ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8KF55 | MLIIPAIDIKEGKCVRLTRGDFAQKKIYLDNPCDMAVIWRKQNAKMIHVVDLDAALTGETVNFERIREIVNVLDIPIQVGGGIRSVEAVEKYLDIGVSRVVIGSAAVTNPGLIADLLKKYRPSQIVVGIDAEHGVPKIKGWTESSNMQDYELAGEMKKLGVERIIYTDITRDGMLQGVGYETTKRFAEKAGMKVTASGGATTSDDLHKLRSLEKYGVDSVIIGKALYECNFPCQELWYAYEQGLGIDGEFSTARKKECCS | 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): 28711
Sequence Length: 260
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
|
Q7P0F0 | MLLIPAIDLKDGQCVRLRQGAMDDATIFSDDPVKVAAHWRDQGARRLHLVDLNGAFAGKPKNLAVIRDILGEVGEDMPVQLGGGIRDLDTIEAYLDMGLAYVIIGTAAVKTPGFLHDACDAFPGQVIVGLDAKDGMVAIDGWAKITNHNVIDLAKRFEDYGVNSVIYTDIGRDGMMTGVNIEATVKLAQALTIPVIASGGLTNLDDIRALCAVEDEGIEGAITGRAIYEGSIDFAAAQTLADELAG | 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): 26034
Sequence Length: 246
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
|
Q97KH9 | MIILPAIDIKQGKCVRLYQGRFEKSSVVAESPALTAKSFENDGAKYIHVVDLDGALEGEIINLDAVKSIVQVTSVPIELGGGIRNIKVVEKLINIGVKRIILGTAALKDKEFTREAIKEYGKSIAVGIDAKDGYVAVNGWLNVSKINYIEFAKIMEDMGTEDIILTDISKDGTLKGPNFDMLKKLQENVNCNITASGGIKDLDDLIKLKEMNIYGAIVGKAIYSEKINLKEAIAVIEKR | 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): 26112
Sequence Length: 239
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
|
Q1D4M2 | MIAIPAIDLREGACVQLVGGSYAAEKVRVEEPLEALKQWRRHGFRAFHVVDLDAALGKGSNADAIFQLTAYERGLTFSVGGGVRDSDRVETVLSGGAEFVVVGTRAIEDAGWLADIANRFPGRVVVAADVKGREVVTRGWTAGSHRDIREVLAAFEPLPLGGLLVTAVHKEGQLSGVDLPLMREVASTSRHRLYASGGVTTMEDLRALAAAGAYGAVIGMALYTGRLDASAVAREFAG | 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): 25158
Sequence Length: 238
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
|
Q3IT10 | MFPSFEVIPAVDMQDGQVVQLVGGERGTETEYGDPVAAAQRWVDAGAETLHLVDLDGAFEGERANADAVEAVLEATDVSVQLGGGIRTVDDADSLLSMGVDRVILGTAAVENPDIVGEINDRHPGSVVVSLDAKDGEVVVSGWTESTGLDPAEAAARYEAEGAGGVLFTDVDVEGQLSGVRADEIARVVDAVDIPVIASGGVSTLSDIEALKDAGAAATVVGTALYEGEFTLEEAAAVV | 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): 24424
Sequence Length: 239
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
|
Q7RXQ8 | MTRFRPCIDLHAGQVKQIVGGTLDSATSELRTNFVSPHPPAYFAKLYRDNDLSGAHVIMLGPGNKEAALESLKAWPGGLQVGGGITDANAREWVEAGAEKVIITSYLFPNGKFSQSHLDAVLAALDGDKSKLVIDLSCRRQGDDRWFVAMNKWQTITDMEVSEESIKALEPYCSEFLIHAADNEGLQKGIDEKLVQRLSEWCSIPVTYAGGGRNLEDLETVKRLSGGKVDLTIGSALDCFGGKGVTLQECVEWNRRQ | 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): 28142
Sequence Length: 257
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
|
A9A5X1 | MKIIPAIDLMDGQVVRLYKGDPKQKTVYSDDPVSVAKKWQKAGADMLHIVDLDATIGTGSNLDLIEKISKELSIPVEVAGGLRNEEIIDRAISFSNRVVIGTMAFKDKEMLQRIAKKYDFSKIVISVDHIDGFIVTHGWQESTKTPLLDAINEFVSMGFTEFLLTNVSKDGTLEGPDLEYLEKACAVQNANVIASGGISNIDDVSDVQRKNAFAVILGKALYENKISIEEAKQLVN | 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): 25960
Sequence Length: 236
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
|
A6Q4V9 | MEILPAIDLKDGKAVRLTKGLMESAKIYSDEPWQVAKRFEEMGSRWLHLVDLNGAFAGEPKNLEQIKKIRANTSLKIELGGGIRDEETIRKYIDLGIERLILGSIAVKNPQFVKAMAAKYPIAVGIDAIDGFVAVEGWAKTSTMRATDLAREFAKSGVQAIICTDVGKDGTLSGVNVDFTVSIAEASGIDTIASGGVRDIEDIKKLQATGTVAGVIVGKAFYEGTLDLEEAFRLVQNG | 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): 25645
Sequence Length: 238
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
|
Q970Z2 | MLKVVPSIDISEGKAVKRIRGVKGSGLILGNPVKIAYEIYEEGYDYLHVVDLDSAEENGNNEEYVKDICKIGFKWVQVGGGIRNVEKAERLLDYDCSAIVISTLPIKDPKSFMDIQKIIGKDKILLSVDYDSSGYVLIRGWKEKSIKVLDFLLSYDSLGYIFTYVENEGTKRGIDNNVKNYVIRIKGLKEYAGGIGSIEDLYKLNEYGINYAIIGMSFYSGSLRGIKYVY | 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): 25878
Sequence Length: 230
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
|
Q67KH9 | MRLDLYPAIDLKDGQVVRLRQGRMDEATVYGVDPVRIAARWAEAGARWIHVVDLDGALRGRPQNAAAVRAIVEALRQRHPGVRVQLGGGLRTLEALEAALALGVSRAIIGTSALEGDVAARAVARFGPDRVAVSIDARGGFVAARGWVEVTRVRAVDLAVRMREVGVRTVVYTDIATDGMLTGPNFAELEMMGRTGLDVIASGGISSLEDIRRLTEIPGVAGAIIGRALYTGAVDLAEALSLCGETRDT | 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): 26416
Sequence Length: 249
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
|
Q2LVE9 | MVIIPAIDLKGGKCVRLLQGDFERVTVYSDHPVEMAKAWREKGAERLHLVDLDGSIAGNPRNAAIISQIVKSVGVPVEIGGGIRDISTIQRYLDMGVQWVILGTAALKDRSFVYNACDLFPGHVILGIDANNGKVAVEGWTEQSAITALELAISYENRGIAAVIYTDISRDGMQTGVNVEGTRVLAEAVDIPVIASGGVATLDDIKRLLPLEESGIAGVIIGKALYSGAIALEEAISLAKSS | 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): 25636
Sequence Length: 242
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
|
Q3AYT2 | MEIIPAIDLLDGACVRLHQGDYDQVTRFSDDPVAQALSWQSQGAKRLHLVDLDGAKRGEPANDAAVRAIANALDIPVQLGGGVRSIERAEDLLNCGLERVILGTVAIEQPDLVQVLAERHPGSVVVGIDANKGKVATRGWLEQSDVLATDLARRFSDSGIAAIITTDIATDGTLAGPNLDALREMAQASSVPVIASGGIGCMADLLSLLPLEDQGVSGVIVGRALYDGRIDLAEAIGAIGDDRLQDITCGSTDLA | 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): 26606
Sequence Length: 255
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
|
Q0AW40 | MIIYPAIDLKDGQCVRLVQGRVENKTVYSDAPANVARSFQEQGASFLHIVDLDGAFQGSPQNLKAIEAIAAAIDISFQVGGGLRQLSDVEKLLALGASRVIIGTRAVSHPDFIANLLDKFGPERIVLGLDAKEGMVAVEGWVSTSSVSAIDFGLQMKALGIQTAIYTDVSRDGLLQGPNLAAIKEMASSTGLDIIASGGVSSLDNIRALKELENDGVSGAIIGKALYDGKIGLVDALREAESKF | 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): 25656
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
|
P74561 | MKILPAIDLLGGKCVRLYQGDYDQSQVYHEDPVEVARQWQAQGASRLHLVDLDGAKEGQPVNLTAIANIVEALTIPVQVGGGLRDRNRVKQLLDLGVGRVILGTIAVENPDLVGELCAEFPGQIVVGIDARNGKVATRGWLETSTVEAGELAQRMEKLGAAAIIYTDIHRDGTMQGPNLDALRQLASQLTIPVIASGGVSQVEDLLNLLSLESLGVNGVIIGKALYTGDIQLAEAIRAVGNGRWQDVPPLDFPRLG | 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): 27350
Sequence Length: 256
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
|
P44340 | MINITIIDTGCANLSSVKFAFDRLGYNTEITFDLNKIKSADKLILPGVGTANAAMYNLQERQLIETIQNLTQPVLGICLGMQLMTEFSEEGNVPTLNLISGKTNRIPDTGLPLPQMGWNRVQFVKNCPLFDGIVQNSHFYFVHSYAVSPNEHSVAISNYGVNFSAAIAKENFYGVQFHPERSGKNGALLLKNFVEKVPF | 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): 22048
Sequence Length: 199
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
|
Q9K6Z4 | MLGIIDYGMGNLHSVSKALERLSWSYIVSEQPEELQKADGLILPGVGSFHDAMSILNETGLTAFIKDWVDEGKPLLGICLGMQLLFEESEENKRTKGLSLLPGRVIRFPGVATDGSTYKVPHMGWNQLTFRKPNHPLLTDVEEGHVYFVHSYVVKTDADDVLLATSHYYETVPAVVGRGNILGTQFHPEKSSNVGMSILRNYGAMVEKGVKARG | 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): 23603
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: Cytoplasm
EC: 4.3.2.10
|
Q5UYV3 | MSVRQTTADVVVVDYGLGNLRSVTRGLERAGANVSLSEDPAEFDAADGIVLPGVGAFSEGMDNAGPFREALVEQAEAGKPLFGICLGMQMLLTTSEEADHEGQGDAEGLDLIPGKNVRFSRDQTVPHMGWNELDVTRDHPLVEGVDSVGSKTPRADGTGGSVDGEHAYFVHSYYAVPDDESATVATTDYGTDFASIVANDAGNVFGTQFHPEKSGETGLRILRNYVDYCLDH | 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): 24699
Sequence Length: 232
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
|
Q7VIW9 | MSKLRVGIINYGVGNLGSVQNAFAFIQTHFSDVLPHTLEIKVESHPERLQDYDKLLLPGVGAFGNAMTHLKNTHLDEAIREFVQSGKFLIGICLGMQLLFEQSEEFGNHKGLGLIEGKVVGFEHIAPLKVPHIGWNSCNFTPEGKHSKLFRGIADGSFFYFVHSFHIQTQPQFILAQCTYGYPFGAIVHKDNLFAIQAHPEKSHNVGLRLLANFLTL | 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): 24227
Sequence Length: 217
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
|
Q31E66 | MTDQKLVTVIDYGMGNLRSVAKAAEHAADSNTRICISDKAEDIRSADAIIFPGQGAAKACMKALNETNITHALIQAATEKPFLGICMGLQVLMTHSQENEGVDCLDILKGDVQKFDLSGHPELKMPHMGWNQIHQTIDHPLWHNIEQNSRFYFVHSYFVSPHDKQIIAGETTHGKRFTSAIAQNNLFAIQAHPEKSADAGLQLFKNFLNWNGQ | 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): 23666
Sequence Length: 213
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
|
