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-MAY-2013, entry version 45.
DE RecName: Full=Histidine biosynthesis bifunctional protein HisB;
DE Includes:
DE RecName: Full=Histidinol-phosphatase;
DE EC=3.1.3.15;
DE Includes:
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase;
DE Short=IGPD;
DE EC=4.2.1.19;
GN Name=hisB; 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 -!- CATALYTIC ACTIVITY: L-histidinol phosphate + H(2)O = L-histidinol
CC + phosphate.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: In the N-terminal section; belongs to the histidinol-
CC phosphatase family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC imidazoleglycerol-phosphate dehydratase family.
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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; EMVPHFF; -.
DR ProtClustDB; PRK05446; -.
DR BioCyc; XCAM509169:GHW4-2143-MONOMER; -.
DR UniPathway; UPA00031; UER00011.
DR UniPathway; UPA00031; UER00013.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004401; F:histidinol-phosphatase activity; IEA:HAMAP.
DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:HAMAP.
DR GO; GO:0016311; P:dephosphorylation; IEA:GOC.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.50.1000; -; 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; SSF56784; HAD-like_dom; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 2.
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
//
