(data stored in ACNUC7421 zone)

SWISSPROT: GMHBB_SALTY

ID   GMHBB_SALTY             Reviewed;         188 AA.
AC   Q8ZRM8;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   11-DEC-2019, entry version 102.
DE   RecName: Full=D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase;
DE            EC=3.1.3.82;
DE   AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase;
DE            Short=HBP phosphatase;
GN   Name=gmhB; OrderedLocusNames=STM0248;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE.
RX   PubMed=12101286; DOI=10.1099/00221287-148-7-1979;
RA   Valvano M.A., Messner P., Kosma P.;
RT   "Novel pathways for biosynthesis of nucleotide-activated glycero-manno-
RT   heptose precursors of bacterial glycoproteins and cell surface
RT   polysaccharides.";
RL   Microbiology 148:1979-1989(2002).
CC   -!- FUNCTION: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate
CC       intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by
CC       removing the phosphate group at the C-7 position. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-
CC         glycero-beta-D-manno-heptose 1-phosphate + phosphate;
CC         Xref=Rhea:RHEA:28518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:60208, ChEBI:CHEBI:61593; EC=3.1.3.82;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-
CC       heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-
CC       glycero-beta-D-manno-heptose 7-phosphate: step 2/4.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GmhB family. {ECO:0000305}.
DR   EMBL; AE006468; AAL19211.1; -; Genomic_DNA.
DR   RefSeq; NP_459252.1; NC_003197.2.
DR   RefSeq; WP_001051726.1; NC_003197.2.
DR   SMR; Q8ZRM8; -.
DR   PaxDb; Q8ZRM8; -.
DR   PRIDE; Q8ZRM8; -.
DR   EnsemblBacteria; AAL19211; AAL19211; STM0248.
DR   GeneID; 1251766; -.
DR   KEGG; stm:STM0248; -.
DR   PATRIC; fig|99287.12.peg.262; -.
DR   eggNOG; ENOG4108ZI0; Bacteria.
DR   eggNOG; COG0241; LUCA.
DR   HOGENOM; HOG000016501; -.
DR   KO; K03273; -.
DR   OMA; EHQICLE; -.
DR   PhylomeDB; Q8ZRM8; -.
DR   BioCyc; SENT99287:STM0248-MONOMER; -.
DR   BRENDA; 3.1.3.82; 5542.
DR   UniPathway; UPA00356; UER00438.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0034200; F:D,D-heptose 1,7-bisphosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR004446; Heptose_bisP_phosphatase.
DR   InterPro; IPR006543; Histidinol-phos.
DR   PANTHER; PTHR42891; PTHR42891; 1.
DR   PIRSF; PIRSF004682; GmhB; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR00213; GmhB_yaeD; 1.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR   TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8ZRM8.
DR   SWISS-2DPAGE; Q8ZRM8.
KW   Carbohydrate metabolism; Cytoplasm; Hydrolase;
KW   Lipopolysaccharide biosynthesis; Magnesium; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..188
FT                   /note="D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-
FT                   phosphatase"
FT                   /id="PRO_0000209405"
FT   REGION          11..13
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          19..22
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          53..56
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          110..111
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        11
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        13
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   METAL           11
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           13
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   METAL           92
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   METAL           94
FT                   /note="Zinc; via pros nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   METAL           107
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   METAL           109
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   METAL           136
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           137
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            53
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000250"
FT   SITE            110
FT                   /note="Contributes to substrate recognition"
FT                   /evidence="ECO:0000250"
FT   SITE            111
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   188 AA;  20920 MW;  42088A34D12CD93B CRC64;
     MAKFVPAIFL DRDGTINVDH GYVHEIDAFE FIDGVIDAMR ELKKMGYALV VVTNQSGIAR
     GKFTEAQFET LTEWMDWSLA DRDVDLDGIY YCPHHPQGSI EEFRQVCDCR KPHPGMLISA
     RDFLHIDMAA SYMVGDKLED MQAAAAANVG TKVLVRTGKP VTAEAENAAD WVLNSLADLP
     SAIKKQQK
//

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