A0A6I8RB27 · A0A6I8RB27_XENTR

Function

function

Catalyzes the peptide bond hydrolysis in dipeptides, displaying a non-redundant activity toward threonyl dipeptides. Mediates threonyl dipeptide catabolism in a tissue-specific way. Has high dipeptidase activity toward cysteinylglycine, an intermediate metabolite in glutathione metabolism. Metabolizes N-lactoyl-amino acids, both through hydrolysis to form lactic acid and amino acids, as well as through their formation by reverse proteolysis. Plays a role in the regulation of cell cycle arrest and apoptosis.

Catalytic activity

  • (S)-lactate + L-phenylalanine = N-[(S)-lactoyl]-L-phenylalanine + H2O
    This reaction proceeds in the forward
    and the backward
    directions.
  • L-cysteinylglycine + H2O = L-cysteine + glycine
    This reaction proceeds in the forward direction.
  • L-seryl-L-threonine + H2O = L-threonine + L-serine
    This reaction proceeds in the forward direction.
  • L-threonyl-L-serine + H2O = L-threonine + L-serine
    This reaction proceeds in the forward direction.
  • L-threonyl-L-threonine + H2O = 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.

Type
IDPosition(s)Description
Binding site91Mn2+ 2 (UniProtKB | ChEBI)
Active site93
Binding site124Mn2+ 2 (UniProtKB | ChEBI)
Binding site124Mn2+ 1 (UniProtKB | ChEBI)
Active site158Proton acceptor
Binding site159Mn2+ 1 (UniProtKB | ChEBI)
Binding site187Mn2+ 2 (UniProtKB | ChEBI)
Binding site187substrate; ligand shared between homodimeric partners; in other chain
Binding site220substrate; ligand shared between homodimeric partners
Site220Important for catalytic activity
Binding site322substrate; ligand shared between homodimeric partners
Binding site335substrate; ligand shared between homodimeric partners; in other chain
Binding site409substrate; ligand shared between homodimeric partners; in other chain
Binding site437Mn2+ 1 (UniProtKB | ChEBI)
Binding site437substrate; 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

Gene names

    • Name
      cndp2

Organism names

Accessions

  • Primary accession
    A0A6I8RB27

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-25
ChainPRO_502775427026-466Cytosolic non-specific dipeptidase

Keywords

Expression

Gene expression databases

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain200-359Peptidase M20 dimerisation

Sequence similarities

Belongs to the peptidase M20A family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    466
  • Mass (Da)
    51,598
  • Last updated
    2020-12-02 v1
  • Checksum
    351D40380A77632E
YTCTTTLFCNSLLLAEWVAIQSVSAWPEKRGEIKRMMEVAAKEIERLGGTTELADIGKQKLPDGTEIPLPPILLGKLGSDPGKKTVCVYGHLDVQPAALEDGWDSEPFVLEERDGKLYGRGSTDDKGPVLAWLNSIEAYQKTNQDLPVNLKFCFEGMEESGSEGLDDLIFARKDTFFKGVDYVCISDNYWLGKTKPCITYGLRGICYFFIEVECSCKDLHSGVYGGSVHEAMTDLIALMGSLVDKKGKILIPGINEAVAPVLKEEKDIYEAIEFDLEDFANDIGAGRLLHESKEKILMHRWRFPSLSLHGIEGAFSATGAKTVIPRKVIGKFSIRLVPDMNPDDVQKQVEDYLTKKFKELGSPNKFQVTMGHGGKPWVSDFNHPHYVAGRKAMKTVFNVEPDLTREGGSIPVTLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRSNYIQGVKLLGAYLYEVSNLE

Genome annotation databases

Similar Proteins

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