(data stored in ACNUC7421 zone)

SWISSPROT: HIS7_RHOPS

ID   HIS7_RHOPS              Reviewed;         197 AA.
AC   Q13E36;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_00076};
DE            Short=IGPD {ECO:0000255|HAMAP-Rule:MF_00076};
DE            EC=4.2.1.19 {ECO:0000255|HAMAP-Rule:MF_00076};
GN   Name=hisB {ECO:0000255|HAMAP-Rule:MF_00076};
GN   OrderedLocusNames=RPD_0415;
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-
CC         (imidazol-4-yl)-2-oxopropyl phosphate + H2O;
CC         Xref=Rhea:RHEA:11040, ChEBI:CHEBI:15377, ChEBI:CHEBI:57766,
CC         ChEBI:CHEBI:58278; EC=4.2.1.19; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00076};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC       {ECO:0000255|HAMAP-Rule:MF_00076}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00076}.
CC   -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00076}.
DR   EMBL; CP000283; ABE37653.1; -; Genomic_DNA.
DR   RefSeq; WP_011500841.1; NC_007958.1.
DR   SMR; Q13E36; -.
DR   STRING; 316057.RPD_0415; -.
DR   EnsemblBacteria; ABE37653; ABE37653; RPD_0415.
DR   KEGG; rpd:RPD_0415; -.
DR   eggNOG; ENOG4105ECC; Bacteria.
DR   eggNOG; COG0131; LUCA.
DR   HOGENOM; HOG000228064; -.
DR   KO; K01693; -.
DR   OMA; ARHGLFD; -.
DR   OrthoDB; 1278103at2; -.
DR   BioCyc; RPAL316057:RPD_RS02135-MONOMER; -.
DR   UniPathway; UPA00031; UER00011.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07914; IGPD; 1.
DR   Gene3D; 3.30.230.40; -; 2.
DR   HAMAP; MF_00076; HisB; 1.
DR   InterPro; IPR038494; IGPD_sf.
DR   InterPro; IPR000807; ImidazoleglycerolP_deHydtase.
DR   InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR23133; PTHR23133; 1.
DR   Pfam; PF00475; IGPD; 1.
DR   SUPFAM; SSF54211; SSF54211; 2.
DR   PROSITE; PS00954; IGP_DEHYDRATASE_1; 1.
DR   PROSITE; PS00955; IGP_DEHYDRATASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13E36.
DR   SWISS-2DPAGE; Q13E36.
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Lyase.
FT   CHAIN         1    197       Imidazoleglycerol-phosphate dehydratase.
FT                                /FTId=PRO_1000010344.
SQ   SEQUENCE   197 AA;  21335 MW;  5988E8C97D459C5C CRC64;
     MRTATIKRKT KETDIEVTVN LDGAGVSNAA TGIGFFDHML DLLAKHSRID ITVKAVGDLH
     VDFHHTTEDV GIALGQAVKQ ALGNMAGINR YASMLMPMDE TLTRVVIDVS GRPFLVFKAD
     FPRDKIGEFD TELVREWFQA FAMNAGVTLH VETLYGENSH HIAESCFKGL ARALRAAVAI
     DPQAAGEVPS TKGQLGG
//

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