ID   HIS63_VIBVY             Reviewed;         260 AA.
AC   Q7MPK7;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Putative imidazole glycerol phosphate synthase subunit hisF3;
DE            EC=4.3.2.10;
DE   AltName: Full=IGP synthase cyclase subunit;
DE   AltName: Full=IGP synthase subunit hisF3;
DE   AltName: Full=ImGP synthase subunit hisF3;
DE            Short=IGPS subunit hisF3;
GN   Name=hisF3; OrderedLocusNames=VV0356;
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 16 is
CC       replaced by a Leu. {ECO:0000305}.
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DR   EMBL; BA000037; BAC93120.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7MPK7; -.
DR   SMR; Q7MPK7; -.
DR   EnsemblBacteria; BAC93120; BAC93120; BAC93120.
DR   KEGG; vvy:VV0356; -.
DR   HOGENOM; CLU_048577_4_0_6; -.
DR   OMA; PKYVGDP; -.
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:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; IPR006062; His_biosynth.
DR   InterPro; IPR004651; HisF.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF00977; His_biosynth; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Lyase;
KW   Reference proteome.
FT   CHAIN           1..260
FT                   /note="Putative imidazole glycerol phosphate synthase
FT                   subunit hisF3"
FT                   /id="PRO_0000142263"
FT   ACT_SITE        135
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   260 AA;  28730 MW;  E095271CAD7213DE CRC64;
     MRVYRMLRSR VIPVLLMREK GLVKTVKFKE GKYVGDPLNA VKIFNEQEAD ELTLLDIDAS
     RLGHEPDYVL IERIASECRM PLCYGGGIKT VEQAERILKL GVEKVSLSSA VFENPKIITQ
     LAERVGRQSI VVCLDVKKRL FGSKFDCFTI NGTKKQSVDT IEFVKQIQTL GAGEIVLNFI
     DNDGVMKGYD LDAVSKFKAL VKVPLTVVGG AGCVDDIAKL VQQEKLVGAA AGSLFVFKGK
     YKAVLINYPS PSEKKKALEL