B4DKM6 · B4DKM6_HUMAN
- ProteinParaoxonase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids363 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
Catalytic activity
- a phenyl acetate + H2O = a phenol + acetate + H+
Cofactor
Note: Binds 2 calcium ions per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 74 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 75 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Active site | 135 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 137 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: I | ||||||
Binding site | 176 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: N | ||||||
Binding site | 177 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 232 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: N | ||||||
Binding site | 277 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 278 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | membrane | |
Molecular Function | acyl-L-homoserine-lactone lactonohydrolase activity | |
Molecular Function | arylesterase activity | |
Molecular Function | metal ion binding | |
Biological Process | response to toxic substance |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameParaoxonase
- EC number
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionB4DKM6
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Peripheral membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 21-43 | Helical | ||||
Sequence: AMGRLVAVGLLGIALALLGERLL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 63↔361 | In form B | ||||
Sequence: CHLIKGIEAGSEDIDILPNGLAFFSVGLKFPGLHSFAPDKPGGILMMDLKEEKPGARELRISRGFDLASFNPHGISTFIDNEFKNTVEIFKFEEAENSLLHLKTVKHELLPSVNDITAVGPAHFYATNDHYFSDPFLKYLETYLNLHWANVVYYSPNEVKVVAEGFDSANGINISPDDKYIYVADILAHEIHVLEKHTNMNLTQLKVLELDTLVDNLSIDPSSGDIWVGCHPNGQKLFVYDPNNPPSSEVLRIQNILSEKPTVTTVYANNGSVLQGSSVASVYDGKLLIGTLYHRALYC | ||||||
Glycosylation | 278 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 332 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Glycosylated.
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Homotrimer.
Structure
Sequence
- Sequence statusComplete
- Length363
- Mass (Da)40,028
- Last updated2008-09-23 v1
- ChecksumAC841159D01021D2