Q2T109 · Q2T109_BURTA

Function

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Features

Showing features for active site, binding site, site.

118720406080100120140160180
TypeIDPosition(s)Description
Active site13Proton donor
Binding site13Mg2+ (UniProtKB | ChEBI)
Active site15Proton donor
Binding site15Mg2+ (UniProtKB | ChEBI)
Site56Stabilizes the phosphoryl group
Binding site95Zn2+ (UniProtKB | ChEBI)
Binding site97Zn2+ (UniProtKB | ChEBI)
Binding site103Zn2+ (UniProtKB | ChEBI)
Binding site105Zn2+ (UniProtKB | ChEBI)
Site106Contributes to substrate recognition
Site107Stabilizes the phosphoryl group
Binding site132Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionmetal ion binding
Molecular Functionphosphatase activity
Biological Processcarbohydrate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    D,D-heptose 1,7-bisphosphate phosphatase
  • EC number

Gene names

    • Ordered locus names
      BTH_I0583

Organism names

Accessions

  • Primary accession
    Q2T109

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond95Interchain

Family & Domains

Sequence similarities

Belongs to the gmhB family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    187
  • Mass (Da)
    20,093
  • Last updated
    2006-01-24 v1
  • Checksum
    B48E10DD6D3C1E33
MPTSPSKKLVVLDRDGVINVDSDAFVKSPDEWVALPGSLEAIARLNHAGYRVVVATNQSGIGRGLFDMATLNAMHLKMHRAAAAVGGRIDAVFFCPHTADDHCDCRKPMPGMMKLIAERFEIDPADTPVVGDSLRDLQAGAALGFRPHLVLTGKGKKTLAAGGLPEGTRVHDDLRAFALDFLSKEHE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000086
EMBL· GenBank· DDBJ
ABC38211.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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