTNQPTNQPTNQNSNVSEQLEQINVSGSTENSDTKTPPKIAETVKTAKTLEREQANNIKDIVKYETGVTVVEAGRFGQSGFAIRGVDENRVAINIDGLRQAETLSSQGFKELFEGYGNFNNTRNGAEIETLKEVNITKGANSIKSGSGSLGGSVIYKTKDARDYLLNKDYYVSYKKGYATENNQSFNTLTLAGRYKKFDALVVTTRRNGHELENYDYKNADSLTQGKKREKADPYKIEQDSTLLKLSFNPTENHRFTLAADLYEHRSRGQDLSYTLKYQRSGNETPEVESRHTN... | Function: Acts as a receptor for hemoglobin of the human host and is required for heme uptake.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 113617
Sequence Length: 993
Subcellular Location: Cell outer membrane
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P11569 | MPKTVSPGVQALRDVVEKVYRELREAKERGEKVGWSSSKFPCELAESFGLHVGYPENQAAGIAANRDGEVMCQAAEDIGYDNDICGYARISLAYAAGFRGANKMDKDGNYVINPHSGKQMKDANGKKVFDADGKPVIDPKTLKPFATTDNIYEIAALPEGEEKTRRQNALHKYRQMTMPMPDFVLCCNNICNCMTKWYEDIARRHNIPLIMIDVPYNEFDHVNEANVKYIRSQLDTAIRQMEEITGKKFDEDKFEQCCQNANRTAKAWLKVCDYLQYKPAPFNGFDLFNHMADVVTARGRVEAAEAFELLAKELEQHVKE... | Cofactor: Binds 1 [4Fe-4S] cluster per heterodimer.
Function: Involved in the fermentation of L-glutamate via the hydroxyglutarate pathway . Catalyzes the reversible syn-elimination of water from (R)-2-hydroxyglutaryl-CoA to yield (E)-glutaconyl-CoA . The dehydration mechanism involves a transient one electron reductio... |
P11570 | MAISALIEEFQKVSASPKTMLAKYKAQGKKAIGCLPYYVPEELVYAAGMVPMGVWGCNGKQEVRSKEYCASFYCTIAQQSLEMLLDGTLDGLDGIITPVLCDTLRPMSQNFKVAMKDKMPVIFLAHPQVRQNAAGKQFTYDAYSEVKGHLEEICGHEITNDAILDAIKVYNKSRAARREFCKLANEHPDLIPASVRATVLRAAYFMLKDEYTEKLEELNKELAAAPAGKFDGHKVVVSGIIYNMPGILKAMDDNKLAIAADDCAYESRSFAVDAPEDLDNGLQALAVQFSKQKNDVLLYDPEFAKNTRSEHVCNLVKESG... | Cofactor: Binds 1 [4Fe-4S] cluster per heterodimer.
Function: Involved in the fermentation of L-glutamate via the hydroxyglutarate pathway . Catalyzes the reversible syn-elimination of water from (R)-2-hydroxyglutaryl-CoA to yield (E)-glutaconyl-CoA . The dehydration mechanism involves a transient one electron reductio... |
P11568 | MSIYTLGIDVGSTASKCIILKDGKEIVAKSLVAVGTGTSGPARSISEVLENAHMKKEDMAFTLATGYGRNSLEGIADKQMSELSCHAMGASFIWPNVHTVIDIGGQDVKVIHVENGTMTNFQMNDKCAAGTGRFLDVMANILEVKVSDLAELGAKSTKRVAISSTCTVFAESEVISQLSKGTDKIDIIAGIHRSVASRVIGLANRVGIVKDVVMTGGVAQNYGVRGALEEGLGVEIKTSPLAQYNGALGAALYAYKKAAK | Cofactor: Binds 1 [4Fe-4S] cluster per dimer.
Function: Involved in the fermentation of L-glutamate via the hydroxyglutarate pathway. HgdC (CompA) has a very low ATPase activity, whose the role is to activate dehydratase HgdA-HgdB complex and then maintain an appropriate redox state via an ATP-dependent electron transf... |
D2RJU7 | MKVLCYGVRDVELPIFEACNKEFGYDIKCVPDYLNTKETAEMAAGFDAVILRGNCFANKQNLDIYKKLGVKYILTRTAGTDHIDKEYAKELGFPMAFVPRYSPNAIAELAVTQAMMLLRHTAYTTSRTAKKNFKVDAFMFSKEVRNCTVGVVGLGRIGRVAAQIFHGMGATVIGEDVFEIKGIEDYCTQVSLDEVLEKSDIITIHAPYIKENGAVVTRDFLKKMKDGAILVNCARGQLVDTEAVIEAVESGKLGGYGCDVLDGEASVFGKDLEGQKLENPLFEKLVDLYPRVLITPHLGSYTDEAVKNMVEVSYQNLKDL... | Function: Catalyzes the reduction of 2-oxoglutarate to 2-hydroxyglutarate.
Catalytic Activity: (R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) + NADH
Sequence Mass (Da): 36586
Sequence Length: 331
EC: 1.1.1.399
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Q9ZRA2 | MEEKKKELEELKYQSGFGNHFSSEAIAGALPLDQNSPLLCPYGLYAEQISGTSFTSPRKLNQRSWLYRVKPSVTHEPFKPRVPAHKKLVSEFDASNSRTNPTQLRWRPEDIPDSEIDFVDGLFTICGAGSSFLRHGFAIHMYVANTGMKDSAFCNADGDFLLVPQTGRLWIETECGRLLVTPGEIAVIPQGFRFSIDLPDGKSRGYVAEIYGAHFQLPDLGPIGANGLAASRDFLAPTAWFEDGLRPEYTIVQKFGGELFTAKQDFSPFNVVAWHGNYVPYKYDLKKFCPYNTVLLDHGDPSINTVLTAPTDKPGVALLD... | Catalytic Activity: homogentisate + O2 = 4-maleylacetoacetate + H(+)
Sequence Mass (Da): 51455
Sequence Length: 461
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 4/6.
EC: 1.13.11.5
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Q89XH1 | MNINTSPDQIIRSSAQVTPGYMSGFGNSFETEALPGALPIGRNSPQRCAYGLYAEQLSGSPFTAPRGTNERSWLYRIRPSVKHSGRFEKADAGLWRSAPCHEYDLPIAQMRWDPTPVPKEEVTFVQGVQTMTTAGDVNTQAGMAAHVYLITKSMVDQHFYNADGELMFVLQQGNLRLVTEFGRIDAEPGEIVVIPRGVKFRVEIPNGPARGYLCENYGGAFTLPERGPIGANCLANARDFLTPVANYEDKDTPTELFVKWGGSLFKTTLPHSPIDVVAWHGNYAPYKYDLRTFSPVGAIGFDHPDPSIFTVLTSPSETAG... | Function: Involved in the catabolism of homogentisate (2,5-dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring cleavage of the aromatic ring of homogentisate to yield maleylacetoacetate.
