ID A0A0A8LBZ0_9SACH Unreviewed; 552 AA.
AC A0A0A8LBZ0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 13-SEP-2023, entry version 27.
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 ORFNames=KLDO_g3867 {ECO:0000313|EMBL:CDO95633.1};
OS Kluyveromyces dobzhanskii CBS 2104.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO95633.1, ECO:0000313|Proteomes:UP000031516};
RN [1] {ECO:0000313|EMBL:CDO95633.1, ECO:0000313|Proteomes:UP000031516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA Nystedt B., Astrom S.;
RT "The genome of Kluyveromyces dobzhanskii.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDO95633.1}.
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DR EMBL; CCBQ010000045; CDO95633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A8LBZ0; -.
DR OrthoDB; 2782495at2759; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000031516; Unassembled WGS sequence.
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 194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 194
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT ACT_SITE 196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 196
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; 60531 MW; B5D761A33FCFAE07 CRC64;
MTVVHIIDVE SGNLQSLQNA VNYLGYETRL IKSATDPELQ TAEQIILPGV GNFGHFVDNL
TSRGFEQPIK DYIASGRPLM GICVGLQALF NGSVESPSSK GLSFINGTLS KFDTSEGKSV
PEIGWNTVIP EADLFFGLDP YKRYYFVHSF AMIVDENRVN EMNKEGWNVA LTKYGNETFV
SAIHRDNVFA TQFHPEKSGK AGLQIIDNFL KGIHPVTEYS NEQKSLLEND YTNFGLTRRI
IACLDVRTND QGDLVVTKGD QYDVREKSDE GDVRNLGKPV ELAQRYYDQG ADEVTFLNIT
SFRNCPLKDT PMLDVLKLAA KTVFVPLTVG GGIKDVVDVD GTKVPALEVA GMYFRSGADK
VSIGTDAVFA AEKFYANGEK GDGTSPIETI SKAYGAQAVV ISVDPKRVYV NNENETKNKC
FQTSRPNAEG QNWCWYQCTI MGGRESRDLG AWELAHACEA LGAGEILLNC IDKDGSNSGY
DLELIDYVKS AVSIPVIASS GAGNPSHFEE GFIKTRADAC LGAGMFHRGE YTVNEVKSHL
TSSGLKVRID KE
//
