位置:首页 > 蛋白库 > GMHBB_ECOL6
GMHBB_ECOL6
ID   GMHBB_ECOL6             Reviewed;         190 AA.
AC   Q8FKZ1;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=c0241;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014075; AAN78733.1; -; Genomic_DNA.
DR   RefSeq; WP_001140167.1; NC_004431.1.
DR   AlphaFoldDB; Q8FKZ1; -.
DR   SMR; Q8FKZ1; -.
DR   STRING; 199310.c0241; -.
DR   EnsemblBacteria; AAN78733; AAN78733; c0241.
DR   KEGG; ecc:c0241; -.
DR   eggNOG; COG0241; Bacteria.
DR   HOGENOM; CLU_085077_3_0_6; -.
DR   OMA; EHQICLE; -.
DR   BioCyc; ECOL199310:C0241-MON; -.
DR   UniPathway; UPA00356; UER00438.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000001410; 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;
KW   Carbohydrate metabolism; Cytoplasm; Hydrolase;
KW   Lipopolysaccharide biosynthesis; Magnesium; Metal-binding; Zinc.
FT   CHAIN           1..190
FT                   /note="D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-
FT                   phosphatase"
FT                   /id="PRO_0000209391"
FT   ACT_SITE        11
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        13
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         11..13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         19..22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         53..56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         110..111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="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   190 AA;  21145 MW;  3313858A1128FA74 CRC64;
     MAKSVPAIFL DRDGTINVDH GYVHEIDNFE FIDGVIDAMR ELKKMGFALV VVTNQSGIAR
     GKFTEAQFET LTEWMDWSLA DRDVDLDGIY YCPHHPQGSV EEFRQVCDCR KPHPGMFLSA
     RDYLHIDMAA SYMVGDKLED MQAAAAASVG TKVLVRTGKP ITPEAENAAD WVLNSLADLP
     QAIKKQQKPA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024