Catalytic Activity: homogentisate + O2 = 4-... |
Q93ZH9 | MDQNGHNDEAETVSCGNGNCKSKIVPGDDHGGDESSGTKRRKKRKTQQKTMKRRELMSYCELPEYMKDNEYILNYYRADWSIRDAFFSVFSFHNESLNVWTHLIGFIFFVALTVANIIHHDGFFPVDAKSPGNVTRWPFFVFLGGSMFCLLASSICHLFCCHSKELNVFLLRIDYAGITAMIITSFFPPIFYIFQCTPRWYFIYLAGITSMGIFTIITLFTPSLSAPKYRAFRALLFASMGLFGIVPAAHALVVNWGNPQRNVTLVYELLMAVFYLVGTGFYVGRVPERLKPGWFDRVGHSHQIFHVFVLLGALSHYAAA... | Function: May act as a negative regulator of abscisic acid (ABA)-mediated osmotic stress signaling and function in cross-talk between cold and osmotic signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37877
Sequence Length: 332
Subcellular Location: Membrane
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P40235 | MALDLRIGNKYRIGRKIGSGSFGDIYLGTNVVSGEEVAIKLESTRAKHPQLEYEYRVYRILSGGVGIPFVRWFGVECDYNAMVMDLLGPSLEDLFNFCNRKFSLKTVLLLADQLISRIEFIHSKSFLHRDIKPDNFLMGIGKRGNQVNIIDFGLAKKYRDHKTHLHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLVYFCRGSLPWQGLKATTKKQKYEKIMEKKISTPTEVLCRGFPQEFSIYLNYTRSLRFDDKPDYAYLRKLFRDLFCRQSYEFDYMFDWTLKRKTQQDQQHQQQLQQQLSATPQAIN... | Function: Involved in DNA repair. Has a probable role in repairing alkylated DNA and may regulate the activity of protein(s) involved in double strand break repair caused by gamma rays.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 42450
Sequence Length: 365
... |
Q84N34 | MQKRRTVKESTKIRNGKGMDSGEKKRSEKRLMKFEELPRYLKDNEFIHNHYRCEWSIKETFLSAFSWHNETLNIWTHLCGFAIFTWMMVVSSMETTELGLAGFVSLLSGATIRWPWPSMAMSKDVYFSSDQTLHHDLNVTHTRSLLNSQGDVNYEAIPKWPWLVFLTGAMGCLICSSMSHLFACHSRRFNLFFWRLDYAGISLMIVCSFFAPIYYAFSCHTYWRLFYLSSISILGLLAIFTLLSPSLSAPRFRSFRAALFLTMGFSGVIPATHVLYLHKDHPNVLIALVYELAMAVLYATGAAFYVTRIPERWKPGAFDI... | Function: May play a role in abiotic stress response.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41025
Sequence Length: 358
Subcellular Location: Membrane
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P40236 | MTVVDIKIGNKYRIGRKIGSGSFGQIYLGLNTVNGEQVAVKLEPLKARHHQLEYEFRVYNILKGNIGIPTIRWFGVTNSYNAMVMDLLGPSLEDLFCYCGRKFTLKTVLLLADQLISRIEYVHSKSFLHRDIKPDNFLMKKHSNVVTMIDFGLAKKYRDFKTHVHIPYRDNKNLTGTARYASINTHIGIEQSRRDDLESLGYVLLYFCRGSLPWQGLQADTKEQKYQRIRDTKIGTPLEVLCKGLPEEFITYMCYTRQLSFTEKPNYAYLRKLFRDLLIRKGYQYDYVFDWMILKYQKRAAAAAAASATAPPQVTSPMVS... | Function: Involved in DNA repair. May regulate the activity of protein(s) involved in double strand break repair caused by gamma rays.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 45832
Sequence Length: 400
Subcellular Location: Nucleus
EC: 2.7.11.1
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Q9ZUH8 | MKRRRSAKKSPAMVTVTDWKGLDCGEETRIVRRLMKFEDLPEYLKDNEFIHNHYRCQWSLKDTFLSAFSWHNETLNIWTHLIGFGIFLWMTVVSCLETTEISLAGVFNGMAGVRICLSSNQTLLHDSNVTHHISCLTSQGEAIPKWPWLVYLVGAMGCLICSSVSHLLACHSKRFNVFFWRLDYAGISLMIVASFFAPIYYAFSCHPNFRLLYLSSISILGLLAIITLLSPALSTPRFRPFRANLFLAMGSSAVIPATHVLCLYWDHPNVFIALGYEIATALSYFVGATFYVSRVPERWKPGAFDMAGHSHQIFHVFVVM... | Function: May play a role in abiotic stress response.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38853
Sequence Length: 344
Subcellular Location: Membrane
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Q9SZG0 | MGDEAEIKEHLKPQASSETMDKKHNVKGKRLWQKVKYQLVEFHSLPAYLRDNEYIIGHYRSEWPIKQILLSIFTIHNETLNVWTHLIGFFLFLALTIYTATKVPSVVDLHSLQHRLPDLLRKTDLHKLHSELMARLPSSPSSWHVMDLLYNCLPERFSHGNYTDMCVLHSVREDLANLIAPLIFRPITRWPFYAFLGGAMFCLLASSTCHLLSCHSERVSYIMLRLDYAGIAALIATSFYPPVYYSFMCDPFFCNLYLGFITILGIATVLVSLLPVFQSPEFRVVRASLFFGMGFSGLAPILHKLIIFWDQPEALHTTGY... | Function: May play a role in abiotic stress response.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44172
Sequence Length: 385
Subcellular Location: Membrane
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Q94CD1 | MVAENNKNKDVTLSASMDNNNNNIKGTNIHLEVHQKEPALVKPESETRKGLYFLSNLDQNIAVIVRTIYCFKSEERGNEEAVQVIKKALSQVLVHYYPLAGRLTISPEGKLTVDCTEEGVVFVEAEANCKMDEIGDITKPDPETLGKLVYDVVDAKNILEIPPVTAQVTKFKCGGFVLGLCMNHCMFDGIGAMEFVNSWGQVARGLPLTTPPFSDRTILNARNPPKIENLHQEFEEIEDKSNINSLYTKEPTLYRSFCFDPEKIKKLKLQATENSESLLGNSCTSFEALSAFVWRARTKSLKMLSDQKTKLLFAVDGRAK... | Function: Involved in the synthesis of aromatics of the suberin polymer. Specifically affects the accumulation of the ferulate constituent of suberin in roots and seeds, but has no effect on the content of p-coumarate or sinapate.
