ID   HIS6_LEGPN              Reviewed;         212 AA.
AC   Q9RDX2;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=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   Legionella pneumophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=446;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43109 / NCTC 12008 / RC1 / Olda / Serogroup 1;
RX   PubMed=11043980; DOI=10.1016/s1438-4221(00)80104-6;
RA   Lueneberg E., Zetzmann N., Hartmann M., Knirel Y.A., Kooistra O.,
RA   Zaehringer U., Helbig J., Frosch M.;
RT   "Cloning and functional characterization of a 30 kb gene locus required for
RT   lipopolysaccharide biosynthesis in Legionella pneumophila.";
RL   Int. J. Med. Microbiol. 290:37-49(2000).
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}.
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DR   EMBL; AJ007311; CAB65215.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RDX2; -.
DR   SMR; Q9RDX2; -.
DR   STRING; 91892.BIZ52_04065; -.
DR   eggNOG; COG0107; Bacteria.
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..212
FT                   /note="Imidazole glycerol phosphate synthase subunit HisF"
FT                   /id="PRO_0000142171"
FT   ACT_SITE        11
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   212 AA;  23019 MW;  42BF6E7BE523AEFE CRC64;
     MSNVRLIARL DIKGPNLIKG VHLEGLRVVG NPNEYAMAYY AQGADELIYM DTVASLYGRN
     NLSEIVKTTA ENVFIPITVG GGIRSVDDAE QLLRCGADKV AINTAATKNP TLISDIARRF
     GSQCVVLSIE AKRTVNGRWE VMTDNGREHT GMDVVDWARN GEKFGAGEIL LTSIDQEGTR
     KGFDLELVKQ VSSMVSIPVI ASGGMGKLEE FN