Q02132 | MKKIVIIDYNIGNLQSVQAAFLRLGQETVISRDLEEIRKADALILPGVGAFPTAMNNLKKFNLIELIQERAAAGIPILGICLGMQVLFEKGYEIEERQGLGLLKGEVIPIKTNEKIPHMGWNQLNLAKASPTTHYLSDNDEVYFVHSYQATCPDDELIAYTTYGEVKIPAIVGKNNVIGCQFHPEKSGEIGRKVLKAFLEEI | 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): 22454
Sequence Length: 202
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
|
Q88UE1 | MFAIVDYDTGNTRNLKKAFDYLQVSTILTADPQQLAAADAVILPGVGAFAAAMAALKERQLVGVLQALARSGKPVLGICLGMQLLFESSSEYGEHAGLGLLSGRVSALPTDLNVKVPQMGWNQNELRRPDSPFASIDAAYTYFVHSYYAVCPATEIVATVQHGVQVPSIVQQQNVIGMQFHPEKSGRVGLQQLAAFKEMVSANDFSSN | 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): 22347
Sequence Length: 208
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
|
Q9ZGM1 | MIGILDYGVGNLKAFANVLKGLNFHHQIVKTEQELKGCEKIIMPGVGSFDSVMNKLIESGIRDVLSDLIINKKIPILGVCVGMQILASSSEEGSKSGLGWIRGRVKKFNFDRSDFSLTIPQIGWNEVNSTKENTLLKNLEKNPRFYFLHSYYIECEDKKDVIAIANYGGDFTCAVNRENIYGTQFHPEKSHHNGVALIRNFASL | 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): 22841
Sequence Length: 204
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
|
P61780 | MIAILDYGMGNIHSCLKAVSLYTKDFVFTKDHSTIENSKALILPGDGHFDKAMENLNSTGLRKTIDKHVTSGKPLFGICIGFQILFESSEEIAQGSKKEQIEGLGYIKGKIKKFHGKDFKVPHIGWNRLQIRRKDKSVLLKGIGDQSFFYFIHSYRPTDAEGNAITGLCDYYQEKFPAVVEKNNIFGTQFHPEKSHTHGLKLLENFIRFI | 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): 23829
Sequence Length: 210
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
|
Q8Y9G5 | MLTKRIIPCLDVTAGRVVKGVNFVSLTDVGDPVEIAKAYNEAGADELVFLDITATVELRQTMIDVVERTAEQVFIPLTVGGGISSVSDMKELLQAGADKISLNSAAIKRPELIQEGAAKFGNQCIVVAIDAKWNGTNWSVFTRGGRNDTGLDAIEWAKKAVQLGAGEILLTSMDGDGTKNGYDIPLTKAISEAVSVPVIASGGCGNAAHMVEVFEKTKATAALAASIFHYGELSIKNVKTTLLEKGVNIRP | 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): 26533
Sequence Length: 251
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
|
Q8DTR3 | MLKKRIIPCLDVKDGRVVKGVNFVNLTDVGDPVDAARAYYEAGCDELVFLDITATSDNRETTVDMVRHVADQVFIPFTVGGGIRSVDDMNKMLKAGADKVAVNSSAIANPQLIKDCAEKFGSQCVVVAIDARKEADDSWHVYVAGGRKDTGIDLLAWVKEAVQLGAGEILLTSMDKDGTKSGFDLDMLNAVAQLADIPIIASGGAGNMEHMVEIFEKTPATGALAASIFHYGEVSIADTKKAMKEHGIEVR | 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): 26874
Sequence Length: 251
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
|
Q4J8I9 | MTSKRIIPCLDVKDGRVVKGVNFLNLVDKGDPVELAARYEEEGADEIVFLDITATIEGRKTMMNVVKDTASVISIPLTVGGGIRSLDDVSKILGNGADKVSINTAAVENKDLVSISSAEFGSQAIVVAIDVKRIGNDYYVFTRSGKYNTGINAISWAKEVEKLGAGEILLTSIDRDGTREGYDIEITELISKSVNIPIIASGGAGKIDDFLGILKVADAALAAGVFHDGVIRIMDLKKYLGKNGVEVRM | 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): 26607
Sequence Length: 249
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
|
Q30NR6 | MNYFAKRIIPCLDVKDGRVVKGVNFVGLRDAGDPVEVAKRYNQEGADEITFLDITASSDNRDTIVDIVAQVAREIFIPLTVGGGIRKLEDIYRLLNVGCDKVSVNSAAIKRPQLIDESAKRFGSQCIVTAIDVKKTGDRYNVYLNGGRVDTGIDALEWAKEVVERGSGEILLTSMDADGTKAGFELSITQLISEAVNVPVIASGGAGTMKHIKEAFEHGADAALAATIFHYREIDIMDLKRYLHDNNIPVRL | 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): 27539
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
|
A0RZ75 | MRKNESQRETKETEVSVSVLLDGTGSTTVNTGQPFLDHLVSSLGKHAMFDIDLKASSRDGIVHHLVEDVAITLGGAIDKALGDRSGIMRFGHASVPLDESLSEAVVDLVKRPYHRIEMKIKRPEVEGIAKEDLEHFFDSLLRNLDCCIHLTVKYGNNDHHRVESAIKSLAVALRMAVSADPRREGPPSTKGSM | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21221
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
|
O33564 | MRKAEISRKTAETDISVTVDLDGTGRYDIRTGVGFFDHMMDQLARHALIDITLRCEGDLHIDDHHTVEDCGIALGQALTRALGDKRGIRRYGSFHLAMDDALVRAALDLSGRPFLVWNLPFPTEKIGSFDTELVREFFQALATHGGITLHVDLIHGVNSHHIAEAAFKAVARSLREAVEPDPRRADAIPSTKGML | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21565
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
|
A9WDZ1 | MSEVSSVVNRIRRATIERVTGETNITLTLTIDGSGQADVQTGIGFLDHMLTLWARHGLFDLQVRAQGDLHIDEHHTAEDVCICLGRAIDQALGERAGIVRTAHSFVPMDEALALVAVDLGGRPYCVVQADFVTMRVGQLGTDLVAHLFESVAFNGRFNLHAQVMYGRNDHHKIEALFKAFGRALDAATRIDARLGGTIPSTKGVL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 22299
Sequence Length: 205
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
|
A1ATG7 | MTRTATIERNTSETRIRLTLNIDGRGETSIGSGVPFLDHMLNLFARHGLFDLSLEACGDTQIDFHHTVEDIGIVLGEAFKQALADKQGINRYGQVTVPMDETLASAVVDISGRPYLVYNVDLPKAKVGDFDVELAQEFFQAFANHCGINLHINLLYGDNLHHIIEACFKAVGRAMDMATRLDPRVEGVMSTKGVL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 21504
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
|
Q4FNT4 | MNRIGKVSRKTKETSISVEVNIDGKGQYKIDTGIGFLDHMLEQLSKHSLIDLKVKAKGDTHIDLHHTTEDTGIAIGEALKKALKDFKGIKRYAHAMIPMDETLTRVAIDVSNRPYLIWKVKLKVERLGEMDTELFKEWFQAFSQSAGITLHMENIYGDNSHHIIESCYKALARSLRIALEIDPRNKKSIPSTKGSL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 22173
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
|
O94153 | MSAGLPIRTATVTRNTNETQIVCSISLDHTPGVDQQIIDIQTGIGFLNHMLHAMAKHGNMSLTLHCKGDLEIDDHHTAEDCALALGEAFKLALGERRGIRRYGTGFAPLDEALSRAVLDISSRPYFCGDLPFTREKIGDLSTEMIPHVFESFATAAGVTLHVDCIRGVNNHHIAEASFKALALAIREAITRTGGNDVPSTKGVLL | Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Mass (Da): 22127
Sequence Length: 205
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
EC: 4.2.1.19
|
Q3AD52 | MNKPRYFKEAFAQLKPYEPHLVSYEIKLDANENPYLFPKSLLEEIFSKIGTRDFPLYPDPLAGRLRIRLSEKLGVLPENIVLGNGSDELILCLYLAFGGYGRIALSFSPSFVMYRHHAFVTQTEFFEVSYRDDFSLDLDETKKAIEKYQPHLVFLANPNNPTGTLVDIETIKKLLAYDHLLVVDEAYVEFSGVSAIDLLKKYQNLVILRTFSKARALAGLRLGYLVASVDVVKEIIKVKNPYNVNVFSQIAGEVVLANEEVFQGEIKEIVAERERLYNQLASLGLKPVKSHANFILVEFGEKAKKIHQELINHGILVRYLGGALANYLRITVGTPEENRQLLKKLGEIL | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39608
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
|
Q9A671 | MPKPGIMDIHAYVGGKSKVEGIAHPVKLSSNENILGSSDKAKDAYRNAVDRLHIYPDGKANFLRAAVAERYKLEPERLTFGDGSDEIFALLCQVYLEPGDNIVQGEHGFAAYAIGARACQGEVRMAKEVNHRVDIDEVIKCVDERTRLVFIANPANPTGTWLTGEEIRALHAALPPSVVLVLDGAYAEFCSDPHFEDGLELARTAENVIVTRTFSKIHGLAALRVGWGYAPEHIIAPIERIRPPFNTSIPAQEAAVAALFDDDFQDRSRALVEQWRPWLAQQLGGLGLEVTPSAANFVLATFPTTPGKTAPEAEAFLASKGYLVRAVGNYNLPHAIRITIGLEEQNRAVVELLSQFMGR | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39262
Sequence Length: 359
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
|
Q47GP2 | MSLADQALSYVRAISPYQPGKPITELAREMGIPVEKIVKLASNENPLGMSPKARKAVEAAISGIERYPDQFDLIAKVAERCGVSSNQIVLGNGSNDVLDLIARVFLAPGRSAVFAQHAFAVYPLATLSTGAELISTPAKNYGHDLNAMRAAIRPDTRIVWIANPNNPTGNFLPYPEVRAFLEVVPKDVVVVLDEAYNEYIPPAERVDTATWIKDFPNLVVCRTFSKIFGLAGLRVGYALASTEVADLMNRIRQPFNVNNLAIAAAVAALDDHLFVADSYELNRRGMEQIIAGLKRFGLEHIPSHGNFVTFRAGDAAVVNQKLLKQGVIVRPIGGYGLPEWLRVTIGTEPENARFLEALEKAL | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39502
Sequence Length: 362
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
|
Q5FRR4 | MIPSHTAPSPFFPWSHRMNTAPECRTPPLSLARAEVRQLPVYNAGLSEDAVRAKYGIPRITKLGSNENPYGPSPAALEHWTEIASSLFRYPDASAEGLREELSRQTGIDTDRIVIGNGSEQIIRMICEAFLSPGDRLVTVLPSFGLHLIWPQMMGARAEAIPMTADARFDLPQLHQAVTSDPLKVLMFSNPSNPVGCLMTGDAMQSLIDACPADTLIVIDEAYWEYARSSPDYADSLTILKNQSRPWMVLRTFSKAYGLAGLRVGYALTSDPGLTAVMTRVRDPFNSNSAALEMARLSLLDQEHMHKTVGATLAEGKALKAALEERGYFVAQSFANFLFFNARESASALAERLLEQGVIVKPWKEKGYETWIRVSIARPEDSQAFLAALDRVRQPSHSSAA | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 44168
Sequence Length: 401
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
|
Q4QN73 | MTITTLSRQNIQALTPYQSARKLGGNGTIWLNANEYPTSPEFQLSGKDLNRYPEPQPQRVVQAYANYAGVSTENVLVTRGGDEGIELIIHTFCEPKQDAILFCPPTYGMYAVSAETAGVLSKSVPLTDDFQLNLPEIKNHLNDVKVVFVCSPNNPTGNLLKQSDILDLLQITAGKAIVVVDEAYIEFCPEASVINLLKNYPHLAIIRTLSKAFALAGLRCGFVLANPELIDILSKVIAPYPIPVPSADLAEQALRPANIATVQALTQELLSNRQWLAKALLVLHQVEKVYESEANYLLIKCQNGQAVFKALWEQGIILRDQNKTLHLQNCIRITVGTRNECEKVVEAIKEVK | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 38891
