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Database: UniProt
Entry: W9WT02_9EURO
LinkDB: W9WT02_9EURO
Original site: W9WT02_9EURO 
ID   W9WT02_9EURO            Unreviewed;       587 AA.
AC   W9WT02;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   13-SEP-2023, entry version 33.
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=A1O5_11765 {ECO:0000313|EMBL:EXJ61449.1};
OS   Cladophialophora psammophila CBS 110553.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ61449.1, ECO:0000313|Proteomes:UP000019471};
RN   [1] {ECO:0000313|EMBL:EXJ61449.1, ECO:0000313|Proteomes:UP000019471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ61449.1,
RC   ECO:0000313|Proteomes:UP000019471};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL   Submitted (MAR-2013) 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:EXJ61449.1}.
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DR   EMBL; AMGX01000028; EXJ61449.1; -; Genomic_DNA.
DR   RefSeq; XP_007750525.1; XM_007752335.1.
DR   AlphaFoldDB; W9WT02; -.
DR   STRING; 1182543.W9WT02; -.
DR   GeneID; 19196452; -.
DR   eggNOG; KOG0623; Eukaryota.
DR   HOGENOM; CLU_037550_0_0_1; -.
DR   OrthoDB; 2782495at2759; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000019471; 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   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:UP000019471}.
FT   DOMAIN          6..213
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   REGION          398..399
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          436..438
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          508..509
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          534..535
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          557..558
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   ACT_SITE        81
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT   ACT_SITE        81
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        207
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT   ACT_SITE        209
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        209
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT   ACT_SITE        272
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT   BINDING         81
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   BINDING         365
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   BINDING         503
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
SQ   SEQUENCE   587 AA;  62736 MW;  1CDDF701AC32ED6C CRC64;
     MPKVHLLDYV AGNIRSLVNA IEKCGWEVEW IRSPQDVQKA DKIILPGVGH FGHCLTSLST
     AGYLPAIQSH ISSGKSFFGI CVGLQALFTG SEEAPSVTGL NIIPTSLKRF SAENADGSKK
     SVPCIGWNDA STLHPDWDQS HATALEKGKS FYGLNQGSKY YYVHSYFAPY VPGELEAEGW
     VVASATYGDE TYVGAIGKGN VFATQFHPEK SGAAGLRVIK AFLEGKIWSD PVVLSVFGTT
     STAANGVFSS LAGRTGDGGT NGLTRRIIAC LDVRTNDQGD LVVTKGDQYD VREKSSLTSA
     TGPGQVRNLG KPVDMARRYY EQGADEITFL NITSFRDCPI TDLPMLEILR RTSETVFVPL
     TIGGGIRDMT DPVTGKNVSA LDVAKLYFAS GADKVSIGSD AVLAAEEYHS SGGNLSGRTS
     IETISAAYGA QAVVVSVDPK RIYVSSPSDT AHHTVRTAFP DPQGREYVWY ACTIKGGRET
     RDLDVVQLCT AVQALGAGEI LLNAIDRDGS NRGYDLELIN MVKAAVGVPV IASSGAGVPG
     HFEEVFRRTG VDAALGAGMF HRGEYTVAQV KEHLGQAGLL VRPFEEF
//
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