A0A674GX26 · A0A674GX26_TAEGU
- ProteinCytosolic non-specific dipeptidase
- GeneCNDP2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids474 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
Catalytic activity
- (S)-lactate + L-phenylalanine = H2O + N-[(S)-lactoyl]-L-phenylalanineThis reaction proceeds in the forward and the backward directions.
- H2O + L-cysteinylglycine = glycine + L-cysteineThis reaction proceeds in the forward direction.
- H2O + L-seryl-L-threonine = L-serine + L-threonineThis reaction proceeds in the forward direction.
- H2O + L-threonyl-L-serine = L-serine + L-threonineThis reaction proceeds in the forward direction.
- H2O + L-threonyl-L-threonine = 2 L-threonineThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 manganese ions per subunit.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 99 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 101 | |||||
Sequence: D | ||||||
Binding site | 132 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 132 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 165 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 166 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 194 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 194 | substrate; ligand shared between homodimeric partners; in other chain | ||||
Sequence: D | ||||||
Binding site | 227 | substrate; ligand shared between homodimeric partners | ||||
Sequence: H | ||||||
Site | 227 | Important for catalytic activity | ||||
Sequence: H | ||||||
Binding site | 329 | substrate; ligand shared between homodimeric partners | ||||
Sequence: T | ||||||
Binding site | 342 | substrate; ligand shared between homodimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 416 | substrate; ligand shared between homodimeric partners; in other chain | ||||
Sequence: S | ||||||
Binding site | 444 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 444 | substrate; ligand shared between homodimeric partners; in other chain | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | carboxypeptidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | metallodipeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytosolic non-specific dipeptidase
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Passeriformes > Passeroidea > Estrildidae > Estrildinae > Taeniopygia
Accessions
- Primary accessionA0A674GX26
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Keywords
- PTM
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 207-366 | Peptidase M20 dimerisation | ||||
Sequence: YGLRGVCYYFIEVECCDKDLHSGVYGGSVHEAMTDLIALMGSLVDGKGKILIPGVNEAVAPVTDEELALYEKIDFDLTEYAKDVGATRLLHDAKREILMHRWRYPSLSLHGIEGAFSASGAKTVIPRKVIGKFSIRLVPNMTPEEVTKNVEDYLNKKFAE |
Sequence similarities
Belongs to the peptidase M20A family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length474
- Mass (Da)52,958
- Last updated2020-06-17 v1
- Checksum487C84388BDC425A
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A674GXZ8 | A0A674GXZ8_TAEGU | CNDP2 | 511 | ||
H0ZFS7 | H0ZFS7_TAEGU | CNDP2 | 475 | ||
A0A674H3U3 | A0A674H3U3_TAEGU | CNDP2 | 454 |
Keywords
- Technical term