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Database: UniProt
Entry: W2PHH6_PHYPN
LinkDB: W2PHH6_PHYPN
Original site: W2PHH6_PHYPN 
ID   W2PHH6_PHYPN            Unreviewed;       548 AA.
AC   W2PHH6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=PPTG_18258 {ECO:0000313|EMBL:ETN00292.1};
OS   Phytophthora parasitica (strain INRA-310).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN00292.1, ECO:0000313|Proteomes:UP000018817};
RN   [1] {ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETN00292.1, ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|EMBL:ETN00292.1,
RC   ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica INRA-310.";
RL   Submitted (NOV-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}.
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DR   EMBL; KI669640; ETN00292.1; -; Genomic_DNA.
DR   RefSeq; XP_008914498.1; XM_008916250.1.
DR   AlphaFoldDB; W2PHH6; -.
DR   STRING; 761204.W2PHH6; -.
DR   EnsemblProtists; ETN00292; ETN00292; PPTG_18258.
DR   GeneID; 20187157; -.
DR   VEuPathDB; FungiDB:PPTG_18258; -.
DR   OMA; EAMGTGE; -.
DR   OrthoDB; 2782495at2759; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000018817; 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:UP000018817}.
FT   DOMAIN          6..197
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   REGION          360..361
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          398..400
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          473..474
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          499..500
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          522..523
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        190
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        190
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        192
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT   ACT_SITE        238
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT   ACT_SITE        400
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         328
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   BINDING         468
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
SQ   SEQUENCE   548 AA;  59358 MW;  8988AD499BAACB46 CRC64;
     MVEVTVLDYG AGNVRSLKNA IRAAGHSVKD VSCAEDIRNA DVLIFPGVGN FRAAMEFLNT
     SGYVEELKSY IAADRRFMGI CLGMQTLFEG SEECPELKGL GIIKGKVARF PSEQVTVPHI
     GWNGINAWKK SALFASLPVS TEEAMVYFVH SFRATKTDKN ADWVLSTTNY GELEFVSAVQ
     KGNVMATQFH PEKSGAVGIA ILKGFLENKD LADHDAPIPT AVAAPRTTLS KRIIACLDVR
     ANDQGDLVVT KGDQYDVRET SDSAEGGNVR NMGKPVDLCK RYFEEGADEV AFLNITSFRE
     QPMGDLPMVQ VLEASSECVF VPLTIGGGIR EYVDDQQKTH SALDVAALYF RSGADKVSIG
     SDAVYTAEKY YANGGKGDGS SSIETISAVY GNQAVVVSMD PKRVYVASFY DENAKGHNVV
     KLSQPGPNGE EYCWYQMTVR GGREARDIDV VQLAQAVEAL GAGELLLNCV DMDGQKAGYD
     LDLISLVKKS VRIPVVASSG AGKPEHFTEV FEKTNCDAAL AAGIFHRKEV AIQDVKAQLH
     TDNISVRL
//
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