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Database: UniProt
Entry: B0RSL6
LinkDB: B0RSL6
Original site: B0RSL6 
ID   HIS7_XANCB              Reviewed;         375 AA.
AC   B0RSL6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   29-OCT-2014, entry version 52.
DE   RecName: Full=Histidine biosynthesis bifunctional protein HisB {ECO:0000255|HAMAP-Rule:MF_01022};
DE   Includes:
DE     RecName: Full=Histidinol-phosphatase {ECO:0000255|HAMAP-Rule:MF_01022};
DE              EC=3.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01022};
DE   Includes:
DE     RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_01022};
DE              Short=IGPD {ECO:0000255|HAMAP-Rule:MF_01022};
DE              EC=4.2.1.19 {ECO:0000255|HAMAP-Rule:MF_01022};
GN   Name=hisB {ECO:0000255|HAMAP-Rule:MF_01022};
GN   OrderedLocusNames=xcc-b100_2098;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J.,
RA   Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A.,
RA   Niehaus K., Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use
RT   for the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
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_01022}.
CC   -!- CATALYTIC ACTIVITY: L-histidinol phosphate + H(2)O = L-histidinol
CC       + phosphate. {ECO:0000255|HAMAP-Rule:MF_01022}.
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_01022}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the histidinol-
CC       phosphatase family. {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       imidazoleglycerol-phosphate dehydratase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01022}.
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DR   EMBL; AM920689; CAP51451.1; -; Genomic_DNA.
DR   RefSeq; YP_001903503.1; NC_010688.1.
DR   ProteinModelPortal; B0RSL6; -.
DR   STRING; 509169.xccb100_2098; -.
DR   EnsemblBacteria; CAP51451; CAP51451; xcc-b100_2098.
DR   GeneID; 6324662; -.
DR   KEGG; xca:xccb100_2098; -.
DR   PATRIC; 24084091; VBIXanCam108527_2134.
DR   eggNOG; COG0131; -.
DR   KO; K01089; -.
DR   OMA; GTDSFPQ; -.
DR   OrthoDB; EOG60PHGP; -.
DR   BioCyc; XCAM509169:GHW4-2143-MONOMER; -.
DR   UniPathway; UPA00031; UER00011.
DR   UniPathway; UPA00031; UER00013.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   HAMAP; MF_00076; HisB; 1.
DR   HAMAP; MF_01022; Bifunc_HisB; 1.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR020566; His_synth_bifunc_HisB.
DR   InterPro; IPR005954; HisB_N.
DR   InterPro; IPR006543; Histidinol-phos.
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   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR   TIGRFAMs; TIGR01261; hisB_Nterm; 1.
DR   TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
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; Hydrolase; Lyase; Multifunctional enzyme.
FT   CHAIN         1    375       Histidine biosynthesis bifunctional
FT                                protein HisB.
FT                                /FTId=PRO_1000135372.
FT   REGION        1    168       Histidinol-phosphatase.
FT   REGION      169    375       Imidazoleglycerol-phosphate dehydratase.
SQ   SEQUENCE   375 AA;  41780 MW;  AC9A9B064F19B5EB CRC64;
     MTPILFVDRD GTLITEPADF QIDAYEKLRF VEGVIPAMLK LRDAGYQFVI VSNQDGLGSE
     SYPQASFDGP NNLMLQIFAS QGIVFREVLI DCSWPADNAP TRKPGVGLMV PYLQDRTIDW
     SRSAMVGDRI TDIQFAQNLN IRGFQLRTEQ FGGDWDWAGI AHELADAPRR AVVQRNTKET
     RIRVELDLDR VAEPHTATGL PFFDHMLEQI GKHGGFALDI RAEGDLHIDE HHTIEDTGLA
     LGQALREALG DKRGIGRYGF DPVDSPWRVA GDTAQHGFTL PMDETIASAA LDFSGRPYFV
     FDGDFKRERV GDMPTELVPH FFRSVCDASG LNLHLHVRGE NDHHKVEGCF KALARALRQA
     IRREGTALPS TKGAL
//
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