ID   HIS7_XANC8              Reviewed;         375 AA.
AC   Q4UU42;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=XC_2378;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L.,
RA   Zeng S., Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B.,
RA   Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000050; AAY49431.1; -; Genomic_DNA.
DR   RefSeq; YP_243451.1; -.
DR   GeneID; 3380915; -.
DR   GenomeReviews; CP000050_GR; XC_2378.
DR   KEGG; xcb:XC_2378; -.
DR   HOGENOM; Q4UU42; -.
DR   OMA; Q4UU42; MVSNQDG.
DR   BioCyc; XCAM314565:XC_2378-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_1000063451.
FT   REGION        1    168       Histidinol-phosphatase.
FT   REGION      169    375       Imidazoleglycerol-phosphate dehydratase.
SQ   SEQUENCE   375 AA;  41812 MW;  758A9F43F0F5AF72 CRC64;
     MTPILFVDRD GTLITEPADF QIDAYEKLRF VDGVIPAMLK LRDAGYQFVI VSNQDGLGSE
     SYPQASFDGP NNLMLQIFAS QGIVFREVLI DCSWPADNAP TRKPGVGLMV PYLQDRTIDW
     SRSAMVGDRI TDIQFAQNLN IRGFQLRTEQ FGGDWDWAGI AHELADAPRR AVVQRNTKET
     RIRVELDLDR VAEPHTATGL PFFDHMLEQI GKHGGFALDI RAEGDLHIDE HHTIEDTGLA
     LGQALREALG DKRGIGRYGF DPDDSPWRVA GDTTQHGFTL PMDETIASAA LDFSGRPYFV
     FDGDFKRERV GDMPTELVPH FFRSVCDASG LNLHLHVRGE NDHHKVEGCF KALARALRQA
     IRREGTALPS TKGAL
//