ID   HIS6_METS5              Reviewed;         251 AA.
AC   A4YI34;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=Msed_1946;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
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; CP000682; ABP96086.1; -; Genomic_DNA.
DR   RefSeq; WP_012021873.1; NC_009440.1.
DR   AlphaFoldDB; A4YI34; -.
DR   SMR; A4YI34; -.
DR   STRING; 399549.Msed_1946; -.
DR   EnsemblBacteria; ABP96086; ABP96086; Msed_1946.
DR   GeneID; 5103333; -.
DR   GeneID; 59456920; -.
DR   KEGG; mse:Msed_1946; -.
DR   eggNOG; arCOG00617; Archaea.
DR   HOGENOM; CLU_048577_4_0_2; -.
DR   OMA; IFHYKET; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000000242; 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..251
FT                   /note="Imidazole glycerol phosphate synthase subunit HisF"
FT                   /id="PRO_1000072925"
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;  26810 MW;  CD619B5B81182DEF CRC64;
     MTTRRIIACL DVKDGKVVKG VRFLDLKLKG DPAELASRYE EEGADEIVFL DISATVEGRK
     TLLEKVRETA SVLSIPLTVG GGVRTVEDVS NLLSNGADKV SLNTVAAENP SVVSMASREF
     GAQAVVVAID AKRVGNGWRV FVRSGTKDTG LDAVDWAKRV EEMGAGEILL TSIDRDGTRD
     GYDLELTKAV VRATKVPVIA SGGAGKPDHF LSVFRQAGAD AALAAGIFHD GVIRIRELKD
     YLKDAGIEVR T