ID   HIS7_COLP3              Reviewed;         361 AA.
AC   Q47XB6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-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=CPS_3892;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(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; CP000083; AAZ28659.1; -; Genomic_DNA.
DR   RefSeq; YP_270554.1; -.
DR   GeneID; 3522920; -.
DR   GenomeReviews; CP000083_GR; CPS_3892.
DR   KEGG; cps:CPS_3892; -.
DR   NMPDR; fig|167879.3.peg.3532; -.
DR   TIGR; CPS_3892; -.
DR   HOGENOM; Q47XB6; -.
DR   OMA; Q47XB6; MVSNQDG.
DR   BioCyc; CPSY167879:CPS_3892-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; FALSE_NEG.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Hydrolase; Lyase; Multifunctional enzyme.
FT   CHAIN         1    361       Histidine biosynthesis bifunctional
FT                                protein hisB.
FT                                /FTId=PRO_0000319738.
FT   REGION        1    172       Histidinol-phosphatase.
FT   REGION      173    361       Imidazoleglycerol-phosphate dehydratase.
SQ   SEQUENCE   361 AA;  39901 MW;  0DAD638A63B8A9F1 CRC64;
     MSNTQEKILF IDRDGTLVEE PAIDKQLDTL EKLVFEPNVI AELLKLQAKG FKLVMVSNQD
     GLGTNSFPQA DFDLPHNKMM DLFSSQGVHF QDVLLCPHFD EDNCNCRKPK LGLVSEYLQQ
     GRVDFANSFV IGDRETDMGL AANMGIVGIK YDPETLNWAQ VSEQIITQLE QPRIATVTRT
     TKETDITVTV NLDKAGESSI DTGLGFFDHM LDQISTHGGF SLQCHVSGDY HIDEHHSVED
     TALALGQALK QALGNKRGIN RFGFTIPMDE CRAECAIDLS GRPWLEFDAD FTSANVGTMS
     TQMVPHFFRS LADSMLITLH LSTSKGNCHH QVESLFKVFG RALGQAIKVD GDAMPSSKGT
     L
//