ID   HIS6_LEPIR              Reviewed;         254 AA.
AC   Q9S4H7;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 72.
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 interrogans.
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=173;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Hardjoprajitno / Serogroup Sejroe / Serovar hardjo;
RX   PubMed=10474199; DOI=10.1111/j.1574-6968.1999.tb13749.x;
RA   De la Pena-Moctezuma A., Bulach D.M., Kalambaheti T., Adler B.;
RT   "Comparative analysis of the LPS biosynthetic loci of the genetic subtypes
RT   of serovar Hardjo: Leptospira interrogans subtype Hardjoprajitno and
RT   Leptospira borgpetersenii subtype Hardjobovis.";
RL   FEMS Microbiol. Lett. 177:319-326(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; AF144879; AAD52165.1; -; Genomic_DNA.
DR   RefSeq; WP_025177747.1; NZ_JQQK01000061.1.
DR   AlphaFoldDB; Q9S4H7; -.
DR   SMR; Q9S4H7; -.
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_0000142175"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   254 AA;  28087 MW;  5447C803CFFDDAF5 CRC64;
     MLKPRIIPTL LVQHGGLVKT IKFSNQRYIG DPLNAVRIFN EKEADELTVL DISASREGKA
     PDYRLIERLA NECRMPLSYG GGIKNLEQAS RILSFGVEKI IVSSLAIENP KVISSMATYL
     GNQSVVVAID FKKTLLTRRY EVFIHNGTKK TGISPEDLLK HAIEFGAGEI LLNSIDRDGV
     MEGYDLEMLK KFRSICTVPM TVLGGAGSLQ DLKSLIQNLG IVGVSAGSLF VYKGIHKAVL
     INYPNREDKE ALFY