Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

K5B7Z4 · K5B7Z4_MYCHD

Function

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

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

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site49UDP (UniProtKB | ChEBI)
Binding site49UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site51Mg2+ 1 (UniProtKB | ChEBI)
Binding site51UDP (UniProtKB | ChEBI)
Binding site51UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site78UDP (UniProtKB | ChEBI)
Binding site78UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site110UDP (UniProtKB | ChEBI)
Binding site110UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site111UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site131UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site132UDP (UniProtKB | ChEBI)
Binding site132UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site133Mg2+ 2 (UniProtKB | ChEBI)
Binding site178(R)-malate 2 (UniProtKB | ChEBI)
Binding site178(S)-malate (UniProtKB | ChEBI)
Binding site180(R)-malate 2 (UniProtKB | ChEBI)
Binding site180(R)-malate 1 (UniProtKB | ChEBI)
Binding site180(S)-malate (UniProtKB | ChEBI)
Binding site181(R)-malate 1 (UniProtKB | ChEBI)
Binding site181(R)-malate 2 (UniProtKB | ChEBI)
Binding site181(S)-malate (UniProtKB | ChEBI)
Binding site223UDP (UniProtKB | ChEBI)
Binding site223UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site226UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site253(S)-malate (UniProtKB | ChEBI)
Binding site255(R)-malate 2 (UniProtKB | ChEBI)
Binding site255(R)-malate 1 (UniProtKB | ChEBI)
Binding site255UDP (UniProtKB | ChEBI)
Binding site255UDP-alpha-D-glucose (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionglycosyltransferase activity
Molecular Functionmetal ion binding
Molecular Functionnucleotide binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glucosyl-3-phosphoglycerate synthase
  • EC number

Gene names

    • ORF names
      C731_3243

Organism names

Accessions

  • Primary accession
    K5B7Z4

Proteomes

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the glycosyltransferase 2 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    314
  • Mass (Da)
    33,592
  • Last updated
    2013-01-09 v1
  • MD5 Checksum
    7C8AE0572C42001DE73503653B4BD7E7
MTLVPDLTATDLARHRWLTDNSWTRPTWTVAELEAAKAGRTISVVLPALNEEETVGGVVETIRPLLGGLVDELIVLDSGSTDDTEIRAMAAGARVISREVALPEVAPQPGKGEVLWRSLAATTGDIIVFIDSDLIDPDPMFVPKLVGPLLLSEGVHLVKGFYRRPLKTSGSEDAHGGGRVTELVARPLLAALRPELTCVLQPLGGEYAGTRELLMSVPFAPGYGVEIGLLVDTYDRLGLDAIAQVNLGVRAHRNRPLTDLAAMSRQVIATLFSRCGVPDSGVGLTQFFADGDGFSPRTSEVSLVDRPPMNTLRG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AMRA01000093
EMBL· GenBank· DDBJ
EKF22803.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help