B4DV28 · B4DV28_HUMAN

  • Protein
    Cytosolic non-specific dipeptidase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

Function

Catalytic activity

  • (S)-lactate + L-phenylalanine = H2O + N-[(S)-lactoyl]-L-phenylalanine
    This reaction proceeds in the forward
    and the backward
    directions.
  • H2O + L-cysteinylglycine = glycine + L-cysteine
    This reaction proceeds in the forward direction.
  • H2O + L-seryl-L-threonine = L-serine + L-threonine
    This reaction proceeds in the forward direction.
  • H2O + L-threonyl-L-serine = L-serine + L-threonine
    This reaction proceeds in the forward direction.
  • H2O + L-threonyl-L-threonine = 2 L-threonine
    This reaction proceeds in the forward direction.
  • Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids.
    EC:3.4.13.18 (UniProtKB | ENZYME | Rhea)

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 2 manganese ions per subunit.

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site99Mn2+ 2 (UniProtKB | ChEBI)
Active site101
Binding site120Mn2+ 2 (UniProtKB | ChEBI)
Binding site120Mn2+ 1 (UniProtKB | ChEBI)
Active site154Proton acceptor
Binding site155Mn2+ 1 (UniProtKB | ChEBI)
Binding site183Mn2+ 2 (UniProtKB | ChEBI)
Binding site183substrate; ligand shared between homodimeric partners; in other chain
Binding site216substrate; ligand shared between homodimeric partners
Site216Important for catalytic activity
Binding site318substrate; ligand shared between homodimeric partners
Binding site331substrate; ligand shared between homodimeric partners; in other chain
Binding site405substrate; ligand shared between homodimeric partners; in other chain
Binding site433Mn2+ 1 (UniProtKB | ChEBI)
Binding site433substrate; ligand shared between homodimeric partners; in other chain

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functioncarboxypeptidase activity
Molecular Functionmetal ion binding
Molecular Functionmetallodipeptidase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytosolic non-specific dipeptidase
  • EC number
  • Alternative names
    • CNDP dipeptidase 2
    • Threonyl dipeptidase

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    B4DV28

Subcellular Location

PTM/Processing

Keywords

Proteomic databases

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain196-354Peptidase M20 dimerisation

Sequence similarities

Belongs to the peptidase M20A family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    463
  • Mass (Da)
    51,502
  • Last updated
    2008-09-23 v1
  • Checksum
    4A3998A10B2397B6
MAALTTLFKYIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVKQLGGSVELVDIGKQKLPDGSEIPLPPILLGRLGSDPQKKTVCIYGHLDVQPAALERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQEIPVNVRFCLEGMEESGSEGLDELIFARKDTFFKDVDYVCISDNYWLGKKKPCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMGSLVDKRGNILIPGINEAVAAVTEEEHKLYDDIDFDIEEFAKDVGAQILLHSHKKDILMHRWRYPSLSLHGIEGAFSGSGAKTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKKFAELRSPNEFKVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFGVEPDLTREGGSIPVTLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRYNYIEGTKMLAAYLYEVSQLKD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK300904
EMBL· GenBank· DDBJ
BAG62540.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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