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Protein

D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase

Gene

gmhB

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.By similarity

Catalytic activityi

D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: ADP-L-glycero-beta-D-manno-heptose biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Bifunctional protein HldE (hldE)
  2. D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase (gmhB)
  3. Bifunctional protein HldE (hldE)
  4. ADP-L-glycero-D-manno-heptose-6-epimerase (hldD)
This subpathway is part of the pathway ADP-L-glycero-beta-D-manno-heptose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate, the pathway ADP-L-glycero-beta-D-manno-heptose biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: LPS core biosynthesis

This protein is involved in the pathway LPS core biosynthesis, which is part of Bacterial outer membrane biogenesis.
View all proteins of this organism that are known to be involved in the pathway LPS core biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111NucleophileBy similarity
Metal bindingi11 – 111MagnesiumBy similarity
Active sitei13 – 131Proton donorBy similarity
Metal bindingi13 – 131Magnesium; via carbonyl oxygenBy similarity
Sitei53 – 531Stabilizes the phosphoryl groupBy similarity
Metal bindingi92 – 921ZincBy similarity
Metal bindingi94 – 941Zinc; via amide nitrogenBy similarity
Metal bindingi107 – 1071ZincBy similarity
Metal bindingi109 – 1091ZincBy similarity
Sitei110 – 1101Contributes to substrate recognitionBy similarity
Sitei111 – 1111Stabilizes the phosphoryl groupBy similarity
Metal bindingi136 – 1361MagnesiumBy similarity
Metal bindingi137 – 1371MagnesiumBy similarity
Binding sitei137 – 1371SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Lipopolysaccharide biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciECOL386585:GJFA-201-MONOMER.
UniPathwayiUPA00356; UER00438.
UPA00958.

Names & Taxonomyi

Protein namesi
Recommended name:
D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase (EC:3.1.3.82)
Alternative name(s):
D,D-heptose 1,7-bisphosphate phosphatase
Short name:
HBP phosphatase
Gene namesi
Name:gmhB
Ordered Locus Names:Z0212, ECs0202
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 191191D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatasePRO_0000209390Add
BLAST

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi155864.Z0212.

Structurei

3D structure databases

ProteinModelPortaliP63229.
SMRiP63229. Positions 4-187.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 133Substrate bindingBy similarity
Regioni19 – 224Substrate bindingBy similarity
Regioni53 – 564Substrate bindingBy similarity
Regioni110 – 1112Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the GmhB family.Curated

Phylogenomic databases

eggNOGiENOG4108ZI0. Bacteria.
COG0241. LUCA.
HOGENOMiHOG000016501.
KOiK03273.
OMAiSFMIGDK.
OrthoDBiEOG6QG8GT.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006549. HAD-SF_hydro_IIIA.
IPR004446. Heptose_bisP_phosphatase.
IPR006543. Histidinol-phos.
[Graphical view]
PIRSFiPIRSF004682. GmhB. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR00213. GmhB_yaeD. 1 hit.
TIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01656. Histidinol-ppas. 1 hit.

Sequencei

Sequence statusi: Complete.

P63229-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKSVPAIFL DRDGTINVDH GYVHEIDNFE FIDGVIDAMR ELKKMGFALV
60 70 80 90 100
VVTNQSGIAR GKFTEAQFET LTEWMDWSLA DRDVDLDGIY YCPHHPQGSV
110 120 130 140 150
EEFRQVCDCR KPHPGMLLSA RDYLHIDMAA SYMVGDKLED MQAAVAANVG
160 170 180 190
TKVLVRTGKP ITPEAENAAD WVLNSLADLP QAIKKQQKPA Q
Length:191
Mass (Da):21,294
Last modified:September 27, 2004 - v1
Checksum:iE7814B34A23128FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035926 Genomic DNA. Translation: BAA93568.1.
AE005174 Genomic DNA. Translation: AAG54502.1.
BA000007 Genomic DNA. Translation: BAB33625.1.
PIRiB85505.
B90654.
RefSeqiNP_308229.1. NC_002695.1.
WP_001140187.1. NZ_LPWC01000161.1.

Genome annotation databases

EnsemblBacteriaiAAG54502; AAG54502; Z0212.
BAB33625; BAB33625; BAB33625.
GeneIDi913974.
KEGGiece:Z0212.
ecs:ECs0202.
PATRICi18349352. VBIEscCol44059_0206.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035926 Genomic DNA. Translation: BAA93568.1.
AE005174 Genomic DNA. Translation: AAG54502.1.
BA000007 Genomic DNA. Translation: BAB33625.1.
PIRiB85505.
B90654.
RefSeqiNP_308229.1. NC_002695.1.
WP_001140187.1. NZ_LPWC01000161.1.

3D structure databases

ProteinModelPortaliP63229.
SMRiP63229. Positions 4-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi155864.Z0212.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG54502; AAG54502; Z0212.
BAB33625; BAB33625; BAB33625.
GeneIDi913974.
KEGGiece:Z0212.
ecs:ECs0202.
PATRICi18349352. VBIEscCol44059_0206.

Phylogenomic databases

eggNOGiENOG4108ZI0. Bacteria.
COG0241. LUCA.
HOGENOMiHOG000016501.
KOiK03273.
OMAiSFMIGDK.
OrthoDBiEOG6QG8GT.

Enzyme and pathway databases

UniPathwayiUPA00356; UER00438.
UPA00958.
BioCyciECOL386585:GJFA-201-MONOMER.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006549. HAD-SF_hydro_IIIA.
IPR004446. Heptose_bisP_phosphatase.
IPR006543. Histidinol-phos.
[Graphical view]
PIRSFiPIRSF004682. GmhB. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR00213. GmhB_yaeD. 1 hit.
TIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01656. Histidinol-ppas. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Comparative analysis of the whole set of rRNA operons between an enterohemorrhagic Escherichia coli O157:H7 Sakai strain and an Escherichia coli K-12 strain MG1655."
    Ohnishi M., Murata T., Nakayama K., Kuhara S., Hattori M., Kurokawa K., Yasunaga T., Yokoyama K., Makino K., Shinagawa H., Hayashi T.
    Syst. Appl. Microbiol. 23:315-324(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  3. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiGMHBB_ECO57
AccessioniPrimary (citable) accession number: P63229
Secondary accession number(s): P31546
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: May 11, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.