(data stored in ACNUC10821 zone)

SWISSPROT: HIS6_LISMF

ID   HIS6_LISMF              Reviewed;         251 AA.
AC   Q722Y7;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAY-2019, 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};
GN   OrderedLocusNames=LMOf2365_0592;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
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; AE017262; AAT03374.1; -; Genomic_DNA.
DR   RefSeq; WP_003725465.1; NC_002973.6.
DR   SMR; Q722Y7; -.
DR   EnsemblBacteria; AAT03374; AAT03374; LMOf2365_0592.
DR   KEGG; lmf:LMOf2365_0592; -.
DR   HOGENOM; HOG000224612; -.
DR   KO; K02500; -.
DR   OMA; KRIVPCL; -.
DR   BioCyc; LMON265669:G1G0V-607-MONOMER; -.
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;
DR   PRODOM; Q722Y7.
DR   SWISS-2DPAGE; Q722Y7.
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Lyase.
FT   CHAIN         1    251       Imidazole glycerol phosphate synthase
FT                                subunit HisF.
FT                                /FTId=PRO_0000142179.
FT   ACT_SITE     11     11       {ECO:0000255|HAMAP-Rule:MF_01013}.
FT   ACT_SITE    130    130       {ECO:0000255|HAMAP-Rule:MF_01013}.
SQ   SEQUENCE   251 AA;  26446 MW;  BC43C8370B39C279 CRC64;
     MLTKRIIPCL DVTAGRVVKG VNFVSLTDVG DPVEIAKAYN EAGADELVFL DITATVELRQ
     TMIDVVERTA EQVFIPLTVG GGISSVSDMK ELLQAGADKI SLNSAAIKRP ELIQEGAAKF
     GNQCIVVAID AKWNGTNWSV FTRGGRNDTG LDAIEWAKKA VQLGAGEILL TSMDGDGTKN
     GYDIPLTKAI SAAVSVPVIA SGGCGNAAHM AEVFEKTKAT AALAASIFHY GELSIKNVKT
     TLLEKGVNIR P
//

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