ID   HIS62_VIBVY             Reviewed;         272 AA.
AC   Q7MPP3;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Putative imidazole glycerol phosphate synthase subunit hisF2;
DE            EC=4.3.2.10;
DE   AltName: Full=IGP synthase cyclase subunit;
DE   AltName: Full=IGP synthase subunit hisF2;
DE   AltName: Full=ImGP synthase subunit hisF2;
DE            Short=IGPS subunit hisF2;
GN   Name=hisF2; OrderedLocusNames=VV0319;
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 HisF subunit catalyzes the cyclization
CC       activity that produces IGP and AICAR from PRFAR using the ammonia
CC       provided by the HisH subunit (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   -!- 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   -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
CC   -!- CAUTION: The potential active site Asp residue in position 14 is
CC       replaced by a Val. {ECO:0000305}.
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DR   EMBL; BA000037; BAC93083.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7MPP3; -.
DR   SMR; Q7MPP3; -.
DR   EnsemblBacteria; BAC93083; BAC93083; BAC93083.
DR   KEGG; vvy:VV0319; -.
DR   HOGENOM; CLU_048577_4_0_6; -.
DR   OMA; IMPCLDM; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:InterPro.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04731; HisF; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR020021; Glycosyl_amidation-assoc_WbuZ.
DR   InterPro; IPR006062; His_biosynth.
DR   InterPro; IPR004651; HisF.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF00977; His_biosynth; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR03572; WbuZ; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Lyase;
KW   Reference proteome.
FT   CHAIN           1..272
FT                   /note="Putative imidazole glycerol phosphate synthase
FT                   subunit hisF2"
FT                   /id="PRO_0000142262"
FT   ACT_SITE        133
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   272 AA;  30050 MW;  A3EBEF28B3FB67F2 CRC64;
     MFHMLKIRLI PCIVTKGELV VQSFAFKNYL PIGNVKTAID FFVNWDVDEI IVNDIDASKE
     FREPNVDLVS WAAKECFVPL TVGGGIKTLE HIRNLLKAGA DKVTINTKAI DDPDFIKNAA
     SVFGSQCITV SVDAIKQGNV YKLYDYRDGR VLDVDVVDWV RKVESYGAGE ILLNSVDRDG
     SREGYDVELL KTVSGIVSIP VIALGGIGRF DQLAEGAIEG GCQALSAANI FQHMEHSTIA
     AKAQMRNAKL NVRLSSKVKY ENFDLDFLGR PY