ID   HIS6_LEPBO              Reviewed;         254 AA.
AC   Q9ZGM0;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Putative imidazole glycerol phosphate synthase subunit HisF;
DE            EC=4.3.2.10;
DE   AltName: Full=IGP synthase cyclase subunit;
DE   AltName: Full=IGP synthase subunit HisF;
DE   AltName: Full=ImGP synthase subunit HisF;
DE            Short=IGPS subunit HisF;
GN   Name=hisF;
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 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 11 is
CC       replaced by a Leu. {ECO:0000305}.
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DR   EMBL; AF078135; AAD12949.1; -; Genomic_DNA.
DR   RefSeq; WP_011669953.1; NZ_VCHK01000056.1.
DR   AlphaFoldDB; Q9ZGM0; -.
DR   SMR; Q9ZGM0; -.
DR   OMA; PKYVGDP; -.
DR   UniPathway; UPA00031; UER00010.
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.
FT   CHAIN           1..254
FT                   /note="Putative imidazole glycerol phosphate synthase
FT                   subunit HisF"
FT                   /id="PRO_0000142173"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   254 AA;  27963 MW;  A842AEC1D4512DEB CRC64;
     MLRPRIIPVL LLQENGLVKT IQFGDERYIG DPLNAVRIFN EKEADELAVL DISASKKGKE
     PNYRLIERLA NECRMPLCYG GGIKDLDQAN RILSFGVEKI IVSSLAIENP KMISTMASYL
     GSQSVVVAID FKKAMLSRRY EVMIHNGTKK TGKHLEDLVK EVIELGAGEI ILNSIDRDGT
     MVGYEIEIIK KIQSICKIPI TVLGGAGSLD HIKNLIQELG IIGVAAGSLF VYKGVHKAVL
     INYPNGTDKE ALFP