Catalytic Activity: (E)-feruloyl-CoA + 16-hydroxyhexadecanoate = 16-feruloyloxyhexadecano... |
Q7XXP3 | MKITVRSSTVVVPAAETPRVRLWNANPDLVVPRFHTPSVYFYRRGGEDGGDACYFDAGRMRRALAEALVPFYPMAGRLAHDEDGRVEIDCNAEGVLFVEADAPDGAVDDFGDFVPTMGLKRLIPTVDFTGGISSYPLLVVQVTHFKCGGVALGIAMQHHVADGFSGLHFINSWSDLCRGVPIAVMPFIDRTLLRARDPPVPTHPHIEYQPAPAMLGSEEPQALAGKPESPPTAVDIFKLSRSDLGRLRAQLPTGEGAPRFSTYAVLGAHVWRCASLARGLAPEQPTKLYCATDGRQRLTPTHPDGYFGNVIFTATPLAEA... | Function: Involved in the biosynthesis of avenanthramide phytoalexins, which are phenolic alkaloids found mainly in oats . Catalyzes the N-acylation of 5-hydroxyanthranilate with 4-coumaroyl-CoA or caffeoyl-CoA as acyl donors, forming avenanthramide A and avenanthramide C, respectively . Does not accept feruloyl-CoA as... |
A0A4Y5UJ70 | MAITVRRSTMVRPAAERPRERLWNSNLDLVVPRFHTPSVYFYRRPDAGAGAGPGAAEGFFDAERMRRALAEALVPFYPMAGRLARDEDGRVEIDCSGEGVLFVEARAPGAAVDDYGDFAPTMELKRLIPAVDYSGDISSFPLLVLQVTYFKCGGVSLGVGMQHHVADGMSGLHFINSWSDLCRGAQIAVMPFIDRTLLRARDPPTPSYTHVEYQPAPAMLSSAPQALTGKPTLAPTAVDIFKLTRSELGRLRAQLPTGEGAPRFSTYAVLAAHVWRCVSLARGLPAEQPTKLYCATDGRHRLQPPLPEGYFGNVIFTATP... | Function: Involved in the biosynthesis of avenanthramide phytoalexins, which are phenolic alkaloids found mainly in oats . Catalyzes the N-acylation of 5-hydroxyanthranilate with 4-coumaroyl-CoA or caffeoyl-CoA as acyl donors, forming avenanthramide A and avenanthramide C, respectively . Does not accept feruloyl-CoA as... |
P39982 | MSLSFLLFSPFLPPCFSSISICLSVLSTVSFFFAFTIPHYVLRCGSVDEWHIHSSAEDFRTQRCVCAVKLSASLLGCLLACASWSLLLEVSRIKWHVGTAYS | Function: Involved in vacuolar trafficking.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11341
Sequence Length: 102
Subcellular Location: Membrane
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A0A0H3L116 | MMEYATHLSRQGYAFIPGDYYRSTEAMQFSNKEDFLDELEELKKGYENLLLDPYSPGNRWRGYAQCKKNEKGELTFGKFNPYKQTKAFNPDTGDIIRDYPLLPEAITRNRLFQTLLHDDLSLVDAYESIGPVDSLTIGIHFFRYQATENEPAYSSPVWLHKDDEDVVFVHMINASPNMLGGDSLIASHPRSIDRVLRLEQLFDTLVVNHDKLHAVTPVGARENSGPAQRDIILITFQKNEEKTACPV | Cofactor: Binds 1 ascorbate molecule per subunit.
Function: Catalyzes the hydroxylation of L-4'-hydroxyisoleucine (4'-HIL) at the C-4 position to form L-4,4'-dihydroxyisoleucine (4,4'-DIHIL) . Together with HilA, catalyzes the two step conversion of L-isoleucine into L-4,4'-dihydroxyisoleucine . In vitro, in the absenc... |
O59836 | MNLGRCPLAPRSANIVLPKHDAVSKQKEYRIEEKTNEAQREEIITWKDNREDEGEVKTDFEVVNNENIITTTPKHQTVITPKSYRKSVKRIKHDAPQNEDIPVMKGLAPINADTESKAESMAAGKVLGSKNSSQKARLQEWKRQYKKAFPHFRFYLDGCDPSVAHRVKKQIQQLGGHVETFFSGNVTHVATVRAIQDVSVKYAKQDVITKARQLNMKIWSMEKLCNRVLKTLMENDQCTTNAPTKQGNDLSYLLYVEKVQGTNERDLSVPRQDFVHFRGPYLYVHDIANIYKPILLREWQKPLPDRDVPWPTFRATSIGR... | Function: Activates hsk1 kinase and is essential for G1/S transition. Has a role in S-phase checkpoint control induced by replication fork blocks after nucleotide deprivation and DNA damage.
PTM: Hyperphosphorylated at the G1/S and S-phases of the cell cycle.
