ID   HIS7_XANOM              Reviewed;         375 AA.
AC   Q2P3K1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=XOO2121;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests
RT   contribution of large numbers of effector genes and insertion
RT   sequences to its race diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
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; AP008229; BAE68876.1; -; Genomic_DNA.
DR   RefSeq; YP_451150.1; -.
DR   GeneID; 3857258; -.
DR   GenomeReviews; AP008229_GR; XOO2121.
DR   KEGG; xom:XOO_2121; -.
DR   HOGENOM; Q2P3K1; -.
DR   OMA; Q2P3K1; MVSNQDG.
DR   BioCyc; XORY342109:XOO2121-MON; -.
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 act...; IEA:HAMAP.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01022; -; 1.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR005954; HisB_N.
DR   InterPro; IPR006543; Histidinol-phos.
DR   InterPro; IPR000807; Imidazole_glycer-P_deHydtase.
DR   InterPro; IPR013954; PNK3P_central-region.
DR   PANTHER; PTHR23133:SF2; Imidazole-GPD; 1.
DR   Pfam; PF00475; IGPD; 1.
DR   Pfam; PF08645; PNK3P; 1.
DR   ProDom; PD002282; IGPD; 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_1000063452.
FT   REGION        1    168       Histidinol-phosphatase.
FT   REGION      169    375       Imidazoleglycerol-phosphate dehydratase.
SQ   SEQUENCE   375 AA;  41887 MW;  9D784B4B6573ADE9 CRC64;
     MTPILFVDRD GTLITEPADY QIDAYEKLRF VDHVIPAMLK LRDAGYQFVI VSNQDGLGSE
     SFPRASFDGP NNLMLQIFAS QGIEFREVLI DCSWPSDNAP TRKPGVGLMV PYLQDRTIDW
     ARSAMVGDRI TDIQFAQNLN IRGFQLRTDE FGGEWDWPGI AHELADAPRR AVVQRNTKET
     RIRVELDLDR VAEPKTATGL PFFDHMLEQI GKHGGFALDI RAEGDLHIDE HHTIEDTGLA
     LGQALREALG DKRGIGRYGF DPESSPWQVA GDTAQHGFTL PMDETIASAA LDFSGRPYFV
     FDGQFKRDRL GDMPTELVPH FFRSICDASG VNLHLTVRGE NDHHKVEACF KALARALRQA
     IRREGSALPT TKGAL
//