ID K1VFA9_TRIAC Unreviewed; 597 AA.
AC K1VFA9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=A1Q2_02955 {ECO:0000313|EMBL:EKD02725.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD02725.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKD02725.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD02725.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
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:EKD02725.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMBO01000277; EKD02725.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VFA9; -.
DR STRING; 1220162.K1VFA9; -.
DR eggNOG; KOG0623; Eukaryota.
DR HOGENOM; CLU_037550_0_0_1; -.
DR InParanoid; K1VFA9; -.
DR OMA; EAMGTGE; -.
DR OrthoDB; 2782495at2759; -.
DR UniPathway; UPA00031; UER00010.
DR Proteomes; UP000006757; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006757}.
FT DOMAIN 18..221
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT REGION 389..390
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 431..433
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 517..518
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 543..544
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT REGION 566..567
FT /note="PRFAR binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT ACT_SITE 93
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT ACT_SITE 93
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 208
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 208
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT ACT_SITE 210
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 210
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT ACT_SITE 270
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT ACT_SITE 433
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT BINDING 93
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT BINDING 512
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
SQ SEQUENCE 597 AA; 64218 MW; B2DB4B46A3984921 CRC64;
MATSQTSQDT QTRPKLYVLD YGAGNVRSLA NSIERLGYEF EWIKSVEDFD KAEKLIFPGV
GSFHQAARGL KERGVFEPLL QYIRSGKPYF GICIGMQVLF AGSTEAPGEA GLNVIPYPIT
KFDTEGGTKS VPHMGWNGAW GAYADVAADK DALVVPEEDY YFVHSYAALL GQPGEESVRE
AAHTLSRYGK QTFVSSVRMG NVFGTQFHPE KSGPAGLETL RRWLAAPISA VSALPHPLAP
RPASEWVSAD PRPERAAGTG LTARIVACLD VRSNDAGDLV VTKGDQYDVR EKDEGAGVRN
LGKPVELAQR YYMNGADEVC FLNITSFRSS ALQDQPMLDV VRASAGTVFV PLTVGGGIKD
TVDPDGTPRS ALEVAGAYFR AGADKVSIGS EAVLNVEDML AREARGEEPL TGKTGIETIA
KGYGSQAVVV SIDPKRVYYD TTETNWLQAV PEAHRPCLVT GETATTRTKP DEQGKAWWYQ
CTISGGRAVR DIDVVQLARG VERLGAGEIL LNSVDRDGSG KGFDLDLIKL VRDAVSIPVV
ASSGAGSPKD FEEVFEKTGV EAALAAGIFH RGEVGIDEVK DELKRDGIPV RQTALAP
//