(data stored in ACNUC7421 zone)

SWISSPROT: GMHBB_ECO57

ID   GMHBB_ECO57             Reviewed;         191 AA.
AC   P63229; P31546;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 1.
DT   30-AUG-2017, entry version 89.
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=Z0212, ECs0202;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11108008;
RA   Ohnishi M., Murata T., Nakayama K., Kuhara S., Hattori M.,
RA   Kurokawa K., Yasunaga T., Yokoyama K., Makino K., Shinagawa H.,
RA   Hayashi T.;
RT   "Comparative analysis of the whole set of rRNA operons between an
RT   enterohemorrhagic Escherichia coli O157:H7 Sakai strain and an
RT   Escherichia coli K-12 strain MG1655.";
RL   Syst. Appl. Microbiol. 23:315-324(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Converts the D-glycero-beta-D-manno-heptose 1,7-
CC       bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-
CC       phosphate by removing the phosphate group at the C-7 position.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: D-glycero-beta-D-manno-heptose 1,7-
CC       bisphosphate + H(2)O = D-glycero-beta-D-manno-heptose 1-phosphate
CC       + phosphate.
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-
CC       manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose
CC       from D-glycero-beta-D-manno-heptose 7-phosphate: step 2/4.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core
CC       biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GmhB family. {ECO:0000305}.
DR   EMBL; AB035926; BAA93568.1; -; Genomic_DNA.
DR   EMBL; AE005174; AAG54502.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33625.1; -; Genomic_DNA.
DR   PIR; B85505; B85505.
DR   PIR; B90654; B90654.
DR   RefSeq; NP_308229.1; NC_002695.1.
DR   RefSeq; WP_001140187.1; NZ_MWVM01000012.1.
DR   ProteinModelPortal; P63229; -.
DR   SMR; P63229; -.
DR   STRING; 155864.Z0212; -.
DR   EnsemblBacteria; AAG54502; AAG54502; Z0212.
DR   EnsemblBacteria; BAB33625; BAB33625; BAB33625.
DR   GeneID; 913974; -.
DR   KEGG; ece:Z0212; -.
DR   KEGG; ecs:ECs0202; -.
DR   PATRIC; fig|386585.9.peg.306; -.
DR   eggNOG; ENOG4108ZI0; Bacteria.
DR   eggNOG; COG0241; LUCA.
DR   HOGENOM; HOG000016501; -.
DR   KO; K03273; -.
DR   UniPathway; UPA00356; UER00438.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; IPR023214; HAD-like_dom.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR004446; Heptose_bisP_phosphatase.
DR   InterPro; IPR006543; Histidinol-phos.
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; P63229.
DR   SWISS-2DPAGE; P63229.
KW   Carbohydrate metabolism; Complete proteome; Cytoplasm; Hydrolase;
KW   Lipopolysaccharide biosynthesis; Magnesium; Metal-binding; Zinc.
FT   CHAIN         1    191       D-glycero-beta-D-manno-heptose-1,7-
FT                                bisphosphate 7-phosphatase.
FT                                /FTId=PRO_0000209390.
FT   REGION       11     13       Substrate binding. {ECO:0000250}.
FT   REGION       19     22       Substrate binding. {ECO:0000250}.
FT   REGION       53     56       Substrate binding. {ECO:0000250}.
FT   REGION      110    111       Substrate binding. {ECO:0000250}.
FT   ACT_SITE     11     11       Nucleophile. {ECO:0000250}.
FT   ACT_SITE     13     13       Proton donor. {ECO:0000250}.
FT   METAL        11     11       Magnesium. {ECO:0000250}.
FT   METAL        13     13       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        92     92       Zinc. {ECO:0000250|UniProtKB:Q7WG29}.
FT   METAL        94     94       Zinc; via pros nitrogen.
FT                                {ECO:0000250|UniProtKB:Q7WG29}.
FT   METAL       107    107       Zinc. {ECO:0000250|UniProtKB:Q7WG29}.
FT   METAL       109    109       Zinc. {ECO:0000250|UniProtKB:Q7WG29}.
FT   METAL       136    136       Magnesium. {ECO:0000250}.
FT   METAL       137    137       Magnesium. {ECO:0000250}.
FT   BINDING     137    137       Substrate. {ECO:0000250}.
FT   SITE         53     53       Stabilizes the phosphoryl group.
FT                                {ECO:0000250}.
FT   SITE        110    110       Contributes to substrate recognition.
FT                                {ECO:0000250}.
FT   SITE        111    111       Stabilizes the phosphoryl group.
FT                                {ECO:0000250}.
SQ   SEQUENCE   191 AA;  21294 MW;  E7814B34A23128FA CRC64;
     MAKSVPAIFL DRDGTINVDH GYVHEIDNFE FIDGVIDAMR ELKKMGFALV VVTNQSGIAR
     GKFTEAQFET LTEWMDWSLA DRDVDLDGIY YCPHHPQGSV EEFRQVCDCR KPHPGMLLSA
     RDYLHIDMAA SYMVGDKLED MQAAVAANVG TKVLVRTGKP ITPEAENAAD WVLNSLADLP
     QAIKKQQKPA Q
//

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