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Database: UniProt
Entry: A6WX56
LinkDB: A6WX56
Original site: A6WX56 
ID   HIS7_OCHA4              Reviewed;         202 AA.
AC   A6WX56;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   29-OCT-2014, entry version 46.
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=Oant_0838;
OS   Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Ochrobactrum.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / NCTC 12168;
RX   PubMed=21685287; DOI=10.1128/JB.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M.,
RA   Shin M., Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile
RT   opportunistic pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(2011).
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}.
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DR   EMBL; CP000758; ABS13560.1; -; Genomic_DNA.
DR   RefSeq; YP_001369389.1; NC_009667.1.
DR   ProteinModelPortal; A6WX56; -.
DR   STRING; 439375.Oant_0838; -.
DR   EnsemblBacteria; ABS13560; ABS13560; Oant_0838.
DR   GeneID; 5379323; -.
DR   KEGG; oan:Oant_0838; -.
DR   PATRIC; 20466719; VBIOchAnt73124_0883.
DR   eggNOG; COG0131; -.
DR   HOGENOM; HOG000228064; -.
DR   KO; K01693; -.
DR   OMA; HHIAESC; -.
DR   OrthoDB; EOG60PHGP; -.
DR   BioCyc; OANT439375:GJIT-845-MONOMER; -.
DR   UniPathway; UPA00031; UER00011.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00076; HisB; 1.
DR   InterPro; IPR000807; ImidazoleglycerolP_deHydtase.
DR   InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR23133:SF2; PTHR23133:SF2; 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    202       Imidazoleglycerol-phosphate dehydratase.
FT                                /FTId=PRO_1000010317.
SQ   SEQUENCE   202 AA;  22047 MW;  60BEB112E8825EB9 CRC64;
     MTAESTRKAS IERSTKETSI AVSVDLDGVG KFDITTGVGF FDHMLEQLSR HSLIDMRVMA
     KGDLHIDDHH TVEDTGIALG QAIAKALGER RGIVRYASMD LAMDDTLTGA AVDVSGRAFL
     VWNVNFTTSK IGTFDTELVR EFFQAFAMNA GITLHINNHY GANNHHIAES IFKAVARVLR
     TALETDPRQK DAIPSTKGSL KG
//
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