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Database: UniProt
Entry: K1VFA9_TRIAC
LinkDB: K1VFA9_TRIAC
Original site: K1VFA9_TRIAC 
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}.
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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
//
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