Sequence Mass (Da): 61860
Sequence Length: 545
Subcellular L... |
A0A2Z5TMB8 | MEDIVNRLYAFDWRSLSLGSVPAPTPAPAPQSSVVHHLIAWWDQSKDSMQQYSVASVAIAGFTALVVSVALYRALFSQRQRHDPLNQGCQPLRMYPHKDRIFGLDFVYQNVTTFRRHKYLETLKNRYQTLGTTYGVRVFNRRGILTSDPENIKTILSTRFKDYSLGNRVPIMGPLLGRGIFVSDGQDWSHSRALLRPNFVKEQVADLQMIETHLAQLLKLIPSDGRTVVELQDLFLRFTLDSATDFLFGHSLHTLSRGTAKDQQFGQAFALALDDIALQFRLGPWRALRRPNKDALAAYEICRGYVEGFVADAMAYRHGK... | Function: Cytochrome P450 monooxygenase; part of the him gene cluster that mediates the biosynthesis of himeic acid A, a ubiquitin-activating enzyme (E1) inhibitor . First, himA, together with the trans-enoyl reductase himH, catalyzes the formation of apolyketide chain, which is then condensed with leucine by the NRPS ... |
A0A2Z5TTA9 | MSNSTDPSDYCTFEICPITEAYVYYVPSLAGNAFYLALFAVLLAAQLVLAVRYRTWGYLAGLSGGLILEIIGYIGRIQLHSNPFRFGPYLEYLICLTIGPAILSASIYICLGRIVIVYGEGISRLRPKTYTMVFVACDLVSLVLQAAGGAITSVADADQYDLAQDGINIMIAGLASQVASLALFMALCLDYAWRVYKSPHNLSPETRMRDLRHSLRWKAFLAGLALATVAIFMRSVFRVAELKGGFHSSLANDQVLFMTLEGAMIAIAVIALTVLHPGLCFDGLWDQTKWSFRRSRDSEMQLIEVSAGHEAKAQRADLGM... | Function: Efflux pump that is probably involved in the efflux of himeic acid A, a ubiquitin-activating enzyme (E1) inhibitor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35235
Sequence Length: 321
Subcellular Location: Cell membrane
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A0A2Z5TWF0 | MQIITIFGATGNQGSSVARSLLRNRSFEVRCITRNAESKKAQLLKAQGAVIVEADGYDTSQIQQAFSGSWGAFVNTNGDDPSLASENRTDRDLGLSIIRGAAAAGVKHLVYSSGPWAAKLSGGACSVPSNDAKAEVQHVAQGLGFETVTPIMPGWFFETFLEPQMAAIFGGFPVTPDEEGWLTCRAPLWGGREHVPFLSVDNDFGDIVHGVFLNPVRWNLRPIQAISDFLSFADFVNTYVSLTGKKARFVALSSPMEMETMGHPLLESIRGFFIFSQLRDGEYFGTGPTEKETATALKQAAHRAQANDRKGEQAALTSAR... | Function: NmrA-like family domain-containing oxidoreductase; part of the him gene cluster that mediates the biosynthesis of himeic acid A, a ubiquitin-activating enzyme (E1) inhibitor . First, himA, together with the trans-enoyl reductase himH, catalyzes the formation of apolyketide chain, which is then condensed with ... |
A0A2Z5TIR0 | MAPALTQSLNGATPQVKAALHHLDANTVSIDDIIHYLKHHGGVVVQNLISEEILQEVGADIKPYFDALVEPGFFSSKTRIVTRLPNKSIAFVEKIFGNQVFQDICDHFLTSHHRGWYGNEQYTYSPHPVFNSALAFSTLPGNETQSLHRECMGQHNKLPAIAPEDYPIGRDTVLGMFVADTRTTRENGATRFIPGSHLQSTLDPPDESQTVPVEMNRGDVFLMLGSCYHGASANVSQAEERILYSTFMTQSTRRQLTTCLFLVQEENIYLSVPVDRVRVFSPRMQKRLGFSASDPLFGWVDVKDPRKVFNLPGLSEGQHI... | Function: Polyketide synthase-nonribosomal peptide synthetase; part of the him gene cluster that mediates the biosynthesis of himeic acid A, a ubiquitin-activating enzyme (E1) inhibitor . First, himA, together with the trans-enoyl reductase himH, catalyzes the formation of apolyketide chain, which is then condensed wit... |
A0A2Z5TIQ0 | MASLINQAAWQPKARTRSLQVGPGPTPSPNEHEIVIKVAYAAVNPTDWKMQDTPYFELEYPFIWGTDVAGTIVQLGSEVTQFKVGQRVIGHCDSLLTRKVTNAGFQLYTTVREILVAEIPDSLPLANAAVLPLSVSTAASALYVQLDLPFPSLSPKSTGKRIVIWGGSSSVGSSAIQLAVASGLEVVATASQANHDLVRSLGASQVFDHRAPSVIDQMASVLQPGDYVVDCIGSPDTQAKCGELVGRIGGGTLPVMLWPQGGLPQNVRAVFVNGLDPGMVNLDVGNAVWRKFIPEALAAGKFQAKPDPRIVPGGLEKVQE... | Function: Trans-enoyl reductase; part of the him gene cluster that mediates the biosynthesis of himeic acid A, a ubiquitin-activating enzyme (E1) inhibitor . First, himA, together with the trans-enoyl reductase himH, catalyzes the formation of apolyketide chain, which is then condensed with leucine by the NRPS activity... |
P26631 | VSYTDCTSGQNYCLCGGNFCGDGKHCEMDGSENKCVDGEGTPKRQTSGPSDFEEFSLDDIEQ | Function: Inhibits thrombin, thereby abolishing its ability to cleave fibrinogen.
PTM: O-linked glycan consists of Fuc-Gal-GalNAc trisaccharide.
Sequence Mass (Da): 6693
Sequence Length: 62
Subcellular Location: Secreted
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Q9FM19 | MGNLFCCVQVDQSTVAIKETFGKFEDVLEPGCHFLPWCLGSQVAGYLSLRVQQLDVRCETKTKDNVFVNVVASIQYRALANKANDAYYKLSNTRGQIQAYVFDVIRASVPKLLLDDVFEQKNDIAKAVEEELEKAMSAYGYEIVQTLIVDIEPDEHVKRAMNEINAAARMRLAANEKAEAEKILQIKRAEGEAESKYLSGLGIARQRQAIVDGLRDSVLGFAVNVPGTTAKDVMDMVLVTQYFDTMKEIGASSKSSAVFIPHGPGAVRDVASQIRDGLLQGSSANL | Function: Positive regulator of hypersensitive response (HR)-like cell death. May be involved in potassium ion channel regulation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 31431
Sequence Length: 286
Subcellular Location: Cell membrane
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P60836 | MTDYITIAIPKGRILEESVTLFGKIGINCDELLSNTRKLIFENHEQRMRYMIVRATDVPTYVEYGCADLGIVGKDTLMEQEKDLYEPLDLKFGYCRMMVAEPAGLALDDDPSSWTNIRIATKYPNVTEKYFARKGVQVEIIKLYGSIELAPLVGLSERIVDLVSTGETLRQNGLVEVETIAEITTRLIVNRASLKTKHPRITEIIEGLEKHV | 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-phos... |
Q9S762 | MSLLLPTNLQQYPSSSSFPSSTPILSPPPSTAFSVIVPRRRCLRLVTSCVSTVQSSVATNGSSPAPAPAAVVVERDQIRLGLPSKGRMAADAIDLLKDCQLFVKQVNPRQYVAQIPQLPNTEVWFQRPKDIVRKLLSGDLDLGIVGLDTLSEYGQENEDLIIVHEALNFGDCHLSIAIPNYGIFENINSLKELAQMPQWSEERPLRLATGFTYLGPKFMKENGIKHVVFSTADGALEAAPAMGIADAILDLVSSGITLKENNLKEIEGGVVLESQAALVASRRALNERKGALNTVHEILERLEAHLKADGQFTVVANMRG... | Function: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP).
