A0A0L8G5U4 · A0A0L8G5U4_OCTBM
- ProteinPeptidase M20 dimerisation domain-containing protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids445 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
Catalytic activity
- (5Z,8Z,11Z,14Z)-eicosatetraenoate + L-phenylalanine = H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-phenylalanineThis reaction proceeds in the forward and the backward directions.
- (9Z)-octadecenoate + L-phenylalanine = H2O + N-(9Z-octadecenoyl)-L-phenylalanineThis reaction proceeds in the forward and the backward directions.
- (9Z)-octadecenoate + glycine = H2O + N-(9Z-octadecenoyl)glycineThis reaction proceeds in the backward direction.
- H2O + N-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-L-phenylalanine = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + L-phenylalanineThis reaction proceeds in the forward direction.
- H2O + N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycineThis reaction proceeds in the forward and the backward directions.
- H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-serine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + L-serineThis reaction proceeds in the forward and the backward directions.
- H2O + N-(9Z-octadecenoyl)-L-asparagine = (9Z)-octadecenoate + L-asparagineThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl)-L-glutamine = (9Z)-octadecenoate + L-glutamineThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl)-L-leucine = (9Z)-octadecenoate + L-leucineThis reaction proceeds in the forward and the backward directions.
- H2O + N-(9Z-octadecenoyl)-L-lysine = (9Z)-octadecenoate + L-lysineThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl)-L-methionine = (9Z)-octadecenoate + L-methionineThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl)-L-serine = (9Z)-octadecenoate + L-serineThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl)-L-tryptophan = (9Z)-octadecenoate + L-tryptophanThis reaction proceeds in the forward direction.
- H2O + N-(9Z-octadecenoyl)-L-tyrosine = (9Z)-octadecenoate + L-tyrosineThis reaction proceeds in the forward direction.
- H2O + N-hexadecanoyl-L-phenylalanine = hexadecanoate + L-phenylalanineThis reaction proceeds in the forward direction.
- H2O + N-octadecanoyl-L-phenylalanine = L-phenylalanine + octadecanoateThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Pathway
Lipid metabolism; fatty acid metabolism.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 68 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 70 | |||||
Sequence: D | ||||||
Binding site | 100 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 100 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 134 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 135 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 162 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 406 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides | |
Molecular Function | metal ion binding | |
Molecular Function | peptidase activity | |
Biological Process | amide biosynthetic process | |
Biological Process | amide catabolic process | |
Biological Process | amino acid metabolic process | |
Biological Process | cellular lipid metabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended namePeptidase M20 dimerisation domain-containing protein
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Lophotrochozoa > Mollusca > Cephalopoda > Coleoidea > Octopodiformes > Octopoda > Incirrata > Octopodidae > Octopus
Accessions
- Primary accessionA0A0L8G5U4
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 184-325 | Peptidase M20 dimerisation | ||||
Sequence: EKGQAIVKLSVNGTAGHSAIPPPESVIGILSTAIRRIESNPQPDLFGTGAERAMFEHLAPKLPFLPRMVLSNLWLFRPVVSWVLSRQPQTNALIRTVNAVTKFNAGIKDNVLSDSAEAVIDYRIHPSQTLEQLFDFHLKIIN |
Sequence similarities
Belongs to the peptidase M20A family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length445
- Mass (Da)50,429
- Last updated2015-11-11 v1
- Checksum4FFBB77CBF93E6E0
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KQ423675 EMBL· GenBank· DDBJ | KOF72407.1 EMBL· GenBank· DDBJ | Genomic DNA |