Sequence Length: 352
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
|
Q5QZ49 | MAEFNALELVNPGVKQLRPYQAGKPTSELQRELGLQHVVKLASNENPLGLSEKVKTALEAELTDLVRYPDANGYYLKSRLAELNEVGTQQITLGNGSNDVLEILARTFVSDKDEVIFSQHAFVVYPLVTQAIGAKPVAVPAVDYGHDLDGMAKAVTDKTKMIFIANPNNPTGTFLSTSALKSFLDKIPQHIIVVLDEAYYEYVPEDQRAPSVEWIKEYPNLVVSRTFSKAYGLAGLRAGYAVSHESVADVLNRIRQPFNMNSLSLKAAEVVLDDHAYLQKAVELNAQGMQLLTEFCEESGLNYIPSYGNFLTIEVGPGAEKLYDELLHEGVIVRPVGGYELPNHLRVSIGLPEENQAFIKAMKKLRG | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 40505
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
|
Q5ZW88 | MSILNLVRADLLNSKNYVPGGESARYRSHANELPWSPVTMGEHNLNYYPNIGLQIELQKQLAKRYQIYSDQIILTRGSDDGIDLTTRLFLTAGKDAFMQFPPTFPMYAFYVRLQQAELIECPLDRRTNFRLTLDQIENSWKPNCKIIMFCSPNNPTGNLVDLNLIAKTCELYANQSIIVVDEAYIEFANAPSATSLIGEFENLIVLRTLSKAFGLAGLRLGCIIAQSPIIQAFNKIIAPYSIATPSMELAKRALNNSDWFTKTIEQIKSSRAWVIKKFADNPIIEKIYPTETNFILIQTRFSKQLTTWLAHYGIAVRDFPSSSLLHDHLRITVGHDEQNQLLINTLSSFNADVAGLNYEKDFIY | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 41329
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
|
Q65S79 | MTFLQQANTGVQALSPYQAGKPIEELERELGISNIIKLASNENPFGFPESAKKAIQNQLDNLTRYPDSNGFSLKAAIAEKFNLQPEQITLGNGSNDLIELIAHTFATEGDEIIFSQYAFIVYPLITKAINAKAREIPAKNWGHDLEAFLAAINEKTKLIFIANPNNPTGNFLTEAEIDSFLAKVPPHIVVALDEAYTEFTAKEERVNSLALLKKYPNLVVSRSLSKAYGLAGLRIGFAVSNPEIAGLFNRVRQPFNVNSLALAAAEAVLNDDDFVEKAAENNRRELKRYEEFCQKYGLQYIPSKGNFITIDFQQPAAPVYDALLHEGVIVRPIAGYGMPNHLRISIGLPEENQRLFDALIKILNLK | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 40606
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
|
Q82WM3 | MTSPSPDQVIRQEILALSAYHVPPAKDMVKLDAMENPYRLPPFLCEEISRIAADTSINRYPDPHAAALKEVLSTTLSVPAGMEIMLGNGSDEIIQIIMLAAAKPEAKLLTIEPGFAMFKMIATFANMQYIGIPLKPDFSLDIDRMLAAIERHQPSVIFLAYPNNPSGNLFDTSALEKIIEISPGLVVIDEAYHPFAGKSFIGRLADYPNLLVMRTLSKLGLAGLRLGLLAGRPEWLSHLEKLRLPYNVNVITQLVATKIMQHYDVLQQQADAIRQTRTRLRTFLENLNGIEVFPSNANFILFRLDGASQIFRLLQQHGILVKNLDNSHPLLKNCLRVTVGTPEENDRFCNTLQDLIAGN | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39979
Sequence Length: 359
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
|
Q8YV89 | MTNYFRSNVEAMASYVPGEQPPQGTQVIKLNSNENPYPPSPEALAAIKDIDGECLRRYPEPFGEEFRKAVSQLLGVPCNWVIVGNGSDEILSIVIRACAEPTRKVVYPVPTYVLYRTLTEMQAADILEIPYREYNILPVADLIAAHGSVTFIASPNSPSGHVVPSDDLRKLASELSGVLVIDEAYVDFAEESALNLVQDHENVILIRTLSKGYSLAGLRLGFGVGNPQLLNGLFKVKDSYNVDAIACKVATAAITDQAYKNACVAKVKASRTRLAKDLKQLGFCVWDSQANFLLTQPPQGNAEYLYQQLREKKILIRYFKQPGLEDKLRITVGTDEQNQILLQALRDLLESRD | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39106
Sequence Length: 353
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
|
A6GY79 | MNNFNINNLVRENIKNMQAYASARDEFKDFTHNMVYLDANENPFSNGINRYPDPQQKKLKGFLAQQNKINENQMLLGNGSDEVLDLVFRAFCEPNVDNVITLPPTYGMYGVLANINAIENKEVLLSANFQPNINEILKNINENTKIIFLCSPNNPTGNSFDDQAVLTLLKNFNGLVVIDEAYIDFSKNGSWLHVISDYPNLLITQTLSKAYAMAGLRIGILYASAAIISILNKIKPPYNINNLSQESALKKLEQSTLNFHVKKIINERKKMVQSLISIPFIEKIYPSDANFILIKVEDANKRYNQLIEKGIVIRNRSNQPLCENCLRITIGTKEENEKLITVLKAL | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39232
Sequence Length: 346
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
|
Q2J8K9 | MIFKAAGSGAEDRPWRPWDADGLPLRDSLRGLSPYGAPQLDVPVRLNTNENPHPPSVGLVDAIGKAAALAATEANRYPDRDAEALRADLAYYLTPDAGFGVHTSQVWAANGSNEILQQLLQAFGGPGRVALGFEPSYSMHRLIALATATEWVAGQRAEDFTLSPAVVTDAIARHRPALVFLCSPNNPTGTALPPEVVAAACEAVEATGSGMVVVDEAYAEFRRAGVPSTLTLLPRHPRLVVTRTMSKAFALAGARVGYLAAHPAVVDSLYLVRLPYHLSSFTQAVARTALAHADELLGTVEAVKAQRDRIVRELPALGLRLAPSDANFVFFGRFADQRAVWQSLLDAGVLVRDVGLTGWLRVTAGLPNEVDAFLGALGRTLTGSVIGADGVISLATA | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 42037
Sequence Length: 397
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
|
B0TY45 | MQKIVQNQTTESLIRKDLQKFSAYSSARSLKVDGDIWLNANESPYNDEYLYNRYPEPQPRKLVEKLAKIYDVDASNILVTRGSDEGIDLLFRLYCEYQKDSAFAVEPTFGMYKIAAQLQGVDYKTLKLKEENNFEINITELLANIPDNCKLLFLCTPNNPTGKSIPLADIEQILSELAGNCVVVVDEAYIEFSNEKSVSSIINKYENLVVLRTLSKSFGMAGLRLGVVITNSDRIVWLRKILAPYPIPKTTESTILAMLDDENLANIASQIIEIKEQREHLYQALSQMKIVDKLWSSDANFILVRFRESIFNKLIDNKIVVRSMAHFFNDEKVLRISIGTVSENKRLIEVLQKLSSEYETK | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 41272
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
|
Q39YP6 | MIPLRQNIASMKGYIPGYQPPDIASWIKLNTNENPYPPSPEVVKAILEELGPDGAALRIYPSASSQKLREVAGELYGFDPSWIIMANGSDEVLNNLIRAFAAEGEEIGYVHPSYSYYGTLAEVQGARVRTFGLTGDFRIAGFPERYEGKVFFLTTPNAPLGPSFPLEYIDELARRCAGMLVLDETYAEFAESNALELVRRHENVVVTRTLSKSYSLAGMRIGLAIARPEVIAALDKIRDHYNLDRLAQAACVAALRDQAYLSECCRRIRETREWFTTELRSIGYDVIPSQGNYLFATPPDRDGKRVYDGLYARKVLVRHFSDPLLAHGMRISIGTREEMEQTLAALKEIG | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39135
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
|
Q7NL03 | MMQPYLRPDLDRLQAYHAPHFPEADKLDANELPHDLPEWLKNKLAFLLEQGVRTNRYPEGDPLALKAAIAEYCGVTSEMVCVGNGSDELIRSLITATCLGGRGTVASAEPTFSMYRILAETLAVPYIGVARTANYGVDADVLEAAVGANGVRVLFLANPNSPTGNLLSDEIIERLGSLPVLVVLDEAYYEFSRFSAVPLLWERPNLVILRTFSKAFRLANFRVGYALANPEIAAVLEKVRLPYNLPGLSQLAAFAALEHRDVLLAAIPEILAERRRIERFLADFEQLELFPSDANFLFVRPRIADPEAVRVALAGRGSLVRGAAGGLRVTVGTPEQNDRLIANVAALFTPEMR | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 38753
Sequence Length: 353
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
|
Q0BVW4 | MSNPRPNPGIEAIHPYIGGESKLPGVEQVIKLSSNEGAFGPPPAAQQAYLKAVSSLHRYPDGGSHALREAIGRYFGLDPARIVCGVGSDEMIAHLCMAYSNPDSELIMSVHGFSVYEMYGHYAGAKVVKVPEQALTTDVDALLDAITPRTKVVCIANPNNPTGTMLPTAEIARLRASLPSDVLLVLDAAYAEYVDDPDYDPGVKLVDAGDNTVMTRTFSKIFGLGGLRLGWAYAPPAIVDVLNRVRGPFTVNAAVQEAAIGALEEPGWVERSRAHNSAARAKLATALFDIGIPTLPSVTNFLLADFGSEARAGAADRWLRTRGLIVRRVASYGLPAYLRITIGTNEECDLVAEALRAFMAQAPADSDAAS | Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Mass (Da): 39403
Sequence Length: 370
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
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P38635 | MHSHHSHSGDYSAHGTDPLDSVVDQVVNLNFHTYCLTEHIPRIEAKFIYPEEQSLGKNPEEVITKLETSFKNFMSHAQEIKTRYADRPDVRTKFIIGMEIESCDMAHIEYAKRLMKENNDILKFCVGSVHHVNGIPIDFDQQQWYNSLHSFNDNLKHFLLSYFQSQYEMLINIKPLVVGHFDLYKLFLPNDMLVNQKSGNCNEETGVPVASLDVISEWPEIYDAVVRNLQFIDSYGGAIEINTSALRKRLEEPYPSKTLCNLVKKHCGSRFVLSDDAHGVAQVGVCYDKVKKYIVDVLQLEYICYLEESQSPENLLTVKRLPISQFVNDPFWANI | Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Mass (Da): 38582
Sequence Length: 335
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
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I3J7Q8 | MKIDTSLNMPQLPEALSQAGLQFSVATEEDFDEIMAMSQDIYGGLDYLPTRYTSWLQDTNRTVILARKHGKVIALESVCVIDDGETMLVEGLRVAPQERGKGVAGVLLRFCAELVKSRYPEVKVCRLTRDDQLGPKDFEKYRIITKQGILLMRFRAEDLKLHLSEFGLEGDNESTLSTFCSSPPPVRLDHTAIQQLYLNSDLLHGVLPNATIIQDWQPFKLLPSNMAILLKKEIDWMVDDMSNPTVASLCTFPFRVPIGDDWYYLNIDMFGKDLALARQQFLYHLQRHTATLKGHVMCQMFLDPPLWKAMAEFCHNTLSVELVKEYTEQCVVECDLI | Function: Enzyme responsible for the N-acetyl-histidine (NAH) synthesis, which is a major constituent of brain and lens of ectothermic vertebrates.
Catalytic Activity: acetyl-CoA + L-histidine = CoA + H(+) + N(alpha)-acetyl-L-histidine
Sequence Mass (Da): 38413
Sequence Length: 337
EC: 2.3.1.33
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Q0P4Y1 | MKIEAVPGAPQDGEFEFVLAAEKEFEEIISISHGIYGGLDYLPSRYHSWINEKDRMVVLAKKDGTVIGLLSVFVVDGGETALLEGLRVAPWERGRGVAGVLQRFCIKLVKHRYPSVKVMRLTRDDKLSAKELTKYRVIAKQGILLLSFNAPDLASRLSSIPLPPAASRPPPPIELTPEDVRDVFLERGGLLKDLLPNQTIIQDWQPFQALPGNQDLLRRKTLCWMVDDLIQPQVATLCTAPFPVPAGPLCFYLNIDVFGSELQSVQEQLLSHLHAHVPKLPADVRCQLFLPPNLWRPMADFCTLVLGLHLEKGYTEQYLLEADI | Function: Enzyme responsible for the N-acetyl-histidine (NAH) synthesis, which is a major constituent of brain and lens of ectothermic vertebrates.
