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Database: UniProt
Entry: G2W9Q1_YEASK
LinkDB: G2W9Q1_YEASK
Original site: G2W9Q1_YEASK 
ID   G2W9Q1_YEASK            Unreviewed;       552 AA.
AC   G2W9Q1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   13-SEP-2023, entry version 45.
DE   RecName: Full=Imidazole glycerol phosphate synthase hisHF {ECO:0000256|PIRNR:PIRNR036936};
DE   Includes:
DE     RecName: Full=Glutaminase {ECO:0000256|PIRNR:PIRNR036936};
DE              EC=3.5.1.2 {ECO:0000256|PIRNR:PIRNR036936};
DE   Includes:
DE     RecName: Full=Cyclase {ECO:0000256|PIRNR:PIRNR036936};
GN   Name=K7_HIS7 {ECO:0000313|EMBL:GAA21794.1};
GN   ORFNames=SYK7_005571 {ECO:0000313|EMBL:GAA21794.1};
OS   Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=721032 {ECO:0000313|EMBL:GAA21794.1, ECO:0000313|Proteomes:UP000001608};
RN   [1] {ECO:0000313|EMBL:GAA21794.1, ECO:0000313|Proteomes:UP000001608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyokai no. 7 / NBRC 101557 {ECO:0000313|Proteomes:UP000001608};
RX   PubMed=21900213; DOI=10.1093/dnares/dsr029;
RA   Akao T., Yashiro I., Hosoyama A., Kitagaki H., Horikawa H., Watanabe D.,
RA   Akada R., Ando Y., Harashima S., Inoue T., Inoue Y., Kajiwara S.,
RA   Kitamoto K., Kitamoto N., Kobayashi O., Kuhara S., Masubuchi T.,
RA   Mizoguchi H., Nakao Y., Nakazato A., Namise M., Oba T., Ogata T., Ohta A.,
RA   Sato M., Shibasaki S., Takatsume Y., Tanimoto S., Tsuboi H., Nishimura A.,
RA   Yoda K., Ishikawa T., Iwashita K., Fujita N., Shimoi H.;
RT   "Whole-genome sequencing of sake yeast Saccharomyces cerevisiae Kyokai no.
RT   7.";
RL   DNA Res. 18:423-434(2011).
CC   -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP,
CC       AICAR and glutamate. The glutaminase domain produces the ammonia
CC       necessary for the cyclase domain to produce IGP and AICAR from PRFAR.
CC       The ammonia is channeled to the active site of the cyclase domain.
CC       {ECO:0000256|PIRNR:PIRNR036936}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-
CC         phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-
CC         amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-
CC         erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate;
CC         Xref=Rhea:RHEA:24793, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58278, ChEBI:CHEBI:58359, ChEBI:CHEBI:58475,
CC         ChEBI:CHEBI:58525; EC=4.3.2.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00000619,
CC         ECO:0000256|PIRNR:PIRNR036936};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC         Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001062,
CC         ECO:0000256|PIRNR:PIRNR036936};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC       {ECO:0000256|ARBA:ARBA00005091, ECO:0000256|PIRNR:PIRNR036936}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family.
CC       {ECO:0000256|RuleBase:RU003657}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the HisA/HisF family.
CC       {ECO:0000256|PIRNR:PIRNR036936}.
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DR   EMBL; DG000038; GAA21794.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2W9Q1; -.
DR   SMR; G2W9Q1; -.
DR   HOGENOM; CLU_037550_0_0_1; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000001608; Chromosome II.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01748; GATase1_IGP_Synthase; 1.
DR   CDD; cd04731; HisF; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00278; HisH; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR006062; His_biosynth.
DR   InterPro; IPR004651; HisF.
DR   InterPro; IPR014640; IGPS_HisHF.
DR   InterPro; IPR010139; Imidazole-glycPsynth_HisH.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR00735; hisF; 1.
DR   NCBIfam; TIGR01855; IMP_synth_hisH; 1.
DR   PANTHER; PTHR21235:SF2; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE HISHF; 1.
DR   PANTHER; PTHR21235; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H IGP SYNTHASE SUBUNIT HISF/H; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00977; His_biosynth; 1.
DR   PIRSF; PIRSF036936; IGPS_HisHF; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR036936};
KW   Glutamine amidotransferase {ECO:0000256|PIRNR:PIRNR036936,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102,
KW   ECO:0000256|PIRNR:PIRNR036936};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036936};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR036936};
KW   Multifunctional enzyme {ECO:0000256|PIRNR:PIRNR036936}.
FT   DOMAIN          6..210
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   REGION          364..365
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          402..404
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          474..475
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          500..501
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          523..524
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   ACT_SITE        83
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT   ACT_SITE        83
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        193
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        195
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT   ACT_SITE        404
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT   BINDING         83
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   BINDING         332
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   BINDING         469
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
SQ   SEQUENCE   552 AA;  61068 MW;  046E11EA5F83ABA3 CRC64;
     MPVVHVIDVE SGNLQSLTNA IEHLGYEVQL VKSPKDFNIS GTSRLILPGV GNYGHFVDNL
     FNRGFEKPIR EYIESGKPIM GICVGLQALF AGSVESPKST GLNYIDFKLS RFDDSEKPVP
     EIGWNSCIPS ENLFFGLDPY KRYYFVHSFA AILNSEKKKN LENDGWKIAK AKYGSEEFIA
     AVNKNNIFAT QFHPEKSGKA GLNVIENFLK QQSPPIPNYS AEEKELLMND YSNYGLTRRI
     IACLDVRTND QGDLVVTKGD QYDVREKSDG KGVRNLGKPV QLAQKYYQQG ADEVTFLNIT
     SFRDCPLKDT PMLEVLKQAA KTVFVPLTVG GGIKDIVDVD GTKIPALEVA SLYFRSGADK
     VSIGTDAVYA AEKYYELGNR GDGTSPIETI SKAYGAQAVV ISVDPKRVYV NSQADTKNKV
     FETEYPGPNG EKYCWYQCTI KGGRESRDLG VWELTRACEA LGAGEILLNC IDKDGSNSGY
     DLELIEHVKD AVKIPVIASS GAGVPEHFEE AFLKTRADAC LGAGMFHRGE FTVNDVKEYL
     LEHGLKVRMD EE
//
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