ID   HIS7_SODGM              Reviewed;         355 AA.
AC   Q2NTX3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=SG1127;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K.,
RA   Hattori M., Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights
RT   into the symbiotic lifestyle of Sodalis glossinidius in the tsetse
RT   host.";
RL   Genome Res. 16:149-156(2006).
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; AP008232; BAE74402.1; -; Genomic_DNA.
DR   RefSeq; YP_454807.1; -.
DR   SMR; Q2NTX3; 3-164.
DR   GeneID; 3867555; -.
DR   GenomeReviews; AP008232_GR; SG1127.
DR   KEGG; sgl:SG1127; -.
DR   NMPDR; fig|343509.6.peg.2310; -.
DR   HOGENOM; Q2NTX3; -.
DR   OMA; Q2NTX3; MVSNQDG.
DR   BioCyc; SGLO343509:SG1127-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    355       Histidine biosynthesis bifunctional
FT                                protein hisB.
FT                                /FTId=PRO_1000063449.
FT   REGION        1    166       Histidinol-phosphatase.
FT   REGION      167    355       Imidazoleglycerol-phosphate dehydratase.
SQ   SEQUENCE   355 AA;  39469 MW;  0BDC33A77F10CC7E CRC64;
     MNQKVLFIDR DGTLINEPPA DFQVDRMDKL ALEPGVIPVL LALQKAGFRL VMITNQDGLG
     TTSFPQADFD GPHDLMMAIF TSQGIVFDEV LICPHLPTDG CACRKPQTGI VTPWLKEHAL
     DSAHSYVIGD RETDMALAAN MGITGLRYQR ASLNWPAIGE QLTRSDRHAR VNRVTRETAI
     DVEVWLDREG DSRINTGIGF FDHMLDQIAT HGGLRINIAV KGDLHIDDHH TVEDTALALG
     EALNKALGDK RGIGRFGFVL PMDECLARCA LDISGRPHLE YKAKYSFQRV GDLSTEMVEH
     FFRSLSYAMA CTLHLRTKGK NDHHRVESLF KAFGRTLRQA IRVEGDTLPS SKGVL
//