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + ATP
Sequence Mass (Da): 44556
Sequence Length: 411
Pathway: Amino-acid biosynthesis; L-... |
A3DJF0 | MRYLTIALSKGRLTDMSVELFEAIGIDCTELKNSSRKLILTDEKNKIKFFLAKPSDVPTYVEYGAADIGIVGKDTLMEEGRHLYEVLNLGFAACKMVVAGPAELMGKLDRLTNKRVATKYPRIAREYFEHKRKESIEVIKLNGSVELAPLVGLSEVIVDLVESGRTLKENGLVVLDTIADISARLVVNRVSMKMKSERINPIIDAIRKELEKR | 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-ribos... |
B7JA13 | MSTGITIALSKGRILQEAIPLFAGAGIHLAEDPEESRKLIIPSTDPTVRFLVIRASDVPTYVTWGAADVGIAGKDVLLEQEGLDLYEPLDLRIGICHMAVAEPAAMAADDAPQSWERVRIATKYPHITRHYFHSRGVQTEIIKLYGSMELAPLVGLADRIVDLVSSGRTLKENGLVEVEEIMPISSRLVVNRAAMKLKRRAIETLIRQLEAQVTP | 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-ribos... |
Q8UHK1 | MITIALPSKGRMKEDASAVLERAGLKVASVGNDRSYRGRIEGRDDIEVAYLSASEIAREIGAGTVDFGVTGEDLVREGLTNADAQVEFCARLGFGHADVVVAVPEIWLDVDSMADLGDVASEFRARHGRRLAIATKYWRLTQQFFSRQHGIQLYRIVESLGATEGAPAAGQADIIVDITSTGSTLKANHLKILSDGIIVRSEACFVRARKPEHEGDAAIQEIASRIKAAV | 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-ribos... |
Q8X8T4 | MTDNTRLRIAMQKSGRLSDDSRELLARCGIKINLHTQRLIAMAENMPIDILRVRDDDIPGLVMDGVVDLGIIGENVLEEELLNRRAQGEDPRYFTLRRLDFGGCRLSLATPVDDAWDGPLSLNGKRIATSYPHLLKRYLDQKGISFKSCLLNGSVEVAPRAGLADAICDLVSTGATLEANGLREVEVIYRSKACLIQRDGEMEESKQQLIDKLLTRIQGVIQARESKYIMMHAPTQRLDEVIALLPGAERPTILPLAGDQQRVAMHMVSSETLFWETMEKLKALGASSILVLPIEKMME | 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-ribos... |
Q8CTV1 | MLRVALAKGRLLKSFIEYLQQVNQIDIATVLLNRQRQLLLTVDNIEMILVKGSDVPTYVEQGIADVGIVGSDILNGQKYNINKLLDLPFGKCHFALAAKPETSCYKKVATSYVHTATQFFNKEGMDVEVIHLNGSVELSCVVDMVDAIVDIVQTGSTLTANGLVEKKYISEINAKLITNKESYFKQSSEIERLIKQLGVSISYA | 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-ribos... |
Q9K6Z7 | MNVDDLTFDDKGLIPAVVQDAQSKEVVTVAYMNRESFEKTVETGETWFYSRSRQELWHKGATSGHTQKVVDIRYDCDGDALVVLVELKGPACHTGKYSCFFESVFGKKIYGASDRFGIIATLEALIAEREAEMPEGAYTTYLFEKGVDKILKKVGEEATEVVIAAKNRDAEELKWEVADLLYHLLVLLREQKLPVDEVLAVLEERHRPKEE | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 23906
Sequence Length: 211
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytopl... |
A1WW04 | MSNAASERTAADTLRALAETIEQRRGASADTSYVARLHDKGLDAILKKVGEEATEAVIAAKGGEREQVVYETADLWFHTLVMLSASGVSVDEVLAELERRVGRSGLDEKAARGE | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 12245
Sequence Length: 114
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytopl... |
Q5UZW6 | MSDDTGDVIDELFAVIEDRKANLPEDSYTASLFTHEKGENAVLEKLGEETTELILAAKDDDTEELAHESADIVYHLLVLLSMKEMDIDDLRAELAKRR | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 11036
Sequence Length: 98
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytopla... |
B0R877 | MSDPLRELFDVIEDRKETMPENSYTASLLADDEKGENAALEKVGEEATEFLLAAKDGDTDELAHEGADVVYHMLVVLAQQDMDVEALLAELDDRR | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 10583
Sequence Length: 95
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytopla... |
Q18KL7 | MTDDELPKTVFDDLFSVIESRRETLPDDSYTASLFAHEKGENAALEKLGEEATETILAAKDSDSAAIQAESADLIYHLFVVLAMEEITLDDLREELHGRL | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 11142
Sequence Length: 100
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytopl... |
Q7VJ02 | MQDVFRQIDWERYELIPTIVQEKQSQQILMLAYSSKQSLELSLQTHLAHYFSRSKQRIWQKGEQSGHIQHIKEVKLDCDNDSLIFIVEQVGVACHTGEKSCFFRIFSLDKNCQNPPVSMPQKYPIGVYHILDDLYHIIEQRRCENIEHSYTASLLAKGVNGIGKKIIEEAGELCFALKDKDEKAIIYECADLFYHILVGLALEHITPERVLQELRRRMGQSGIEEKASRKH | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 26830
Sequence Length: 231
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytopl... |
A8A8G1 | MSDFLSELWLVIKKRIEEKPQGSYTAEIVKRGLPFAARKFGEESVELIVASLSEPRDSVIYEAADVIYHLMVLLALRGVDWAEVIKELERRSRAKSGAGGNS | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 11422
Sequence Length: 102
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytopl... |
Q88UE5 | MQNMEELYELIKQRKATPKKGSYTDYLFTKGLDKILKKVGEESTEVIVAAKNPGDDELTYETADLLYHVLVLLVERGVSFDQIKQELAKREGKMSDYKDRPEIKNL | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 12241
Sequence Length: 106
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytopl... |