Catalytic Activity: acetyl-CoA + L-histidine = CoA + H(+) + N(alpha)-acetyl-L-histidine
Sequence Mass (Da): 36276
Sequence Length: 324
EC: 2.3.1.33
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Q46125 | MKKFLTAFLVAFTGLFLVACQNTKTENNASNEANTTLTLKVGTAPNYKPFNFKQDSKLTGFDTDLIEEIAKKNGIEIVWVETNFDGLIPALKSGKIDMIASAMSATDERRQSVDFTKPYYMSKNLYLKLKNNDSLQTKNDLEGKKIGVQLGTLQENTAKAIKNAQVQSNKDLNIAVLALKNNKIDAIVADQDTAKGFLAENPELVSFYQETDGGEGFSFAFDKNKQKDIIEIFNKGIDEAKTDGFYDTLIKKYELE | Function: Involved in histidine transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 28531
Sequence Length: 256
Subcellular Location: Cell membrane
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Q06758 | MNMKKWIAAALACSALALSACGGQGKDAAAPAANPGKVYRVASNAEFAPFESLDSKGNVEGFDVDLMNAMAKAGNFKIEFKHQPWDSLFPALNNGDADIVMSGVTITDDRKQSMDFSDPYFEITQVVLVPKGKKVSSSDDLKKMNKVGVVTGHTGDFSVSKLLGNDNPKIARFENVPLIIKELENGGLDSVVSDSAVIANYVKNNPAKGMDFVTLPDFTTEHYGIAVRKGDEATVKMLNDALEKVRESGEYDKIYAKYFAKEGGQAAK | Function: Involved in histidine transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 28859
Sequence Length: 268
Subcellular Location: Cell membrane
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P0AEU5 | MIEILHEYWKPLLWTDGYRFTGVAITLWLLILSVVIGGVLALFLAIGRVSSNKYIQFPIWLFTYIFRGTPLYVQLLVFYSGMYTLEIVKGTEFLNAFFRSGLNCTVLALTLNTCAYTTEIFAGAIRSVPHGEIEAARAYGFSTFKMYRCIILPSALRIALPAYSNEVILMLHSTALAFTATVPDLLKIARDINAATYQPFTAFGIAAVLYLIISYVLISLFRRAEKRWLQHVKPSSTH | Function: Part of the histidine permease ABC transporter. Also part of a lysine/arginine/ornithine transporter. Probably responsible for the translocation of the substrate across the membrane. Required to relay the ATPase-inducing signal from the solute-binding protein to HisP (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26870
Sequence Length: 238
Subcellular Location: Cell inner membrane
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P56160 | MTPDLQLALELAEKAGKLTLDYFGRRSLQVFSKRDDTPVTEADRNAEELIRQGISAKFPDDGLFGEEFDEHPSGNGRRWIIDPIDGTRSFIHGVPLYGVMIALEVEGAMQLGVINFPALGELYQAERGSGAFMNGSPVQVSAIAENSASTVVFTEKEYLLDPPSNHPVDQLRIDAGLVRGWGDCYGHMLVASGRAEVAVDKIMSPWDCAAVIPIVEEAGGCCFDYRGRQSIIDGEGLVSANNAMGRNLIAAIGNGERDR | Function: Catalyzes the dephosphorylation of histidinol-phosphate to histidinol, the direct precursor of histidine.
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Mass (Da): 28059
Sequence Length: 259
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
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Q8NS80 | MSKYADDLALALELAELADSITLDRFEASDLEVSSKPDMTPVSDADLATEEALREKIATARPADSILGEEFGGDVEFSGRQWIIDPIDGTKNYVRGVPVWATLIALLDNGKPVAGVISAPALARRWWASEGAGAWRTFNGSSPRKLSVSQVSKLDDASLSFSSLSGWAERDLRDQFVSLTDTTWRLRGYGDFFSYCLVAEGAVDIAAEPEVSLWDLAPLSILVTEAGGKFTSLAGVDGPHGGDAVATNGILHDETLDRLK | Function: Catalyzes the dephosphorylation of histidinol-phosphate to histidinol, the direct precursor of histidine.
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Mass (Da): 27893
Sequence Length: 260
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
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P95189 | MSHDDLMLALALADRADELTRVRFGALDLRIDTKPDLTPVTDADRAVESDVRQTLGRDRPGDGVLGEEFGGSTTFTGRQWIVDPIDGTKNFVRGVPVWASLIALLEDGVPSVGVVSAPALQRRWWAARGRGAFASVDGARPHRLSVSSVAELHSASLSFSSLSGWARPGLRERFIGLTDTVWRVRAYGDFLSYCLVAEGAVDIAAEPQVSVWDLAALDIVVREAGGRLTSLDGVAGPHGGSAVATNGLLHDEVLTRLNAG | Function: Catalyzes the dephosphorylation of histidinol-phosphate to histidinol, the direct precursor of histidine.
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Mass (Da): 27693
Sequence Length: 260
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
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Q9K4B1 | MPDYLDDLRLAHVLADAADAATMDRFKALDLKVETKPDMTPVSEADKAAEELIRGHLSRARPRDSVHGEEFGVAGTGPRRWVIDPIDGTKNYVRGVPVWATLIALMEAKEGGYQPVVGLVSAPALGRRWWAVEDHGAFTGRSLTSAHRLHVSQVSTLSDASFAYSSLSGWEEQGRLDGFLDLTREVWRTRAYGDFWPYMMVAEGSVDLCAEPELSLWDMAANAIIVTEAGGTFTGLDGRPGPHSGNAAASNGRLHDELLGYLNQRY | Function: Catalyzes the dephosphorylation of histidinol-phosphate to histidinol, the direct precursor of histidine.
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Mass (Da): 29084
Sequence Length: 266
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
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P73058 | MTRILKLSHLTPQQLNQLKRRSEQNIDQALAIAKEVIEQVKMEGDAGVLHYSRQFDFAGATAENLRVSEAEFAEAEKLVDPELRRAVEHAFRNIEKVHAGQMPPPMHLAEIEPGVFAGEKITPLPTVGLYVPRGKGAFPSMMLMLAVPARVAGVKKIVVCTPPDKEGKVEPVSLVTARMAGVDEVYKLGGVQALAAIAYGTKTVSKVDKLIGPCSIYGAAAKRLLSGIVDVGLPAGPSESIVLADETTDPKLAALDLLIEAEHGSDSAALLVTHSASLAEKALGYLGEYLEKLPPWRKKFCEDGLGSYGGILLTDSLQASLDFINDYAPEHLQVLTADPLKLVGKIDNAGEILLGNYTPSSAATYAIGVNAVLPTGGFARSYSAVSVFDFLKRSTLAYLTEEGFAGVKETVTTLADYEDFPAHALAIRERENLL | 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): 46534
Sequence Length: 434
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
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Q5JFR5 | MKGLEEYVREILEDIRRRGLEALREYSERFDNYSGPFRVSEGEFEEAEELVPEEDKRVIEETMERLWEYHARQFRDVELYIKRGSLYGLIYRPIGRIGIYVPGGKPLPSTLMMVGIPARIAGVREIAVTTPPKDGKVNPYVLYVAKLLGIEEVYKLGGVGAIAAMAYGVGMRRVDKIFGPGNRFVNEAKRQVFGIVGIDSLAGPSEIAVIADESADKDYVLADLLSQLEHGKDSKAWLLTTSRELADYCSREGIEVLLCRNLEECAEKANEIAPEHLEIITENPEELVDLIENAGAIYLGPYTPVPAADYFLGVNHVLPTGGAARFSGVLTVMDFMKPITLARVSREEFLAYRRLGMRLAEIEGMEAHRRSLEVRR | 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): 42216
Sequence Length: 376
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
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Q9X0D1 | MILMNNPGDKEVLRLLKQRMESVSQVEETVKEIIRRVKEEGDRALEEFLKRFEKHPVGIENLRVTEKEISEAQVEEEFVETIKIVIEDLKEFHRRQEERSFFFTTKGGSFLGEMVVPLESVGIYVPGGKVPYFSTLLMCAVPAIVAGVERIAVTTPPNENGGISPYILKTCEILGLKEIYRMGGAHAVAALTYGTETVKPVDKIVGPGGVFVTLAKKHVYGDVGIDSIAGPSEIAIVTDGSADLDLIAADFLSQAEHDENAMSVVITTSKEVFEKLPQVIERHLEALPEERRKTARISTENFGTIILTDSLKRAFEISNLIAPEHLEVLVENPFEPLGHIKNAGSVFLGKYTCESVGDYGAGPNHVLPTFRSARFSSGLRVSDFTKKIFITHLSEEDFRRKSELYSKMARWEGFEAHARAIDVRREKL | 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): 47749
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
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Q8P9P2 | MNTLDWTQLTADARTQALTRPVQTVATQTREAVATLIADVRARGDVALREITARFDGVTLESFAVSDAEFAAADAAIAPELRQAMQDAVARIDTFHRAGMSEGYAVETAPGVVCEKIVRPIGRVGLYVPAGSAPLPSTALMLGVPARLAGCREVVLCTPPRKDGSVDPAVLVAAQLTGVRRVFKLGGAQAIAAMAYGTDSIPSCDKLFGPGNSFVTEAKQQVAQSGAAAIDMPAGPSEVLVIADAGAQPAFVAADLLSQAEHGPDSQVLLLSDSDALITAVQEQLDLQLAQLSRADIARQALAQSRLIKVATLQDAFEISNRYAPEHLILALREPRAWLAQVEAAGSVFLGDYTPEALGDYCSGTNHVLPTSGAARAYSGVSVASFQNMVSVQAASKAGIDGIGACAVILARAEGLDAHANAVALRMGVAA | 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): 44665
Sequence Length: 431
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
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Q4FTX3 | MLPDGVADVLFEDAHKQEVLRHQLTQQLITHGYQLVSPPMIEFTESLLSGASEDLKRQTFKIIDQLTGRLMGIRADITPQILRIDAHHGGDGIARYCYAGDVIHTLPSGLFGSRTPLQLGAEIFGCESIAADIELIDVLFSMINSLDMSAVLHVDLGHVTIFKRLAELAALSASDTEQLMQLYANKNLPELKQVCQVLPMGSDFYTLARFGHDIANLLGRLSENAQQDTKIVTAIDELQRLKAHLQVQWQCAVSIDVTELSGYHYHTGIVFNGYINSETQPLVRGGRFDGMKSNQLATNQPRQATGFSMDVSRLLAHTQLDAPFIVLIDYDAFNNLDSAQRQLLLQQVASLRQQGYRVTMPLTAEDMPVGLTHRLSLADNQWRLHAV | Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Sequence Mass (Da): 43028
Sequence Length: 387
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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Q7VZF5 | MIVVTGAAGFIGSNLVRGLNRRGIQDIIAVDDLTDGDKFRNLVDCSIADYLDKDEFRERVRGGNLPALRAVLHQGACSDTTERNGRYMLDNNYRVTLELFEYCQAERVPFLYASSAAVYGGSSVYVEDPANEHPLNVYGYSKLLFDQVLRTRMDSLTAQVVGLRYFNVYGPHEQHKGRMASVAFHNMNQFLAEGHVRLFAGWDGYEDGGQSRDFISVEDVVAVNLHFLDNPDQSGVFNCGTGRAQPFNDVAAAVVNTLRAERGEAALPLAELVKKGLLRYIPFPDDLKGRYQSYTQADVSRLRATGFSAPMRDVQTGVSEYVRYWRALK | Cofactor: Binds 1 NADP(+) per subunit.
Function: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
Catalytic Activity: ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose
Sequence Mass (Da): 36760
Sequence Length: 329
Domain: Contains a large N-terminal NADP-binding domain, and a smaller C-terminal substrate-binding domain.
