HIS6_RHOPB
ID HIS6_RHOPB Reviewed; 258 AA.
AC Q21CK1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=RPC_0310;
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-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; CP000301; ABD85885.1; -; Genomic_DNA.
DR RefSeq; WP_011470793.1; NC_007925.1.
DR AlphaFoldDB; Q21CK1; -.
DR SMR; Q21CK1; -.
DR STRING; 316056.RPC_0310; -.
DR EnsemblBacteria; ABD85885; ABD85885; RPC_0310.
DR KEGG; rpc:RPC_0310; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_5; -.
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..258
FT /note="Imidazole glycerol phosphate synthase subunit HisF"
FT /id="PRO_1000063130"
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 258 AA; 27584 MW; 99ACA380AB0D1C6F CRC64;
MFKVRVIPCL DVKDGRVVKG INFVDLRDAG DPVEAAIAYD AAGADELCFL DITATHENRG
IMLDVVRRTA EACFMPLTVG GGVRTVDDIK VLLRSGADKV SINSAAVSRR EFVKEAAEKF
GDQCIVVAID AKRVKRGGGG ERWEIFTHGG RNSTGIDAIE YAQEVVSLGA GEILLTSMDR
DGTRQGFDIP LTSAIADSVH VPVIASGGVG TLDHLVDGIR NGHATAVLAA SIFHFGEFTI
RQAKDHMVRA GLPMRLDP