ID   HIS6_HALHL              Reviewed;         254 AA.
AC   A1WW05;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Hhal_1091;
OS   Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS   halophila (strain DSM 244 / SL1)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=349124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA   Richardson P.;
RT   "Complete sequence of Halorhodospira halophila SL1.";
RL   Submitted (DEC-2006) 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; CP000544; ABM61867.1; -; Genomic_DNA.
DR   RefSeq; WP_011813890.1; NC_008789.1.
DR   AlphaFoldDB; A1WW05; -.
DR   SMR; A1WW05; -.
DR   STRING; 349124.Hhal_1091; -.
DR   EnsemblBacteria; ABM61867; ABM61867; Hhal_1091.
DR   KEGG; hha:Hhal_1091; -.
DR   eggNOG; COG0107; Bacteria.
DR   HOGENOM; CLU_048577_4_0_6; -.
DR   OMA; IMPCLDM; -.
DR   OrthoDB; 1522718at2; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000000647; Chromosome.
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;
KW   Reference proteome.
FT   CHAIN           1..254
FT                   /note="Imidazole glycerol phosphate synthase subunit HisF"
FT                   /id="PRO_1000063068"
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   254 AA;  27021 MW;  F16A1C5E2704AF25 CRC64;
     MTAKRIIPCL DVDAGRVVKG VRFVDIRDAG DPVEIARRYD AMGADELTFL DITASHEERE
     TIYDVVEAVA GQVFIPLTVG GGVRSVADVR RLLNAGADKV AINTAAVHRP DFVREAAERF
     GSQCIVVAVD AKQVEDDPPR WEVFTHGGRN PTGLEVVSWC QRLVALGAGE ILLTSMDRDG
     TRAGFDLGLT RAVADAVSVP VIASGGVGEL EHLADGVDDG GADAVLAASI FHFGDHTVGE
     AKAHMAERGI EVRR