ID   HIS6_CHLCH              Reviewed;         251 AA.
AC   Q3ATG0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Imidazole glycerol phosphate synthase subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
DE            EC=4.3.2.10 {ECO:0000255|HAMAP-Rule:MF_01013};
DE   AltName: Full=IGP synthase cyclase subunit {ECO:0000255|HAMAP-Rule:MF_01013};
DE   AltName: Full=IGP synthase subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
DE   AltName: Full=ImGP synthase subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
DE            Short=IGPS subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
GN   Name=hisF {ECO:0000255|HAMAP-Rule:MF_01013}; OrderedLocusNames=Cag_0442;
OS   Chlorobium chlorochromatii (strain CaD3).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=340177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CaD3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_01013}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01013};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01013}.
CC   -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000255|HAMAP-
CC       Rule:MF_01013}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01013}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000255|HAMAP-
CC       Rule:MF_01013}.
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DR   EMBL; CP000108; ABB27715.1; -; Genomic_DNA.
DR   RefSeq; WP_011361488.1; NC_007514.1.
DR   AlphaFoldDB; Q3ATG0; -.
DR   SMR; Q3ATG0; -.
DR   STRING; 340177.Cag_0442; -.
DR   EnsemblBacteria; ABB27715; ABB27715; Cag_0442.
DR   KEGG; cch:Cag_0442; -.
DR   eggNOG; COG0107; Bacteria.
DR   HOGENOM; CLU_048577_4_0_10; -.
DR   OMA; IFHYKET; -.
DR   OrthoDB; 1522718at2; -.
DR   UniPathway; UPA00031; UER00010.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04731; HisF; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01013; HisF; 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.
DR   TIGRFAMs; TIGR00735; hisF; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Lyase.
FT   CHAIN           1..251
FT                   /note="Imidazole glycerol phosphate synthase subunit HisF"
FT                   /id="PRO_0000230126"
FT   ACT_SITE        11
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01013"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01013"
SQ   SEQUENCE   251 AA;  27666 MW;  47DFDAC690FE376D CRC64;
     MLAKRIIPCL DVRDGRVVKG INFEGLRDAG SILEQARFYN NELADELVFL DISASLESRR
     TTLEEVMKVS EEVFIPLTVG GGISSVERAR EVFLHGADKV SVNTAAVNDP YLISRIAEKY
     GSQAVVVAID IKKVGNHYMV HTHSGKQITQ YEALEWALKV QELGAGEILL TSMDRDGTKE
     GYENNSLRMI STAVHIPVIA SGGAGNLEHL YDGFSKGCAD AALAASIFHF RHYSIRQAKE
     YLHKRGVAVR F