Pathway: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4.
EC: 5.1.3.20
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C0QZ84 | MIIVTGGAGFIGSNIVKGLNNLGIDDILVVDNLKNASKHKNLNRIKFRDYIDKEDFNLDYLTSFVNNNKVEAIFHQGACSDTMETDGKYMMKNNYEYTKNILHICLDKKIRLFYASSASVYGNGENGFEEDEKNEYPLNVYAFSKYHFDRYLNKLFKENKVNSQVVGLRYFNVYGPQENHKGRMASVAFHLFNQIKAGERMKIFEGSENFLRDFIHIDDVVSVNNFFFENPNKSGIFNCGTGNAESFVEIAKALKEVYKSASIEYIAFPDALRGKYQKYTQADLKKLRAAGYDKPFMNVNTGVKKYAEVLEKSGGYLM | Cofactor: Binds 1 NADP(+) per subunit.
Function: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
Catalytic Activity: ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose
Sequence Mass (Da): 36366
Sequence Length: 318
Domain: Contains a large N-terminal NADP-binding domain, and a smaller C-terminal substrate-binding domain.
Pathway: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 4/4.
EC: 5.1.3.20
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A8I5B0 | MLAETQLAPIAVIGDVMVDRYITGSVSRISPEAPVPVLVHGAERIVPGGAANVAANAAALGAPVLLVGLVGEDEAASQLADALATYPGISLAHMVVDAKRPTITKTRVMSGRQQIVRIDAEVTRACDAAEEAALIGAAEAAIAKAGVVVLSDYAKGVLSDAVIAAAMAAAKARNVPVIVDPKRRTFEAYRGATLVTPNRRELAEATGLPDETDADAARAAEAAGRQFGGDVLVTRAEKGMTLWRQDGRVLHVPAEAREVFDVSGAGDTALAALAVSLAGGQSLEASVGIANAAAALAVAKLGTAVVTRAELRAALERTAAQIAPPGALVSREDACAVVAAWKAQGLRVVFTNGCFDLVHPGHVSLLEQSAAQGDRLVVALNTDASVRRLKGPSRPLQDEQARARVMGAMRCVDLVVLFDEETPLETIKALLPDVLVKGADYAPHEVVGADVVTANGGELVLVDLVAGKSTSSLVAKART | Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+)
Sequence Mass (Da): 49173
Sequence Length: 479
Pathway: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4.
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Q89HR3 | MPTPILDFDALAQTISGRTVLCIGDIMLDEFVYGEVSRISPEAPTPVIVAQRSEIHIGGAGNVARNVASLGARCIFVGLVGEDDAGKRLAAALADQAAIESVLVCDPSRPTTRKVRFVSEHFSTHMLRADWEQAQPASDEVEAKLIEAILPQIARADIVLLSDYAKGVLTARVIRHTIDAARKLGKPVIVDPKSLNWAIYRGATLLTPNRKEFAEATRSRADTPQSIVDASEDVMRLADCEAILVTQGEHGMTLVPRNGAAVHVPAVPVKVRDVSGAGDTVAAALAVSLAAGADWDTALRVANAAASVAVSKLGTAIVSTAELRRKILPHAYLAAEEKIVLEPAALDAQLAEWRTQGLRVGFTNGCFDILHPGHVKVLTAARGACDRLVVGLNSDASVRRLKGADRPVQDERARAEVLAALEAVDLVVIFEEDTPIDLITRIKPAALVKGGDYTREQVVGHEVVEAAGGVVVLVDILQGFSTTALVHRARGGAK | Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+)
Sequence Mass (Da): 52389
Sequence Length: 494
Pathway: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4.
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Q6TG09 | MLEFLSQQKPKILIIGDFMVDNYTWCDCSRISPEAPVLIAKTLKEDKRLGGAANVYANLKSLGADVFALGVVGDDESGKFLQENLKGEFLIQKGRKTPFKNRIMAHNQQVLRLDEEDISEILLENELIALFDEKIKDFKAVVLSDYAKGVLTPKVCKAVIEKAKVLNIPVLVDPKGSDFNKYSGATLLTPNKKEALEALKFENLEGENLEKGIKKLKEDFSLRYSIITLSEAGIALFDEGLKIAPAKALEVYDVTGAGDSVIAVLAFCLANEIEIFKACELANEAAAVVVSKIGSVSVSFDEIKSFKRVDFEKKIKSKEELLVLLKQNNKKIVFTNGCFDIVHFGHIKYLDKAKRLGDVLIVGLNSDASVKRLKGESRPVNSEFQRACMLAAFYFVDFVVIFDEDTPLELISFLKPDILVKGADYKDKLVVGADIVSRVELIDFEEGFSTSKIIEKIKDKK | Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+)
Sequence Mass (Da): 51238
Sequence Length: 461
Pathway: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4.
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Q9A2C5 | MDDALAHLPRAFAGKTVLVLGDVMLDRFIYGAVDRISPEAPVPVIAVEKETAMLGGAGNVARNVAALGAKAVLIGLVGRDDAGAALRGMIDAEAGLEAELVVDPARRTTEKVRYISGSHQMLRVDREDRSPGDGAALLAAFETRLASADVVVLSDYAKGVLTPAVVRGAIDAAKAAGKPVIVDPKSRDFARYDGATLIKPNRKEAAEATGIVETSDAASEDAGAAILAMAPGLQAALITRGGAGMTLAVRNQPPIHLPATAIEVFDVSGAGDTVAATLALAVAAGASLAQAAQLANLAGGLVVAKLGTDVVTAAELTACASSAQGEPGEIKIADREQAQRIVEGWRARGLKVGFTNGCFDLLHPGHVSLLSQAKAACDRLIVGLNTDASVSKLKGPTRPVQKEQGRATVLASLSSVDLVVLFDEDTPLELIKAFRPDVLVKGADYTVETVVGSDVVLGYGGKVVLAELKQGQSTTNLIARMNS | Function: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 7-phosphate = ADP + D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H(+)
Sequence Mass (Da): 49622
Sequence Length: 483
Pathway: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4.
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Q6H7M3 | MEQNGENHLKDPLLQADGGGSGASPAGASPRKERKTRKVMFNVRGISCASCAVSIETVVAGLKGVESVSVSPLQGQAVVQYRPEEADARTIKEAIEGLNFEVDELQEQEIAVCRLQIKGMACTSCSESVERALQMVPGVKKAAVGLALEEAKVHFDPNITSRDLIIEAIEDAGFGADLISSGDDVNKVHLKLEGVSSPEDIKLIQSRLESVEGVNNVECDTAGQTIIVAYDPDVTGPRLLIQCIQDAAQPPKYFNASLYSPPKQREAERHHEIRNYRNQFLWSCLFSVPVFMFSMVLPMISPFGDWLFYKVCNNMTIGMLLRWLLCSPVQFIIGWRFYVGAYHALKRGYSNMDVLVALGTNAAYFYSVYIVLKALTSESFEGQDFFETSAMLISFILLGKYLEVVAKGKTSDALSKLTELAPETACLLTLDKDGNAISETEISTQLLQRNDVIKIVPGEKVPVDGVVIKGQSHVNESMITGEARPIAKKPGDKVIGGTVNDNGCIIVKVTHVGSETALSQIVQLVEAAQLARAPVQKLADRISRFFVPTVVVAAFLTWLGWFVAGQFDIYPREWIPKAMDSFELALQFGISVLVVACPCALGLATPTAVMVATGKGASQGVLIKGGNALEKAHKVKAIIFDKTGTLTVGKPSVVQTKVFSKIPLLELCDLAAGAEANSEHPLSKAIVEYTKKLREQYGSHSDHIMESKDFEVHPGAGVSANVEGKLVLVGNKRLMQEFEVPISSEVEGHMSETEELARTCVLVAIDRTICGALSVSDPLKPEAGRAISYLSSMGISSIMVTGDNWATAKSIAKEVGIGTVFAEIDPVGKAEKIKDLQMKGLTVAMVGDGINDSPALAAADVGLAIGAGTDVAIEAADIVLMRSSLEDVITAIDLSRKTLSRIRLNYVWALGYNVLGMPVAAGVLFPFTGIRLPPWLAGACMAASSVSVVCSSLLLQLYKKPLHVEEVAAGPKNDPDLV | Function: Copper (Cu) transporter that mediates Cu transport in root vacuoles. Involved in Cu detoxification by sequestrating Cu into root vacuoles and limiting translocation of Cu from the roots to the shoots, and accumulation in grains.
Catalytic Activity: ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 105130
Sequence Length: 978
Subcellular Location: Vacuole membrane
EC: 7.2.2.8
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Q9SH30 | MATKLLSLTCIRKERFSERYPLVRKHLTRSRDGGGGSSSETAAFEIDDPISRAVFQVLGMTCSACAGSVEKAIKRLPGIHDAVIDALNNRAQILFYPNSVDVETIRETIEDAGFEASLIENEANERSRQVCRIRINGMTCTSCSSTIERVLQSVNGVQRAHVALAIEEAEIHYDPRLSSYDRLLEEIENAGFEAVLISTGEDVSKIDLKIDGELTDESMKVIERSLEALPGVQSVEISHGTDKISVLYKPDVTGPRNFIQVIESTVFGHSGHIKATIFSEGGVGRESQKQGEIKQYYKSFLWSLVFTVPVFLTAMVFMYIPGIKDLLMFKVINMLTVGEIIRCVLATPVQFVIGWRFYTGSYKALRRGSANMDVLIALGTNAAYFYSLYTVLRAATSPDFKGVDFFETSAMLISFIILGKYLEVMAKGKTSQAIAKLMNLAPDTAILLSLDKEGNVTGEEEIDGRLIQKNDVIKIVPGAKVASDGYVIWGQSHVNESMITGEARPVAKRKGDTVIGGTLNENGVLHVKVTRVGSESALAQIVRLVESAQLAKAPVQKLADRISKFFVPLVIFLSFSTWLAWFLAGKLHWYPESWIPSSMDSFELALQFGISVMVIACPCALGLATPTAVMVGTGVGASQGVLIKGGQALERAHKVNCIVFDKTGTLTMGKPVVVKTKLLKNMVLREFYELVAATEVNSEHPLAKAIVEYAKKFRDDEENPAWPEACDFVSITGKGVKATVKGREIMVGNKNLMNDHKVIIPDDAEELLADSEDMAQTGILVSINSELIGVLSVSDPLKPSAREAISILKSMNIKSIMVTGDNWGTANSIAREVGIDSVIAEAKPEQKAEKVKELQAAGHVVAMVGDGINDSPALVAADVGMAIGAGTDIAIEAADIVLMKSNLEDVITAIDLSRKTFSRIRLNYVWALGYNLMGIPIAAGVLFPGTRFRLPPWIAGAAMAASSVSVVCCSLLLKNYKRPKKLDHLEIREIQVERV | Function: Involved in copper import into the cell. May play a role in copper detoxification in roots.
