ID   HIS7_BAUCH              Reviewed;         356 AA.
AC   Q1LT69;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, 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=BCI_0402;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(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; CP000238; ABF13797.1; -; Genomic_DNA.
DR   RefSeq; YP_588845.1; -.
DR   GeneID; 4056379; -.
DR   GenomeReviews; CP000238_GR; BCI_0402.
DR   KEGG; bci:BCI_0402; -.
DR   HOGENOM; Q1LT69; -.
DR   OMA; Q1LT69; MVSNQDG.
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   PANTHER; PTHR23133:SF2; Imidazole-GPD; 1.
DR   Pfam; PF00475; IGPD; 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    356       Histidine biosynthesis bifunctional
FT                                protein hisB.
FT                                /FTId=PRO_1000063441.
FT   REGION        1    166       Histidinol-phosphatase.
FT   REGION      167    356       Imidazoleglycerol-phosphate dehydratase.
SQ   SEQUENCE   356 AA;  40624 MW;  3D2AF3DAD6D75C53 CRC64;
     MSKKVLFIDR DGTLINEPLD NFQIDRIEKL VLEPYVINAL LILQQANFQL VMVSNQDGLG
     TSSFPQEDFD RPHNLMMQIF KSQNIFFDQV LICPHLAKDK CHCRKPGIAL VAPWLVGNKI
     DRTKSYVIGD RETDIKLAYN MGINSLRYNR NTMNWQAICN YLTSLNRYAH VKRITKETSI
     NVEVWLDREA PSKINTGINF FDHMLEQIAT HSGLCMTIEV KGDLYIDDHH TIEDTAIALG
     TALKQGLGDK HGINRFGFLL PMDECLARCV IDLSGRPFLE YTAEYSYQKV GDMSTEMVEH
     FFRSLSYAMA CTLYLKTEGK NDHHRVESLF KVFGRALRQA ICVESNVLPS SKGVLS
//