ID   GMHB_BURMA     STANDARD;      PRT;   189 AA.
AC   Q9AI34; Q62HG5;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   07-MAR-2006, entry version 22.
DE   D,D-heptose 1,7-bisphosphate phosphatase (EC 3.1.3.-) (D-glycero-D-
DE   manno-heptose 1,7-bisphosphate phosphatase).
GN   Name=gmhB; Synonyms=wcbN; OrderedLocusNames=BMA2293;
OS   Burkholderia mallei (Pseudomonas mallei).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=13373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   MEDLINE=21267073; PubMed=11373120; DOI=10.1006/mpat.2000.0430;
RA   DeShazer D., Waag D.M., Fritz D.L., Woods D.E.;
RT   "Identification of a Burkholderia mallei polysaccharide gene cluster
RT   by subtractive hybridization and demonstration that the encoded
RT   capsule is an essential virulence determinant.";
RL   Microb. Pathog. 30:253-269(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M.,
RA   Daugherty S.C., Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F.,
RA   Madupu R., Mohammoud Y., Nelson W.C., Radune D., Romero C.M.,
RA   Sarria S., Selengut J., Shamblin C., Sullivan S.A., White O., Yu Y.,
RA   Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
RN   [3]
RP   BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE.
RX   MEDLINE=22095940; PubMed=12101286;
RA   Valvano M.A., Messner P., Kosma P.;
RT   "Novel pathways for biosynthesis of nucleotide-activated glycero-
RT   manno-heptose precursors of bacterial glycoproteins and cell surface
RT   polysaccharides.";
RL   Microbiology 148:1979-1989(2002).
CC   -!- FUNCTION: Converts the D-glycero-alpha-D-manno-heptose
CC       1,7-bisphosphate intermediate into D-glycero-alpha-D-manno-heptose
CC       1-phosphate by removing the phosphate group at the C-7 position
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: D-glycero-alpha-D-manno-heptose
CC       1,7-bisphosphate + H(2)O = D-glycero-alpha-D-manno-heptose
CC       1-phosphate + phosphate.
CC   -!- PATHWAY: Capsular polysaccharide (CPS) biosynthesis; GDP-D-
CC       glycero-alpha-D-manno-heptose biosynthesis; first step.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: This enzyme is insensitive to the anomeric
CC       configuration of the D-glycero-D-manno-heptose 1,7-bisphosphate
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the gmhB family.
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DR   EMBL; AF285636; AAK26470.1; -; Genomic_DNA.
DR   EMBL; CP000010; AAU49840.1; -; Genomic_DNA.
DR   GenomeReviews; CP000010_GR; BMA2293.
DR   TIGR; BMA2293; -.
DR   InterPro; IPR006549; HAD_SF-IIIA.
DR   InterPro; IPR006543; Histidinol-phos.
DR   InterPro; IPR004446; Hstdl_phs_rel.
DR   TIGRFAMs; TIGR00213; GmhB_yaeD; 1.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR   TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
KW   Bacterial capsule; Carbohydrate metabolism; Complete proteome;
KW   Hydrolase.
FT   CHAIN         1    189       D,D-heptose 1,7-bisphosphate phosphatase.
FT                                /FTId=PRO_0000209385.
SQ   SEQUENCE   189 AA;  20428 MW;  C176C93FCE0144B4 CRC64;
     MKNRALFLDR DGVINRDDGY VFEIEKFVFL DGIFELAGAA KALGYLSIVV TNQAGIGRGY
     YSEDDFFRLS DWMKGVFATE GAPIDGVYFC PTHPEHGIGR YKVESRFRKP NPGMILAAQH
     DFDLDLGASL LVGDKESDIQ AGSTAGVGTT LLICDRDASR VATAASAVVR NPRDVIPFLT
     GPGPDAGSF
//