Q8CQ91 | MNKLIDFSKGLVPVILQHAQTDSVLMLGYMNEEAYQKTLKEKKVTFFSRSKQRLWTKGETSGHFQHVESIHLDCDQDAILIKVMPQGPTCHTGSLSCFNSEIESRFKIQALAQTIHQSAKSNQSNSYTQYLLKEGIEKISKKFGEEAFEVVIGAIKHNREEVINETADVMYHLFVLLHSLDIPFSEVEQVLAHRHQKRNNFKGERKKVQEW | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 24334
Sequence Length: 211
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytopl... |
Q9EWK0 | MSKKTFEELFTELQHKAANGDPATSRTAELVDKGVHAIGKKVVEEAAEVWMAAEYEGKDAAAEEISQLLYHVQVMMVARGISLDDVYAHL | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 9919
Sequence Length: 90
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytoplas... |
A3CNS8 | MLETLYQEALKRKKEPKEGSYTSYLYDKGLDKILKKVGEEATEVVIAAKNADKNEMANETADLLYHLAVALVETGVSLEEVETVLQARQGKQSRIHDRPEIDHY | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 11807
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: Cytopl... |
Q03K84 | MLETLYKEALDRKNNPKEGSYTNYLFDKGLDKILKKVGEEATEVVIGAKNADKTEIANETADVLYHLAVMLVETGVSPEDVEAVLRARQGKQSNVHDRKEVTDY | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 11670
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: Cytopl... |
A4VGE1 | MSDTLTRLAEVLEARKGAAPDSSYVASLYHKGLNKILEKVGEESVETILAAKDAAVSGDSSDLIYETADLWFHSLVMLAALGQHPQAVLDELDRRFGLSGHAEKAARPQT | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 11865
Sequence Length: 110
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytopl... |
P74755 | MSHSDLPLANAVPLDKIRYNDQGLVPAIAQDYLDGTVLMLAWMNEAALAKTLATGQVWYWSRSRQELWHKGATSGHFQKLLGIRYDCDSDALLLTIEQKGDIACHTGERSCFHQLDGHKSPPPADMLTELARVIGDRRDHPTPESYTCKLLAGGDNKILKKIGEESAEVVMACKDDDPEAIAGEVADLFYHTLVALAHHNVDLRAVYRKLGDRRR | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 23945
Sequence Length: 215
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytopl... |
Q9X0C5 | MMTLYPVVVQERTTGEVLMLAYANEEALELTKKTGYAHFFSRERQKIWKKGETSGNTMRVVEIRRDCDDDAYLYIVDFPEDKVACHTGNRSCFFKVEHRFEETGSPTFWLELYRLVRKRKEEMPEGSYTVKLFKEGKGKIAKKFGEEAVEVITGYLQNDRENLVWEIADMMYHLTVLMADAGVTVQDVMRELEKRRK | Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Mass (Da): 23130
Sequence Length: 197
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Subcellular Location: Cytopl... |
P60542 | MITIDFQKMGGLIPAIIQDHATNEVLMVAFMDEKTLNLTLESGKTWFFSRSRNKYWMKGEESGNTQEVVEVLTDCDADAVVIKVKQNGPAACHTGNRSCFYVRWEDGQWVEHSEPLFDPAEVYKK | 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): 14263
Sequen... |
Q5FPD9 | MQWTAAFGSLARLVSRGDAFVTYVPPAPSIVDDIIAQVKFDANGLISALAQAPDGVVLMLAWMNADALRETLLTGRVCYWSRSRQKLWRKGETSGQQQKLIEARLDCDMDAVLMIVDQTGVACHTGRRSCFYHGVTPDGLRDTSQPEISAEELYGR | 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): 17207
Sequen... |
Q0BTI5 | MSDVFDIIRFNDQGLVTAIAQQHDTGEVLMLAWMNREAIEETLATGRVCYFSRSRNGLWRKGETSGQVQTLIELRVDCDGDALLVLVDQPGVACHTGRRSCFYRAMGKDGTVTTLTEPLIDPHTLYGS | 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): 14223
Sequen... |
B0R7I1 | MEEFDVDLDFGGAGHTDDGDGLVAVIAQDADSRDVLMLAYATREAVARTATTGRAHYYSRSRDELWEKGATSGNTQSVDEIRVDCDGDALLYLVAQTGGACHTGHESCFHRTLDGDTVGDQVFDPDDAY | 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): 13909
Sequen... |
Q18DH0 | MTDDAVTGSQDDAEIEIRFNSDGLVPAIAQDADSGEVLMLAYVSPTALKRTRETGQAHYYSRSREELWKKGETSGHTQHIREIRADCDADTILYLVEQTGGACHTGHQSCFYRTLDGTEVTERVFDPETVYE | 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): 14748
Sequen... |
P15516 | MKFFVFALILALMLSMTGADSHAKRHHGYKRKFHEKHHSHRGYRSNYLYDN | Function: Histatins are salivary proteins that are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). In addition, histatins exhibit antibacterial and antifungal activities. His3-(20-43)-peptide (histatin-5) is especially effective against C.albicans and C.n... |
Q0BWU4 | MTPFPPPLSGSAQDETPELRPRFDENGLIAAIAQDAGTGEVLMLAWMNAEALQKTIETGRATYWSRSRGALWVKGETSGHTQEVIELRVDCDQDAVLLKVRQTGGACHTHRESCFYRRIEGGVLSFTGKAD | 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): 14378
Sequen... |
Q81G03 | MEIFPAIDLKEGRCVRLYQGEFSKETVMNEDPVAQAIIFEKLGAEILHIVDLDGAIAGESLNLPVIEKICKAVRIPVQVGGGIRSLVTVEKLLSAGVEKVILGTAALYDKSFLEEAVRLYKEKIIVGIDAKNGFVATRGWLDLSEISYVSLAKQMESLGVQTIVFTDISKDGTLAGPNFEQLAILQKSVGIRLIASGGVASIQDVKKLNDMNIYGVIIGKALYEKTIDLEEVLQVTKLC | 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): 25967
Sequence Length: 239
Pathway: Amino-acid biosynthesis; L-hist... |