Catalytic Activity: ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 108336
Sequence Length: 995
Subcellular Location: Membrane
EC: 7.2.2.8
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A3AWA4 | MAASTRALFLSCFHGSGGGGGTSEVSRRLVLRPRYPSMPRRPRSAAVAGEGGEGGGGGGDGDLEAAAVGAEEEEKVAVFEVSGMTCAACAGSVEKAVKRLQGIHDAAVDVLGGRAQVVFYPAFVSEEKIRETIQDVGFEAKLIDEEVKEKNILVCRLHIKGMTCTSCASTVESILQVVPGVQRASVALATEEAEIRYDRRIVTASQLTHAVEETGFEAILITTGDDQSRIDLKVDGTLNERSIMIVKSSVQALPGVEDIKVDPELHKITISYKPDQTGPRDLIEVIESAASGDLTVSIYPEADGRQQHRHGEIKRYRQSFLWSLVFTIPVFLTSMVFMYIPGLKDGLEKKVINMMSIGELLRWILSTPVQFVIGRRFYTGAYKALSHGSSNMDVLIALGTNTAYFYSVYSILRAASSHNYMATDFFETSSMLISFILLGKYLEILAKGKTSEAIAKLMDLAPETATMLIYDHEGNVVGEKEIDSRLIQKNDVIKVVPGGKVASDGFVIWGQSHVNESMITGESRPVAKRKGDTVIGGTVNENGVLHVRATFVGSESALAQIVRLVESAQMAKAPVQKFADQISRVFVPLVIILSLLTWLAWFLAGRLHGYPNSWIPSSMDSFQLALQFGISVMVIACPCALGLATPTAVMVATGVGASQGVLIKGGQALESAQKVDCIVFDKTGTLTIGKPVVVNTRLLKNMVLREFYAYVAAAEVNSEHPLGKAVVEHAKKFHSEESHVWTEARDFISVTGHGVKAKISGRAVMVGNKSFMLTSGIDIPVEALEILTEEEEKAQTAIIVAMDQEVVGIISVSDPIKPNAREVISYLKSMKVESIMVTGDNWGTANAISKEVGIENTVAEAKPEQKAEKVKELQSAGRTVAMVGDGINDSPALVSADVGLAIGAGTDVAIEAADIVLMKSNLEDVITAIDLSRKTFFRIRMNYVWALGYNIIGIPIAAGVLFPSTRFRLPPWVAGAAMAASSVSVVCWSLLLRYYKSPKLGR | Function: Copper (Cu) transporter that plays an essential role in promoting translocation of Cu from roots to shoots. Involved in loading Cu to the xylem of the roots and other organs, including panicles.
Catalytic Activity: ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 107987
Sequence Length: 1002
Subcellular Location: Cell membrane
EC: 7.2.2.8
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Q9SZC9 | MESTLSAFSTVKATAMARSSGGPSLPLLTISKALNRHFTGARHLHPLLLARCSPSVRRLGGFHGSRFTSSNSALRSLGAAVLPVIRHRLECLSSSSPSFRSISSGGGSGFGGYNGGSGGGGGGGSESGDSKSKLGANASDGVSVPSSDIIILDVGGMTCGGCSASVKKILESQPQVASASVNLTTETAIVWPVPEAKSVPDWQKSLGETLANHLTNCGFQSTPRDLVTENFFKVFETKTKDKQARLKESGRELAVSWALCAVCLVGHLTHFLGVNAPWIHAIHSTGFHVSLCLITLLGPGRKLVLDGIKSLLKGSPNMNTLVGLGALSSFSVSSLAAMIPKLGWKTFFEEPVMLIAFVLLGRNLEQRAKIKATSDMTGLLSVLPSKARLLLDGDLQNSTVEVPCNSLSVGDLVVILPGDRVPADGVVKSGRSTIDESSFTGEPLPVTKESGSQVAAGSINLNGTLTVEVHRSGGETAVGDIIRLVEEAQSREAPVQQLVDKVAGRFTYGVMALSAATFTFWNLFGAHVLPSALHNGSPMSLALQLSCSVLVVACPCALGLATPTAMLVGTSLGARRGLLLRGGDILEKFSLVDTVVFDKTGTLTKGHPVVTEVIIPENPRHNLNDTWSEVEVLMLAAAVESNTTHPVGKAIVKAARARNCQTMKAEDGTFTEEPGSGAVAIVNNKRVTVGTLEWVKRHGATGNSLLALEEHEINNQSVVYIGVDNTLAAVIRFEDKVREDAAQVVENLTRQGIDVYMLSGDKRNAANYVASVVGINHERVIAGVKPAEKKNFINELQKNKKIVAMVGDGINDAAALASSNVGVAMGGGAGAASEVSPVVLMGNRLTQLLDAMELSRQTMKTVKQNLWWAFGYNIVGIPIAAGVLLPLTGTMLTPSMAGALMGVSSLGVMTNSLLLRYRFFSNRNDKNVKPEPKEGTKQPHENTRWKQSS | Function: Mediates copper transfer across the plastid envelope. Required for the delivery of copper into the plastid stroma, which is essential for the function of copper proteins. Seems to be selective for monovalent copper Cu(+) transport. Also plays a role in glucose signaling-mediated cell proliferation of root meristem in non-green tissues.
Catalytic Activity: ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 99997
Sequence Length: 949
Subcellular Location: Plastid
EC: 7.2.2.8
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Q9S7J8 | MAPSRRDLQLTPVTGGSSSQISDMEEVGLLDSYHNEANADDILTKIEEGRDVSGLRKIQVGVTGMTCAACSNSVEAALMNVNGVFKASVALLQNRADVVFDPNLVKEEDIKEAIEDAGFEAEILAEEQTQATLVGQFTIGGMTCAACVNSVEGILRDLPGVKRAVVALSTSLGEVEYDPNVINKDDIVNAIEDAGFEGSLVQSNQQDKLVLRVDGILNELDAQVLEGILTRLNGVRQFRLDRISGELEVVFDPEVVSSRSLVDGIEEDGFGKFKLRVMSPYERLSSKDTGEASNMFRRFISSLVLSIPLFFIQVICPHIALFDALLVWRCGPFMMGDWLKWALVSVIQFVIGKRFYVAAWRALRNGSTNMDVLVALGTSASYFYSVGALLYGAVTGFWSPTYFDASAMLITFVLLGKYLESLAKGKTSDAMKKLVQLTPATAILLTEGKGGKLVGEREIDALLIQPGDTLKVHPGAKIPADGVVVWGSSYVNESMVTGESVPVSKEVDSPVIGGTINMHGALHMKATKVGSDAVLSQIISLVETAQMSKAPIQKFADYVASIFVPVVITLALFTLVGWSIGGAVGAYPDEWLPENGTHFVFSLMFSISVVVIACPCALGLATPTAVMVATGVGATNGVLIKGGDALEKAHKVKYVIFDKTGTLTQGKATVTTTKVFSEMDRGEFLTLVASAEASSEHPLAKAIVAYARHFHFFDESTEDGETNNKDLQNSGWLLDTSDFSALPGKGIQCLVNEKMILVGNRKLMSENAINIPDHVEKFVEDLEESGKTGVIVAYNGKLVGVMGIADPLKREAALVVEGLLRMGVRPIMVTGDNWRTARAVAKEVGIEDVRAEVMPAGKADVIRSLQKDGSTVAMVGDGINDSPALAAADVGMAIGAGTDVAIEAADYVLMRNNLEDVITAIDLSRKTLTRIRLNYVFAMAYNVVSIPIAAGVFFPVLRVQLPPWAAGACMALSSVSVVCSSLLLRRYKKPRLTTVLKITTE | Function: Involved in copper import into the cell. Essential for ethylene signaling, which requires copper. Acts by delivering copper to create functional hormone receptors.
Catalytic Activity: ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 107395
Sequence Length: 1001
Subcellular Location: Membrane
EC: 7.2.2.8
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B9DFX7 | MASNLLRFPLPPPSSLHIRPSKFLVNRCFPRLRRSRIRRHCSRPFFLVSNSVEISTQSFESTESSIESVKSITSDTPILLDVSGMMCGGCVARVKSVLMSDDRVASAVVNMLTETAAVKFKPEVEVTADTAESLAKRLTESGFEAKRRVSGMGVAENVKKWKEMVSKKEDLLVKSRNRVAFAWTLVALCCGSHTSHILHSLGIHIAHGGIWDLLHNSYVKGGLAVGALLGPGRELLFDGIKAFGKRSPNMNSLVGLGSMAAFSISLISLVNPELEWDASFFDEPVMLLGFVLLGRSLEERAKLQASTDMNELLSLISTQSRLVITSSDNNTPVDSVLSSDSICINVSVDDIRVGDSLLVLPGETFPVDGSVLAGRSVVDESMLTGESLPVFKEEGCSVSAGTINWDGPLRIKASSTGSNSTISKIVRMVEDAQGNAAPVQRLADAIAGPFVYTIMSLSAMTFAFWYYVGSHIFPDVLLNDIAGPDGDALALSLKLAVDVLVVSCPCALGLATPTAILIGTSLGAKRGYLIRGGDVLERLASIDCVALDKTGTLTEGRPVVSGVASLGYEEQEVLKMAAAVEKTATHPIAKAIVNEAESLNLKTPETRGQLTEPGFGTLAEIDGRFVAVGSLEWVSDRFLKKNDSSDMVKLESLLDHKLSNTSSTSRYSKTVVYVGREGEGIIGAIAISDCLRQDAEFTVARLQEKGIKTVLLSGDREGAVATVAKNVGIKSESTNYSLSPEKKFEFISNLQSSGHRVAMVGDGINDAPSLAQADVGIALKIEAQENAASNAASVILVRNKLSHVVDALSLAQATMSKVYQNLAWAIAYNVISIPIAAGVLLPQYDFAMTPSLSGGLMALSSIFVVSNSLLLQLHKSETSKNSL | Function: Mediates copper transfer across the chloroplast thylakoid membrane. Required for copper delivery into the thylakoids lumen, which is essential for the function of copper proteins.
Catalytic Activity: ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 94260
Sequence Length: 883
Subcellular Location: Plastid
EC: 7.2.2.9
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O52791 | MQNFEIDYVEMYVENLEVAAFSWVDKYAFAVAGTSRSADHRSIALRQGQVTLVLTEPTSDRHPAAAYLQTHGDGVADIAMATSDVAAAYEAAVRAGAEAVRAPGQHSEAAVTTATIGGFGDVVHTLIQRDGTSAELPPGFTGSMDVTNHGKGDVDLLGIDHFAICLNAGDLGPTVEYYERALGFRQIFDEHIVVGAQAMNSTVVQSASGAVTLTLIEPDRNADPGQIDEFLKDHQGAGVQHIAFNSNDAVRAVKALSERGVEFLKTPGAYYDLLGERITLQTHSLDDLRATNVLADEDHGGQLFQIFTASTHPRHTIFFEVIERQGAGTFGSSNIKALYEAVELERTGQSEFGAARR | Cofactor: Binds 1 Fe cation per subunit.
Function: Required to synthesize hydroxyphenylglycine, a recurring skeletal component of nonproteinogenic macrocyclic peptide antibiotics such as vancomycin. Catalyzes the conversion of p-hydroxyphenylpyruvate to p-hydroxymandelate. The decarboxylation and hydroxylation activities of HmaS show novel and distinct regioselectivity, compared to all other known p-hydroxyphenylpyruvate dioxygenases, by hydroxylating the benzylic position of the substrate instead of the phenyl ring.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruvate + O2 = (S)-4-hydroxymandelate + CO2
Sequence Mass (Da): 38339
Sequence Length: 357
Pathway: Antibiotic biosynthesis; vancomycin biosynthesis.
EC: 1.13.11.46
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Q6NT76 | MLSSFPVVLLETMSHYTDEPRFTIEQIDLLQRLRRTGMTKHEILHALETLDRLDQEHSDKFGRRSSYGGSSYGNSTNNVPASSSTATASTQTQHSGMSPSPSNSYDTSPQPCTTNQNGRENNERLSTSNGKMSPTRYHANSMGQRSYSFEASEEDLDVDDKVEELMRRDSSVIKEEIKAFLANRRISQAVVAQVTGISQSRISHWLLQQGSDLSEQKKRAFYRWYQLEKTNPGATLSMRPAPIPIEDPEWRQTPPPVSATSGTFRLRRGSRFTWRKECLAVMESYFNENQYPDEAKREEIANACNAVIQKPGKKLSDLERVTSLKVYNWFANRRKEIKRRANIEAAILESHGIDVQSPGGHSNSDDVDGNDYSEQDDSTSHSDHQDPISLAVEMAAVNHTILALARQGANEIKTEALDDD | Function: Binds directly to 5'-TTAGGG-3' repeats in telomeric DNA . Associates with the telomerase complex at sites of active telomere processing and positively regulates telomere elongation . Important for TERT binding to chromatin, indicating a role in recruitment of the telomerase complex to telomeres (By similarity). Also plays a role in the alternative lengthening of telomeres (ALT) pathway in telomerase-negative cells where it promotes formation and/or maintenance of ALT-associated promyelocytic leukemia bodies (APBs) . Enhances formation of telomere C-circles in ALT cells, suggesting a possible role in telomere recombination . Might also be involved in the DNA damage response at telomeres .
