(data stored in ACNUC7421 zone)

SWISSPROT: HIS6_RHOPS

ID   HIS6_RHOPS              Reviewed;         255 AA.
AC   Q13E40;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 74.
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};
GN   OrderedLocusNames=RPD_0411;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
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.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to
CC       IGP, AICAR and glutamate. The HisF subunit catalyzes the
CC       cyclization activity that produces IGP and AICAR from PRFAR using
CC       the ammonia provided by the HisH subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01013}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-
CC         (5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine
CC         = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide +
CC         D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-
CC         glutamate; Xref=Rhea:RHEA:24793, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58278, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:58475, ChEBI:CHEBI:58525; EC=4.3.2.10;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01013};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine 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}.
DR   EMBL; CP000283; ABE37649.1; -; Genomic_DNA.
DR   RefSeq; WP_011500837.1; NC_007958.1.
DR   SMR; Q13E40; -.
DR   STRING; 316057.RPD_0411; -.
DR   EnsemblBacteria; ABE37649; ABE37649; RPD_0411.
DR   KEGG; rpd:RPD_0411; -.
DR   eggNOG; ENOG4105C0S; Bacteria.
DR   eggNOG; COG0107; LUCA.
DR   HOGENOM; HOG000224612; -.
DR   KO; K02500; -.
DR   OMA; KRIVPCL; -.
DR   OrthoDB; 1522718at2; -.
DR   BioCyc; RPAL316057:RPD_RS02115-MONOMER; -.
DR   UniPathway; UPA00031; UER00010.
DR   Proteomes; UP000001818; 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;
DR   PRODOM; Q13E40.
DR   SWISS-2DPAGE; Q13E40.
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Lyase.
FT   CHAIN         1    255       Imidazole glycerol phosphate synthase
FT                                subunit HisF.
FT                                /FTId=PRO_1000063131.
FT   ACT_SITE     11     11       {ECO:0000255|HAMAP-Rule:MF_01013}.
FT   ACT_SITE    130    130       {ECO:0000255|HAMAP-Rule:MF_01013}.
SQ   SEQUENCE   255 AA;  27358 MW;  A76AEECE6F9AD66A CRC64;
     MFKVRVIPCL DVKDGRVVKG VNFVDLRDAG DPVEAAIAYD AAGADELCFL DITATHENRG
     IMLDVVRRTA EACFMPVTVG GGVRTVDDIK TLLRSGADKV SINSAAVARR EFVKEAAEKF
     GDQCIVVAID AKRVPGRDRW EIFTHGGRKG TGIDAIEFAQ EVVSLGAGEI LLTSMDRDGT
     RSGFDIPLTR AIADSVQVPV IASGGVGDLD HLVDGIREGH ATAVLAASIF HFGEYTIREA
     KDHMVRAGLP MRLDP
//

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