Q64RT1 | MIELIPAIDIIDGKCVRLSQGDYGSKKVYNENPVEVAKEFEANGIRRLHVVDLDGAASHHVVNYRTLDLIASRTSLIIDFGGGLKSDEDLIIAFENGAQMVTGGSIAVRNPDLFCRWIDRYGSGKIILGADVKDRRIAVNGWKVESTCELFPFLKDYTQKGIEKVICTDISCDGMLAGPSLDLYKEILAEHPTLYLIASGGVSSIADIEALHEAGVPAVIFGKALYEGRITLKELQAFL | 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): 26101
Sequence Length: 239
Pathway: Amino-acid biosynthesis; L-hist... |
A8FHR0 | MSEFTLYPAIDMRNGKCVRLVQGDYDQETIYGDSPLDMATRFANEGAKWIHLVDLDGAKAGNRVNHEHVLAIASSLDVKVQIGGGIRTEEDVAFYINNGVARVILGSSAVSNSAFVKKMLAQYGEKIAIGIDARNGFVSTEGWLETSKVKAEDLGKELAKEGAEVFIFTDIQMDGMLAGPNVESTVRLAEATGKQVIASGGISSVADLQKLSAQKQTGVSGAIIGKALYTERFTLAEAIEGLDRV | 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): 26204
Sequence Length: 245
Pathway: Amino-acid biosynthesis; L-hist... |
O35006 | MSAFTLYPAIDMRNGKCVRLVQGDYNKETIYGDSPYDMAELFEKEGAEWIHLVDLDGAKEGKRVNDRHVIEIAQKLNLKVEIGGGIRSENDVYEYLSAGVERVILGSSAVSNPPFVKKMLKQYGEKIAIGLDARNGFVSTEGWLETSTLKATELGKELANEGAEVFIFTDIATDGMLSGPNVKSTVELAKETGKSVIASGGVSSVADLEALARNEADGVSGAIIGKALYTNQFTLSEALERVKRK | 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): 26529
Sequence Length: 245
Pathway: Amino-acid biosynthesis; L-hist... |
Q8A7Z5 | MIEIIPAIDIIDGKCVRLSQGDYDSKKVYNENPVEVAKEFEANGVRRLHVVDLDGAASHHVVNHRVLEQIATRTSLIVDFGGGVKSDEDLKIAFESGAQMVTGGSVAVKDPELFCHWLEVYGSEKIILGADVKEHKIAVNGWKDESACELFPFLEDYINKGIQKVICTDISCDGMLKGPSIDLYKEMLEKFPNLYLMASGGVSNVDDIIALNEAGVPGVIFGKALYEGHITLKDLRIFL | 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): 26268
Sequence Length: 239
Pathway: Amino-acid biosynthesis; L-hist... |
Q1LT71 | MIIPALDLINSTVVRLHQGNYQQQRCYSDDPLYYLHNYLRQGAEMLHLVDLTGARDPSARQIKLLTSLLASVKGRTLVQVGGGIRNAADIEVMLQAGAHRVVIGSTAVKKPLEVQQWFKRFGPEALVLALDIRIDTNGKHWVAVSGWMENSGVLLEQVIDQYTQQVELKNILCTDISRDGTLSGMNIELYRLLCGNWPSIAFQSSGGIGSLTDIIKLRNIGVKGVIIGRALLEEKFTLAEAIACWQKE | 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): 27482
Sequence Length: 248
Pathway: Amino-acid biosynthesis; L-hist... |
B8D115 | MEVIPAVDIKDGSCVRLKKGDFNKRRVYSTSPVDVALYWEKHGASRLHIVDLDGAKSGWPTHLKTIREIALRVNIPLQVGGGIRSLKVIKKYLDSGVDRIILGTVALKNPELVKRALDNFGSNRIVVGVDARGGKVATEGWLKTSQVTVEDIISEMEEVGVKTFIYTDINRDGMLKGPDIEGIKRVLKSTKARIIASGGISSRQDLINLKAIGIKAAIVGKALYEGNLPLEVLNQYP | 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): 25910
Sequence Length: 237
Pathway: Amino-acid biosynthesis; L-hist... |
Q9HN14 | MTFESFTVLPAVDMQDGQVVQLVQGERGTERTYGDPVDAATDWVAAGAEALHLVDLDGAFEGARANATAVEDILDATDVSVQVGGGIRSAEDATALLDRGVDRVILGTAAIETPDIVGEIAAAYSDGVLVSLDAKDGEVVVEGWTEGTGMDPVAAAQRYADLGAAGILFTDVDVEGKQEGVRTDPVRDLVDSVDIPVIASGGVATVDDVRALEAAGAAGAVVGTALYEGNFTLADAQAAVED | 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): 24649
Sequence Length: 242
Pathway: Amino-acid biosynthesis; L-hist... |
Q31E65 | MLLIPAIDLKDGECVRLRQGLMDDATVFSGDIVAMAERWVNQGARRLHMVDLNGAFEGKPVNGDAVYQVREAFPDLPIQIGGGIRDLETIEAYLKAGVSYCIIGTKAVHNPEFVAEACKAFPGHIMVGLDAKEGMVAINGWAEVTDHNVIDLGKQFENDGVEAIIYTDIGRDGMMQGVNIQATQALAKALNIPIIASGGITNLDDIRALATIEKDGVSGAITGRAIYEGSLNFKEGQALSDELSKA | 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): 26285
Sequence Length: 246
Pathway: Amino-acid biosynthesis; L-hist... |
B1ZW12 | MTIYPAIDIKGGRCVRLTQGRAEQETIYAQNPADVAMQFRAAGSEWVHVVDLDGAFAGEPQNLAAVQAIVAVGMKVQFGGGLRTRAAVERALALGVSRVVLGTRAAESESFVGELVQAFGDKIAVGIDAKNGKVAVKGWVATADLSTLVLARRMDTLGVATLIHTDIGTDGMLTGPNLAAQEALCSAVKSRVIASGGVSRRDDVVNLAKLAQRHANLDGVIVGKALYERRVELADLLSLAAAS | 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): 25360
Sequence Length: 243
Pathway: Amino-acid biosynthesis; L-hist... |
A1R562 | MTTSAQSVLELLPAVDIVDGQAVRLLQGEAGSETSYGTPLEAALNWQNDGAEWVHMVDLDAAFGRGNNAALISDVVSQLNVKVELSGGLRDDESLERALELGVARVNLGTAALENPEWTRKAIDRFGDKIAVGLDVRGTTLAGRGWTKEGGDLWEVLARLEDAGCARYVVTDVTKDGTLQGPNVELLRQMVEKTGKPVVASGGISSLEDLRVLRELVPLGVEGAIVGKALYAGAFTLPEALDVAGRR | 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): 26175
Sequence Length: 247
Pathway: Amino-acid biosynthesis; L-hist... |
Q9PBC9 | MNFIVYPALDIRNGAVVRLQQGDYARQTRYDDQVLPRALAFADSGATWMHLVDLDAAKAGGYTLAPLLRQMTRATGLQVQTGGGVRSRDDVARILDAGAARVVIGSLAVRESARVIEWLQAFGPERITVALDTRQDAGGVWRLPVHGWTEVAEATLDVLAQQYAAAGLRHLLCTDIARDGMLSGPNMDVYTYLRALVPAVQLQVSGGARDVADVVAAKMAGCAGIVLGKALLEGRLALKEAVQQGSVADPSDPLPCGELTEPVCR | 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): 28229