Sequence Mass (Da): 47278
Sequence Length: 420
Domain: The homeobox domain is required for binding to 5'-TTAGGG-3' repeats in telomeres, and for telomere localization.
Subcellular Location: Nucleus
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Q12039 | MDKLTPSQWKVINKSYEPASTIKVIAGPGSGKTLTLLYKVLHLITVENIKPEEILIFSLTNKAVDSIIENLLSIFENSHTNKEIVHQIGCYTVHGLANRIVVENEGMINIIEEIGWRGLMKLLPPSKRTPHHFRSYKELEKVVKDYKLNNAKNNNPVIEKLVELMDNCKVMTNDDLIIRAKKYLELDSSDSDASSFTQDLRNKYKVVLIDEFQDLYPSLAPLITMICKGKQLIMFGDTNQSIYGFLGSNNEIMSQLDNLHPKNSTTVLKLFDNFRSTPEIISLASKIINRPLAEKQIIDDTDETPSELVRKLPSGVSPQIMTFDDLAAESEFIIDKITQLICSSAKFSDIAILSRTNSHLTAIASILKKYGIPYQKLKSQPDWMDDLRIQFLLDILKVCSLASDEKHNREFNTGDKWQSNFSILVTMSALKGIGDASIQALYKACSLKNLSIWKYLTMVPNFEWPLGLSIKKKMENYTSNLYEMIENDQVHQLDDPMELLEKVASITNNLNLNPTYFQSLSDAQSSLEFKTHLQEMAQVMKVSKSNKPPGISFVKWFLETYFDQTMVFHQSQQALQTTGPGTVKLSTIHSAKGLEFPIVFLTNGSMSNFPMDTNALYVGITRARNLLYMCNMKHERLVSKSSPYSRNIMSNNLFWTYYNKDLKRSVCDVKVTHGYNVQRYNQLRKNFGFYRAYSSLRGCKSVFRRI | Function: Required for mitochondrial genome maintenance and mitochondrial DNA inheritance.
Catalytic Activity: Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 80576
Sequence Length: 706
Subcellular Location: Mitochondrion inner membrane
EC: 5.6.2.4
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Q9V3U0 | MNDLKPATSYRSTSLHDAVKLRLDEPSSFSQTVPPQTIPEFFKESCEKYSDLPALVWETPGSGNDGWTTLTFGEYQERVEQAALMLLSVGVEERSSVGILAFNCPEWFFAEFGALRAGAVVAGVYPSNSAEAVHHVLATGESSVCVVDDAQQMAKLRAIKERLPRLKAVIQLHGPFEAFVDHEPGYFSWQKLQEQTFSSELKEELLARESRIRANECAMLIFTSGTVGMPKAVMLSHDNLVFDTKSAAAHMQDIQVGKESFVSYLPLSHVAAQIFDVFLGLSHAGCVTFADKDALKGTLIKTFRKARPTKMFGVPRVFEKLQERLVAAEAKARPYSRLLLARARAAVAEHQTTLMAGKSPSIYGNAKYWLACRVVKPIREMIGVDNCRVFFTGGAPTSEELKQFFLGLDIALGECYGMSETSGAITLNVDISNLYSAGQACEGVTLKIHEPDCNGQGEILMRGRLVFMGYLGLPDKTEETVKEDGWLHSGDLGYIDPKGNLIISGRLKELIITAGGENIPPVHIEELIKKELPCVSNVLLIGDHRKYLTVLLSLKTKCDAKTGIPLDALREETIEWLRDLDIHETRLSELLNIPADLQLPNDTAALAATLEITAKPKLLEAIEEGIKRANKYAISNAQKVQKFALIAHEFSVATGELGPTLKIRRNIVHAKYAKVIERLYK | Function: Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation . Probably by regulating lipid storage and catabolism, plays a role in neuronal function .
Catalytic Activity: a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate
Sequence Mass (Da): 75152
Sequence Length: 681
EC: 6.2.1.3
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Q7W025 | MTLQARNLTLARGGAPILTDVSLTLAPGALVGLLGANGAGKSTLLAALAGELAPRSGQVFLGDADLATLSARQLARRRAVLPQKPSLSFDLGVSDVVGMGAYPFPELDPAAVRQLVRDALEQAGVTHLAQRRYPQLSGGEQQRVQFARVLAQCHAMHAPGQTRYLMLDEPISNLDPRHQMELLATARALAHEAGMGVLVIVHDINQAARWCDTLALLADGRLAALGPPADVLTPDHMRRVYGIEADVLAHPTLPGRLLVLAR | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27800
Sequence Length: 262
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q93SH7 | MSAVIEARHLSKRAGRAKLLDGVGLTVAAGEMVAIIGPNGAGKSTLLRLLSGDLRPSQGEVWLKQRDIGSYTPRELAARRAMLSQHINVTFPFTVEEIVLMGAGDRSAREAGRLVDAALDEVGLAHFRERQLPTLSGGEQQRAHFARVLVQLACGEAEHGPGLLLLDEPTSSLDLRHQIDLVEAARRRAGTGTAVIAILHDLNLAIRFADRLVVLSGGKLAADGPRTEVVTRETIRDIFEIDAVVHQADGVPYVLPQSMRAAASAARI | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28745
Sequence Length: 268
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q62A98 | MLNADHLHVARDGRAILNDLSIRIAPGCVTALLGRNGAGKSTLLGVLAGDLPAGGLARGATVRGGVALNGEPLHAIDAPRLARLRAVLPQASRPAFAFSAREIVLLGRYPHARRAGALTHADGEIASQALALAGATALDARDVTTLSGGELARVQFARVLAQLWPPPGAAQPPRYLLLDEPTAALDLAHQHQLLDTVRRLSRDWNLGVLTIVHDPNLAARHADRIAMLADGAIVAQGAPADVLRPEPIARCYGFRVRLVDAGDGVAPVIVPA | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28401
Sequence Length: 272
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q9RZU5 | MTASSPSIRVTDLSYSVAGRELLSKLKFHLQSGEMLAVLGRNGAGKSTLLKHLTGELGKSGVELFGQPLRDIKPAEAAKRRAVLPQQTPLSFAYEVLDVVLLGRIPHGQRETVQDRAIAAACLERVGLSGYETRDVLTLSGGEQQRVHFARTLAQLHGVIGERVLLLDEPTASLDLAHQHATLRLARELCREGVGVLAVLHDLNLAAQYADRVLMLAEGHVIACDHPAVALTPESIRTAYGHEVLVTQHPCLNCPLIVSAS | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28142
Sequence Length: 261
Subcellular Location: Cell membrane
EC: 7.6.2.-
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Q0TBU8 | MISAQNLVYSLQGRRLTDNVSLTFPGGEIVAILGPNGAGKSTLLRQLTGYLQPDSGECRLFNKPLNEWSITELAKHRAVMRQNSHMAFPFSVQEVIQMGRHPHRTGNQDNETAQIMALCDCQALANRDYRQLSGGEQQRVQLARLLVQLWEPTPSPKWLFLDEPTSALDIHHQQHLFRLLRQLVHERQFNVCCVLHDLNLAARYADRVVLMQKGKVIANGKPQDVLTQQALTMLYGADITVLKDPANHSPLIVLDH | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28881
Sequence Length: 256
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q1R597 | MISAQNLVYSLQGRRLTDNVSLTFPGGEIVAILGPNGAGKSTLLRQLTGYLQPDSGECRLFNKPLNEWSITELAKHRAVMRQNSHMAFPFSVQEVIQMGRHPHRTGNQDNETAQIMALCDCQALANRNYRQLSGGEQQRVQLARLLVQLWEPTPSPKWLFLDEPTSALDIHHQQHLFRLLRQLVHERQFNVCCVLHDLNLAARYADRVVLMQKGKVIANGKPQDVLTQQALTMLYGADITVLKDPANHSPLIVLDH | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28880
Sequence Length: 256
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q84EY8 | MAERYTAENLTFTRSGRTLTDNVSLSLSQGELVTLIGPNGAGKSTLLRLLTGYLKPDSGGCSLAGKALDEWHPQTLSRYRAVMRQQSQPGFDWQVEEIVGMGRAPWTRHPEPSIVREVLQLTGCLPLAGRRYHALSGGEQQRVQLARALAQLGVTERRAAWLFLDEPTSALDLYHQQHLLRLLKSLTRQGHLHACVVLHDLNLAALWSDRILLLHNGRIVSQGIPETVLQADALAHWYGAQVHVGMTSGARRTAGFSRPLA | Function: Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28817
Sequence Length: 261
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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P52708 | MAVFISSSGSPGRATATTTTTTTLLLAVLAAAAAAGLLLAPVAARGSPPEHDKQLQLQQQEDDRIPGLPGQPNGVAFGMYGGYVTIDDNNGRALYYWFQEADTADPAAAPLVLWLNGGPGCSSIGLGAMQELGPFRVHTNGESLLLNEYAWNKAANILFAESPAGVVFSYSNTSSDLSMGDDKMAQDTYTFLVKWFERFPHYNYREFYIAGESGHFIPQLSQVVYRNRNNSPFINFQGLLVSSGLTNDHEDMIGMFELWWHHGLISDETRDSGLKVCPGTSFMHPTPECTEVWNKALAEQGNINPYTIYTPTCDREPSPYQRRFWAPHGRAAPPPLMLPPYDPCAVFNSINYLNLPEVQTALHANVSGIVEYPWTVCSNTIFDQWGQAADDLLPVYRELIQAGLRVWVYSGDTDSVVPVSSTRRSLAALELPVKTSWYPWYMAPTEREVGGWSVQYEGLTYVSPSGAGHLVPVHRPAQAFLLFKQFLKGEPMPAEEKNDILLPSEKAPFY | Function: Involved in cyanogenesis, the release of HCN from injured tissues. Is involved in the catabolism of the cyanogenic glycoside dhurrin.
PTM: The N-terminus of chain A is blocked.
Catalytic Activity: (S)-4-hydroxymandelonitrile = 4-hydroxybenzaldehyde + hydrogen cyanide
Sequence Mass (Da): 56319
Sequence Length: 510
EC: 4.1.2.11
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Q9LFT6 | MERKHHFVLVHNAYHGAWIWYKLKPLLESAGHRVTAVELAASGIDPRPIQAVETVDEYSKPLIETLKSLPENEEVILVGFSFGGINIALAADIFPAKIKVLVFLNAFLPDTTHVPSHVLDKYMEMPGGLGDCEFSSHETRNGTMSLLKMGPKFMKARLYQNCPIEDYELAKMLHRQGSFFTEDLSKKEKFSEEGYGSVQRVYVMSSEDKAIPCDFIRWMIDNFNVSKVYEIDGGDHMVMLSKPQKLFDSLSAIATDYM | Function: Involved in cyanogenesis, the release of HCN from injured tissues (By similarity). Displays R-selective hydroxynitrile lyase activity. Also accepts nitromethane (MeNO2) as a donor in a reaction with aromatic aldehydes to yield (R)-beta-nitro alcohols.
Catalytic Activity: (R)-mandelonitrile = benzaldehyde + hydrogen cyanide
Sequence Mass (Da): 29217
Sequence Length: 258
EC: 4.1.2.10
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P52704 | MAFAHFVLIHTICHGAWIWHKLKPLLEALGHKVTALDLAASGVDPRQIEEIGSFDEYSEPLLTFLEALPPGEKVILVGESCGGLNIAIAADKYCEKIAAAVFHNSVLPDTEHCPSYVVDKLMEVFPDWKDTTYFTYTKDGKEITGLKLGFTLLRENLYTLCGPEEYELAKMLTRKGSLFQNILAKRPFFTKEGYGSIKKIYVWTDQDEIFLPEFQLWQIENYKPDKVYKVEGGDHKLQLTKTKEIAEILQEVADTYN | Function: Involved in cyanogenesis, the release of HCN from injured tissues. Decomposes a varieties of (R) or (S) cyanohydrins into HCN and the corresponding aldehydes and ketones. The natural substrate of this enzyme is (S)-acetone cyanohydrin.
