ID   HIS5_LEPBO              Reviewed;         204 AA.
AC   Q9ZGM1;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 95.
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   Leptospira borgpetersenii.
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=174;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=L171 / Serovar Hardjobovis;
RX   PubMed=10458921; DOI=10.1006/mpat.1999.0285;
RA   Kalambaheti T., Bulach D.M., Rajakumar K., Adler B.;
RT   "Genetic organization of the lipopolysaccharide O-antigen biosynthetic
RT   locus of Leptospira borgpetersenii serovar Hardjobovis.";
RL   Microb. Pathog. 27:105-117(1999).
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}.
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DR   EMBL; AF078135; AAD12948.1; -; Genomic_DNA.
DR   RefSeq; WP_011669952.1; NZ_VCHK01000056.1.
DR   AlphaFoldDB; Q9ZGM1; -.
DR   SMR; Q9ZGM1; -.
DR   OMA; DKVPHMG; -.
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; -; 1.
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; 1.
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..204
FT                   /note="Imidazole glycerol phosphate synthase subunit HisH"
FT                   /id="PRO_0000152385"
FT   DOMAIN          1..204
FT                   /note="Glutamine amidotransferase type-1"
FT   ACT_SITE        80
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        186
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        188
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   204 AA;  22841 MW;  2439005C152FD353 CRC64;
     MIGILDYGVG NLKAFANVLK GLNFHHQIVK TEQELKGCEK IIMPGVGSFD SVMNKLIESG
     IRDVLSDLII NKKIPILGVC VGMQILASSS EEGSKSGLGW IRGRVKKFNF DRSDFSLTIP
     QIGWNEVNST KENTLLKNLE KNPRFYFLHS YYIECEDKKD VIAIANYGGD FTCAVNRENI
     YGTQFHPEKS HHNGVALIRN FASL