Sequence Length: 265
Pathway: Amino-acid biosynthesis; L-hist... |
P9WMM1 | MTAKSVVVLDYGSGNLRSAQRALQRVGAEVEVTADTDAAMTADGLVVPGVGAFAACMAGLRKISGERIIAERVAAGRPVLGVCVGMQILFACGVEFGVQTPGCGHWPGAVIRLEAPVIPHMGWNVVDSAAGSALFKGLDVDARFYFVHSYAAQRWEGSPDALLTWATYRAPFLAAVEDGALAATQFHPEKSGDAGAAVLSSWVDGL | 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 Activit... |
Q9K0H2 | MQTAIIDYGMGNLHSVLKSVRTAGQLAGKNTEIFLSGDPDRVSRADKVIFPGQGAMPDCMAALKRDGLDEAVKDALKNKPFFGICVGAQLLFDHSEEGNTDGLGWFGGKVRRFERDLRDPQGCRLKVPHMGWNTVRQTQNHPLFKDIPQDTRFYFVHSYYFAPENPETILGESDYPSPFACIVGKDNVFATQFHTEKSHDAGLTMLKNFLNW | 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 Activit... |
Q5YYP7 | MTRKSVALLDYGSGNLHSAERALVRAGADVRVTADPDAALAVDGLVVPGVGAFAACMAGLRAVRGEKIIGQRLAGGRPVLGICVGMQILFERGVEFGVETEGCAEWPGVVERLDAPVLPHMGWNTVSAPADSVLFAGMDADTRFYFVHSYAAQRWELPPNEHFAAPKLTWAEHGVRFLAAVENGPLSATQFHPEKSGDAGAQLLRNWVDSL | 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... |
Q8ESS0 | MIAIIDYGAGNIKSLQFALDKLNKHSIVTTEAAEIKQADSIILPGVGAFKDAMEAIRQLQLDSVIQEEAQKGKPILGICLGMQLFYEQSLENGDWEGLGLLKGSIKRISGEVKVPHMGWNTLDIQQASPLFDSKLENPYVYFVHSYAVSSFEENTLLASSQYGQLIPAIVQKGNITGMQFHPEKSGEFGIELLKRYEEMIR | 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... |
Q4FNT5 | MNVTIVDYNSGNISSVINSFKEVAKDKVNIEVTSDLNKIRSSDKVVLPGQGSFKSCVDALNAINGLVETLNEFTVTNKKPLLGICVGLQMFADLGYEETETKGLGWISGKVSKIDNQNNKFKLPHIGWNEINIVKESKIFEGIKNKSHMYFVHSYEFIPDDKSVISATTDYSSNIVCSVEKENIFGTQFHPEKSDKLGLKIIENFLNL | 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... |
A8AAK3 | MPLTKRIIPCLDVKDGRVVKGVSFQNLRDAGDPVELAAYYQEQGADEIVFLDISATPEGRETMIEVVRRTAENLSIPLTVGGGVRSLEHIEKLLKAGADKVSINTAAVKNPLLITAAAEEFGSQAVVVAIDAKRKGNGWEVYVSAGKVPTGLDAVEWAKKAEELGAGEILLTSIDYDGTQNGYDLELTRAVSEAVKIPVIASGGAGELEHFYAVLTEGKADAALAASVFHYGKFTVGDVKKYLIQRGVPVRPCCW | 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-b... |
A6WC96 | MSVAVRVIPCLDVDAGRVVKGVNFADLRDAGDPVELARRYDAEGADELTFLDVTASSGSRETTYDVVRRTAEQVFIPLTVGGGVRSVADVEKLLRAGADKVGVNTAAIARPELIGEIAHRFGAQVLVLSVDARRTLPGEPTTASGFEVTTHGGRRGTGLDAVEWAARAAELGAGEILLNSMDADGTKAGFDLEMLTEVRARVTVPLVASGGAGAVGHFPPAVAAGADAVLAASVFHFGQLTVGEVKDALRAAGSAVR | 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-b... |
Q02133 | MLTKRIIPCLDIKNGKVVKGINFVGLREIGDPVELAKIYEEQCADEIVFLDITASFEEREIIGELIGRAARELSIPLTVGGGIRSIDDFRRILARGADKVSVNSAAIENPELIRQAANEFGVQCVVVAIDAKKRADHRGYDVYIKGGRENAGLDLVDWAKKCERLGAGEILLTSMDKDGTKTGYDLEMLNDVCTAVNIPVVASGGCGKISDIVEVFQNTRSDAALFASLFHYGEATVDEVKDELIKNNIPARIIKKETL | 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... |
Q88UE3 | MLAKRIIPCLDVADGRVKKGVNFVNLTDVGDPVAIAAAYQQQGADELVFLDIAATNEHRETMAAMVEQVSAQVFMPLTIGGGITSVADMQRILRAGADKTAINSAAVANPELIRAGAEKFGNQCIVVAIDAAWDAAAGQYRVYTHGGQQATDLDAVAWAKQAVALGAGELLVTSMDRDGTKAGFDTKLYQALGATVNVPIIASGGAGNLQDFVDVFSTTPVDGALAASVFHFGELTIADVKATLRKQGVVVR | 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-b... |
Q9RDX2 | MSNVRLIARLDIKGPNLIKGVHLEGLRVVGNPNEYAMAYYAQGADELIYMDTVASLYGRNNLSEIVKTTAENVFIPITVGGGIRSVDDAEQLLRCGADKVAINTAATKNPTLISDIARRFGSQCVVLSIEAKRTVNGRWEVMTDNGREHTGMDVVDWARNGEKFGAGEILLTSIDQEGTRKGFDLELVKQVSSMVSIPVIASGGMGKLEEFN | 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... |
O66455 | MREAEVFRETRETKIKLYINLDGSGNYEVNTPVGFLTHMLESFAKHGRFDLKVEAEGDVHVSHHHTVEDCGIVLGQAVLKALGDKKGIRRYGYSIIPMDEALVLSSIDISGRPLFFYEDKDLRGKITEFDFELIWEFFKGFALESRSTLHIKVLDGKILHHVAEACFKSFAITLKEAVKVEGSGVPSTKGVI | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21587
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: Cytoplas... |
Q6NPM8 | MLAQSHFFSKSFDLIPPQSPALRSANPSLRISSSYSNSRLSFLSSSAIAVPVSRRRFCLTMASNSKRPNISNESPSELSDTELDRFAAVGNALADASGEVIRKYFRKKFDIVDKDDMSPVTIADQMAEEAMVSIIFQNLPSHAIYGEEKGWRCKEESADYVWVLDPIDGTKSFITGKPVFGTLIALLYKGKPILGLIDQPILKERWIGMNGRRTKLNGEDISTRSCPKLSQAYLYTTSPHLFSEEAEKAYSRVRDKVKVPLYGCDCYAYALLASGFVDLVIESGLKPYDFLALVPVIEGAGGTITDWTGKRFLWEASSSA... | Function: Phosphatase required for histidine production. Acts also on L-galactose 1-phosphate (L-Gal 1-P), D-myoinositol 3-phosphate (D-Ins 3-P) and D-myoinositol 1-phosphate (D-Ins 1-P).
Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate
Sequence Mass (Da): 38235
Sequence Length: 346
Pathway... |
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