PTM: The N-terminus is blocked.
Catalytic Activity: a monosubstituted aliphatic (S)-hydroxynitrile = an aldehyde + hydrogen cyanide
Sequence Mass (Da): 29228
Sequence Length: 257
EC: 4.1.2.47
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P19807 | MSIRNDNASGGYMQPDQSSNASMHKRDLRVEEEIKPLDDMDSKGAVAADGEVHLRKSFSLWSILGVGFGLTNSWFGISTSMVAGISSGGPMMIVYGIIIVALISICIGTSLGELSSAYPHAGGQFWWSLKLAPPKYKRFAAYMCGSFAYAGSVFTSASTTLSVATEVVGMYALTHPEFIPKRWHIFVCFELLHLFLMFFNCYGKSLPIISSSSLYISLLSFFTITITVLACSHGKFNDAKFVFATFNNETGWKNGGIAFIVGLINPAWSFSCLDCATHMAFEVEKPERVIPIAIMGTVAIGFVTSFCYVIAMFFSIQDLDAVLSSTTGAPILDIYNQALGNKSGAIFLGCLILFTSFGCVIACHTWQARLCWSFARDNGLPLSRLWSQVNPHTGVPLNAHLMSCAWITLIGLLYLASSTAFQSLITGCIAFLLLSYIIPVICLLAKKRNIAHGPFWLGKFGFFSNIVLLGWTVFSVVFFSFPPVLPVTKDNMNYVCVVIVGYTAYSILYWKYKGKKEFHALEESENEQAEYSNNFDTIEDSREFSVAASDVELENEHVPWGKK | Function: Sole choline transporter in yeast.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62056
Sequence Length: 563
Subcellular Location: Membrane
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Q7SYS9 | MDSGLRSLLSDHSRYVESFRLFLQNSTEHQCMQHFIETKLPDIISSIGNDKPVIDVLGIGSGSGEIDLQMIAKIQARWPGVSINNQIVEPSAEQILGYKERVAKAPNLGYVTFSWHHQTSSEFEHRVTEDKQMTKYDFIHMIQMLYYVKDVPGTLKFFKSCLAPNGKLLIILVSGNSGWAPLWKKYGQRLPLNDLCLYVTAGDIAEMLSSMGARFQSHELQSDMDITKCFIEGDKNGELLLDFLTETCDFRKNAPAELRDQIICDLKSPRCSTTKDGKVIFNNNLSVIVVEAD | Function: Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine.
Catalytic Activity: histamine + S-adenosyl-L-methionine = H(+) + N(tau)-methylhistamine + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33060
Sequence Length: 293
Subcellular Location: Cytoplasm
EC: 2.1.1.8
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U3NEE3 | MEPTPEMKRNRLPSMNFEAEILADPHDNSELYVIPSMRSLTAEEYVEAFQSFLDHSTEHQCMDEFNKEVMPHIMAGLGNGKSTINILGVGSGTGEQDLKMIQILQAAHPGVLINNEIIEPNPQHVAAYKELVNRAPDLQGVSFTWHQLTSSEYEQQVKEKNTHKKFDFIHMIQMLYRVEDIPNTIKFFHSCLNHQGKLLIIILSDSSGWASLWKKYRHCLPSTDSGHYITSDSITAVLRKLGIKYHVYEFPSGWDITECFIEGDPAGGHMMDFLTGTKNFLGTAPAALRSRLQEALCQPECSSRKDGRVIFCNNLSMIVAES | Function: N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles.
Catalytic Activity: carnosine + S-adenosyl-L-methionine = anserine + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36375
Sequence Length: 322
EC: 2.1.1.22
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P21526 | MQDSHGNTQILNQANSMVKRTWRLLFRIATLILLVSIFVLSLIIVLQSTPGNLQNDINIIRKELNELMENFETTSKSLLSVSNQITYDVSVLTPIRQEAIETNIISKIKDHCKDRVIKEGSTCTLNRSPLHDVSFLNGFNKFYFTYKDNMQIKFKSLLDYPNFIPTATTPHGCIRIPSFSLGQTHWCYTHNINLLGCADPASSNQYVSLGTLQVLKMGDPYFKVEHSHYLNDGRNRKSCSVVAVPDGCLRNCVTMTKNETENFKDLNWQHNYLHTYHIMVPLKTRIINPPGSSRDWVHIAPGVGSGLLYAKLLIFPLYGGLTEKSVIHNNQSGKYFFPNSTKLQCRNSTMEKIKGAKDSYTITYFSGRLIQSAFLVCDLRQFLSEDCEILIPSNDYMMVGAEGRLYNIENNIFYYQRGSSWWPYPSLYRIRLNLSKKYPRITEIKFTKIEIAPRPGNKDCPGNKACPKECITGVYQDILPLSYPNTAFPHLKQAYYTGFYLNNSLERRNPTFYTADNLDYHQQERLGKFNLTAGYSTTTCFKQTTTARLYCLYIIEVGDSVIGDFQITLFLAA | Function: Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion (By similarity).
Catalytic Activity: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 65544
Sequence Length: 573
Subcellular Location: Virion membrane
EC: 3.2.1.18
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P04850 | MVAEDAPVRATCRVLFRTTTLIFLCTLLALSISILYESLITQKQIMSQAGSTGSNSGLGSITDLLNNILSVANQIIYNSAVALPLQLDTLESTLLTAIKSLQTSDKLEQNCSWSAALINDNRYINGINQFYFSIAEGRNLTLGPLLNMPSFIPTATTPEGCTRIPSFSLTKTHWCYTHNVILNGCQDHVSSNQFVSMGIIEPTSAGFPFFRTLKTLYLSDGVNRKSCSISTVPGGCMMYCFVSTQPERDDYFSAAPPEQRIIIMYYNDTIVERIINPPGVLDVWATLNPGTGSGVYYLGWVLFPIYGGVIKGTSLWNNQANKYFIPQMVAALCSQNQATQVQNAKSSYYSSWFGNRMIQSGILACPLRQDLTNECLVLPFSNDQVLMGAEGRLYMYGDSVYYYQRSNSWWPMTMLYKVTITFTNGQPSAISAQNVPTQQVPRPGTGDCSATNRCPGFCLTGVYADAWLLTNPSSTSTFGSEATFTGSYLNTATQRINPTMYIANNTQIISSQQFGSSGQEAAYGHTTCFRDTGSVMVYCIYIIELSSSLLGQFQIVPFIRQVTLS | Function: Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion (By similarity).
Catalytic Activity: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 62205
Sequence Length: 565
Subcellular Location: Virion membrane
EC: 3.2.1.18
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P04853 | MDGDRGKRDSYWSTSPSGSTTKPASGWERSSKADTWLLILSFTQWALSIATVIICIIISARQGYSMKEYSMTVEALNMSSREVKESLTSLIRQEVIARAVNIQSSVQTGIPVLLNKNSRDVIQMIDKSCSRQELTQHCESTIAVHHADGIAPLEPHSFWRCPVGEPYLSSDPEISLLPGPSLLSGSTTISGCVRLPSLSIGEAIYAYSSNLITQGCADIGKSYQVLQLGYISLNSDMFPDLNPVVSHTYDINDNRKSCSVVATGTRGYQLCSMPTVDERTDYSSDGIEDLVLDVLDLKGRTKSHRYRNSEVDLDHPFSALYPSVGNGIATEGSLIFLGYGGLTTPLQGDTKCRTQGCQQVSQDTCNEALKITWLGGKQVVSVIIQVNDYLSERPKIRVTTIPITQNYLGAEGRLLKLGDRVYIYTRSSGWHSQLQIGVLDVSHPLTINWTPHEALSRPGNKECNWYNKCPKECISGVYTDAYPLSPDAANVATVTLYANTSRVNPTIMYSNTTNIINMLRIKDVQLEAAYTTTSCITHFGKGYCFHIIEINQKSLNTLQPMLFKTSIPKLCKAES | Function: Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion.
PTM: N-glycosylated; glycans consist of a mixture of high mannose-type oligosaccharides and of complex-type oligosaccharides.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Sequence Mass (Da): 63410
Sequence Length: 575
Subcellular Location: Virion membrane
EC: 3.2.1.18
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P72849 | MSVNLASQLREGTKKSHSMAENVGFVKCFLKGVVEKNSYRKLVGNLYFVYSAMEEEMAKFKDHPILSHIYFPELNRKQSLEQDLQFYYGSNWRQEVKISAAGQAYVDRVRQVAATAPELLVAHSYTRYLGDLSGGQILKKIAQNAMNLHDGGTAFYEFADIDDEKAFKNTYRQAMNDLPIDQATAERIVDEANDAFAMNMKMFNELEGNLIKAIGIMVFNSLTRRRSQGSTEVGLATSEG | Function: Catalyzes the opening of the heme ring with the release of iron. Key enzyme in the synthesis of the chromophoric part of the photosynthetic antennae.
Catalytic Activity: heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]
Sequence Mass (Da): 27051
Sequence Length: 240
EC: 1.14.14.18
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P74133 | MTNLAQKLRYGTQQSHTLAENTAYMKCFLKGIVEREPFRQLLANLYYLYSALEAALRQHRDNEIISAIYFPELNRTDKLAEDLTYYYGPNWQQIIQPTPCAKIYVDRLKTIAASEPELLIAHCYTRYLGDLSGGQSLKNIIRSALQLPEGEGTAMYEFDSLPTPGDRRQFKEIYRDVLNSLPLDEATINRIVEEANYAFSLNREVMHDLEDLIKAAIGEHTFDLLTRQDRPGSTEARSTAGHPITLMVGE | Function: Catalyzes the opening of the heme ring with the release of iron. Key enzyme in the synthesis of the chromophoric part of the photosynthetic antennae.
Catalytic Activity: heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]
Sequence Mass (Da): 28540
Sequence Length: 250
EC: 1.14.14.18
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Q6D796 | MAKKILLCDPTLRDGNHAVRHQLTRESFAAYCQAAEAANVPVVEVGHGNGLGASSMLVGECLLSDEDIFTISREHLHKSRMAIHLIPGFCTIKKDLTRALELGVDLFRVASHCTEADITDRHIHFVRNSGKEAWGILMMSHMTSPAVLLEEARKMESYGAEAIVIMDSAGAYFPDDVKERISTLVNGLTVPVGFHGHNNLGMSVINSVVAVQEGATIIDGTIRGFGAGAGNTQLEVLVAVFERLGYETGIDLYKILDAADIAEKGFNPVAPSISPLSIVSGLAGVFSGFAKPVAKAAKDYNVDPRDIFFGLGERKAVAGQESLIYEVARDLAKRNENSVEKGQ | Function: Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds.
Catalytic Activity: (S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
Sequence Mass (Da): 36890
Sequence Length: 343
Pathway: Aromatic compound metabolism; 3-phenylpropanoate degradation.
EC: 4.1.3.39
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P51016 | MTFNPSKKLYISDVTLRDGSHAIRHQYTLDDVRAIARALDKAKVDSIEVAHGDGLQGSSFNYGFGRHTDLEYIEAVAGEISHAQIATLLLPGIGSVHDLKNAYQAGARVVRVATHCTEADVSKQHIEYARNLGMDTVGFLMMSHMIPAEKLAEQGKLMESYGATCIYMADSGGAMSMNDIRDRMRAFKAVLKPETQVGMHAHHNLSLGVANSIVAVEEGCDRVDASLAGMGAGAGNAPLEVFIAVAERLGWNHGTDLYTLMDAADDIVRPLQDRPVRVDRETLGLGYAGVYSSFLRHAEIAAAKYNLKTLDILVELGHRRMVGGQEDMIVDVALDLLAAHKENRA | Function: Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds such as phenols, cresols and catechols.
Catalytic Activity: (S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
Sequence Mass (Da): 37471
Sequence Length: 345
Pathway: Aromatic compound metabolism; benzoate degradation via hydroxylation.
EC: 4.1.3.39
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