ID   HIS5_AZOBR              Reviewed;         192 AA.
AC   P18785;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 2.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Imidazole glycerol phosphate synthase subunit HisH;
DE            EC=4.3.2.10;
DE   AltName: Full=IGP synthase glutaminase subunit;
DE            EC=3.5.1.2;
DE   AltName: Full=IGP synthase subunit HisH;
DE   AltName: Full=ImGP synthase subunit HisH;
DE            Short=IGPS subunit HisH;
GN   Name=hisH;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sp6;
RX   PubMed=2664449; DOI=10.1007/bf00334360;
RA   Fani R., Bazzicalupo M., Damiani G., Bianchi A., Schipani C.,
RA   Sgaramella V., Polsinelli M.;
RT   "Cloning of histidine genes of Azospirillum brasilense: organization of the
RT   ABFH gene cluster and nucleotide sequence of the hisB gene.";
RL   Mol. Gen. Genet. 216:224-229(1989).
CC   -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP,
CC       AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of
CC       glutamine to glutamate and ammonia as part of the synthesis of IGP and
CC       AICAR. The resulting ammonia molecule is channeled to the active site
CC       of HisF (By similarity). {ECO:0000250}.
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   -!- 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   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC   -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- CAUTION: Compared to other HisH it lacks an internal segment that
CC       normally contains the Cys active site residue. {ECO:0000305}.
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DR   EMBL; X17435; CAA35479.1; -; Genomic_DNA.
DR   EMBL; X61207; CAA43516.1; -; Genomic_DNA.
DR   PIR; S16799; PE0007.
DR   AlphaFoldDB; P18785; -.
DR   SMR; P18785; -.
DR   UniPathway; UPA00031; UER00010.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01748; GATase1_IGP_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 2.
DR   HAMAP; MF_00278; HisH; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR010139; Imidazole-glycPsynth_HisH.
DR   PANTHER; PTHR42701; PTHR42701; 2.
DR   Pfam; PF00117; GATase; 1.
DR   PIRSF; PIRSF000495; Amidotransf_hisH; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR01855; IMP_synth_hisH; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Glutamine amidotransferase;
KW   Histidine biosynthesis; Hydrolase; Lyase.
FT   CHAIN           1..192
FT                   /note="Imidazole glycerol phosphate synthase subunit HisH"
FT                   /id="PRO_0000152336"
FT   DOMAIN          3..192
FT                   /note="Glutamine amidotransferase type-1"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   192 AA;  20826 MW;  AB07AB18A14257B9 CRC64;
     METVALIDYG SGNLRSPAKA LERAAAGCHA SFQVLVTSDA DAVRKADRVV LPAVGAFADC
     KRGLSEVPGM QLMAEGGREY GVTEGLGWIK GEVVKLEPAD PTLKIPHMGW NELDIRREHP
     VLAGLRERAH AYFVHSYRFA VERPEDVIAS ADYGGPFAAV VGRDNLVGTQ FHPEKSQETG
     LALVANFLTW RV