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Database: UniProt
Entry: G2YU89_BOTF4
LinkDB: G2YU89_BOTF4
Original site: G2YU89_BOTF4 
ID   G2YU89_BOTF4            Unreviewed;       541 AA.
AC   G2YU89;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   13-SEP-2023, entry version 54.
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=BofuT4_P160080.1 {ECO:0000313|EMBL:CCD55187.1};
OS   Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD55187.1, ECO:0000313|Proteomes:UP000008177};
RN   [1] {ECO:0000313|Proteomes:UP000008177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; FQ790353; CCD55187.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2YU89; -.
DR   STRING; 999810.G2YU89; -.
DR   eggNOG; KOG0623; Eukaryota.
DR   HOGENOM; CLU_037550_0_0_1; -.
DR   InParanoid; G2YU89; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000008177; Unplaced contigs.
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:UP000008177}.
FT   DOMAIN          6..193
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   REGION          351..352
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          389..391
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          461..462
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          487..488
FT                   /note="PRFAR binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   REGION          510..511
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        188
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        188
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
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        232
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-1"
FT   ACT_SITE        391
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         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
FT   BINDING         456
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036936-2"
SQ   SEQUENCE   541 AA;  58525 MW;  713911FEBA029859 CRC64;
     MSKVYLLDYV AGNVRSLANA IEKVGYTIEW IRSPEDVPKA DKLILPGVGH FGHCMTQFSK
     AGYLPAIQKH IDSGKPFMGI CVGLQALFEG SAENPAVPGL GYVKATLDRF DDSSKSVPHI
     GWNSANTSGK EVFGLRPSSK YYYVHSYKVP YKQGELESQG WTVATARYGD EEFVGAIAKG
     NILATQFHPE KSGVAGLRVI KAFLDGDNNS SAVEGLVAAK EGLTRRVIAC LDVRTNDQGD
     LVVTKGDQYD VREKTDGGNV RNLGKPVEMA KKYYEQGADE VTFLNITSFR DCPVADVPML
     EILRQTSKSV FVPLTIGGGI RDTIDTDGTK ISALEIATMY FQSGADKVSI GSDAVTAAEE
     YYSNGKKLSG ATAIEQISGA YGNQAVVVSV DPKRVYVSKP EETQHNTIRT RYPGPNGEEY
     CWYACTIKGG RETRDMDVVE LVTAVEAMGT GEILLNCIDK DGTNSGFDLE LIDQVKNAVS
     IPVIASSGAG NPGHFEEVFS KTSTDAALGA GMFHRGEYTV KQVKDSLAEK GLMVRQFESD
     L
//
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