ID G0VIU9_NAUCC Unreviewed; 553 AA.
AC G0VIU9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=NCAS0H01160 {ECO:0000313|EMBL:CCC71426.1};
GN OrderedLocusNames=NCAS_0H01160 {ECO:0000313|EMBL:CCC71426.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC71426.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC71426.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) 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}.
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DR EMBL; HE576759; CCC71426.1; -; Genomic_DNA.
DR RefSeq; XP_003677775.1; XM_003677727.1.
DR AlphaFoldDB; G0VIU9; -.
DR STRING; 1064592.G0VIU9; -.
DR GeneID; 11528925; -.
DR KEGG; ncs:NCAS_0H01160; -.
DR eggNOG; KOG0623; Eukaryota.
DR HOGENOM; CLU_037550_0_0_1; -.
DR InParanoid; G0VIU9; -.
DR OMA; GNYGHFV; -.
DR OrthoDB; 2782495at2759; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000001640; Chromosome 8.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001640}.
FT DOMAIN 7..211
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT REGION 365..366
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 403..405
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 475..476
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 501..502
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 524..525
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT ACT_SITE 84
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT ACT_SITE 84
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 246
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT ACT_SITE 405
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT BINDING 84
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT BINDING 333
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT BINDING 470
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
SQ SEQUENCE 553 AA; 61171 MW; C78341CC9306537B CRC64;
MSSTVHVIDV ESGNLQSLTN AIEYLGYKVH LIKTPSDPEL ANANRLILPG VGNYGHFVDN
LFSRGFEQPI KSYISSGRPI MGICVGLQAL FSGSVESPES SGLKLIELVL GRFNDDEKPV
PQIGWNSIID DDELFFGLDP LKRYYFVHSF AAILNESIEQ KLKNQGWKLA KARYGTEEFI
AAVWRQNVFA TQFHPEKSGK AGLQIIDNFL KQQHPKLPNY LEEEKQLLSN DYSNYGLTRR
IIACLDVRSN DQGDLVVTKG DQYDVREKEG NKDVKNLGKP VQLAKKYYQQ GADEVTFLNI
TSFRDCPLRD APMLQVLKNS AKTVFVPLTV GGGIKDIVDV DGTKIPALEV ASLYFRSGAD
KVSIGTDAVY AAEKFYALGG HGDGTSPIET ISKAYGAQAV VISVDPKRVY VDSPSDTKNK
TFKTKFPDSK GRTWCWYQCT IKGGRESRDL GVWELTRACE RLGAGEILLN CIDKDGSNSG
YDLELIQHVK DAVRIPVIAS SGAGNPEHFE EAFTETGADA CLGAGIFHRG EYTVNDVKEF
LLTHGLKVRM DNN
//
