ID   HIS52_VIBVY             Reviewed;         214 AA.
AC   Q7MPP4;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Imidazole glycerol phosphate synthase subunit HisH 2;
DE            EC=4.3.2.10;
DE   AltName: Full=IGP synthase glutaminase subunit 2;
DE            EC=3.5.1.2;
DE   AltName: Full=IGP synthase subunit HisH 2;
DE   AltName: Full=ImGP synthase subunit HisH 2;
DE            Short=IGPS subunit HisH 2;
GN   Name=hisH2; OrderedLocusNames=VV0318;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP,
CC       AICAR and glutamate. The HisH subunit provides the glutamine
CC       amidotransferase activity that produces the ammonia necessary to HisF
CC       for the synthesis of IGP and AICAR (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; BA000037; BAC93082.1; -; Genomic_DNA.
DR   RefSeq; WP_011149291.1; NC_005139.1.
DR   AlphaFoldDB; Q7MPP4; -.
DR   SMR; Q7MPP4; -.
DR   EnsemblBacteria; BAC93082; BAC93082; BAC93082.
DR   KEGG; vvy:VV0318; -.
DR   HOGENOM; CLU_071837_2_0_6; -.
DR   OMA; DKVPHMG; -.
DR   OrthoDB; 1726024at2; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000002675; Chromosome I.
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; Reference proteome.
FT   CHAIN           1..214
FT                   /note="Imidazole glycerol phosphate synthase subunit HisH
FT                   2"
FT                   /id="PRO_0000152445"
FT   DOMAIN          2..210
FT                   /note="Glutamine amidotransferase type-1"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        185
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   214 AA;  24405 MW;  1B0323A37B77FC5D CRC64;
     MKIVIIDYDM GNVRSIENAI NHIGDYTIIV SGEPDTIRSA DCLILPGVGA FPDAMKKLEQ
     QKLIDLLTEE VVVRRKPVLG ICLGMQLLFE SSEEIQLTKG LGWIPGKVEY MRPGNDLRVP
     HVGWNSLILK KENSLFDYLQ DDKDFYFVHS LWVNCPEKYK LATFEYGIEM TASVQYENIV
     GMQFHPEKSQ RNGLEAIRSF LDWVKIQKLG VSHA