GenomeNet

Database: UniProt
Entry: Q46WL4
LinkDB: Q46WL4
Original site: Q46WL4 
ID   HIS7_CUPNJ              Reviewed;         195 AA.
AC   Q46WL4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   28-MAR-2018, entry version 81.
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=Reut_A3109;
OS   Cupriavidus necator (strain JMP 134 / LMG 1197) (Ralstonia eutropha
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator
RT   JMP134, a versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
CC   -!- CATALYTIC ACTIVITY: D-erythro-1-(imidazol-4-yl)glycerol 3-
CC       phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H(2)O.
CC       {ECO:0000255|HAMAP-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; CP000090; AAZ62469.1; -; Genomic_DNA.
DR   RefSeq; WP_011299252.1; NC_007347.1.
DR   ProteinModelPortal; Q46WL4; -.
DR   SMR; Q46WL4; -.
DR   STRING; 264198.Reut_A3109; -.
DR   EnsemblBacteria; AAZ62469; AAZ62469; Reut_A3109.
DR   KEGG; reu:Reut_A3109; -.
DR   eggNOG; ENOG4105ECC; Bacteria.
DR   eggNOG; COG0131; LUCA.
DR   HOGENOM; HOG000228064; -.
DR   KO; K01693; -.
DR   OMA; ARHGLFD; -.
DR   OrthoDB; POG091H060Z; -.
DR   UniPathway; UPA00031; UER00011.
DR   Proteomes; UP000002697; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
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;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Lyase; Reference proteome.
FT   CHAIN         1    195       Imidazoleglycerol-phosphate dehydratase.
FT                                /FTId=PRO_1000010339.
SQ   SEQUENCE   195 AA;  21487 MW;  616657E3738C5923 CRC64;
     MRVAEVTRNT SETQIRVSLN LDGTGRQKLA SGVPFLDHML DQIARHGMFD LEVEATGDTH
     IDDHHTVEDV GITLGQAVAK AIGDKKGITR YGHSYVPLDE CLSRVVIDFS GRPGLEFHVP
     FTRARVGSFD VDLTIEFFRG FVNHAGVTLH IDNLRGINAH HQCETVFKAF GRALRMAVEL
     DPRAANTIPS TKGTL
//
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