B4DX19 · B4DX19_HUMAN
- ProteinParaoxonase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids355 (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 | 53 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 54 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 115 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 117 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 168 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: N | ||||||
Binding site | 169 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 224 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: N | ||||||
Binding site | 269 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 270 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | acyl-L-homoserine-lactone lactonohydrolase activity | |
Molecular Function | arylesterase activity | |
Molecular Function | metal ion binding |
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 accessionB4DX19
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-30 | |||||
Sequence: MGKLVALVLLGVGLSLVGEMFLAFRERVNA | ||||||
Chain | PRO_5029941838 | 31-355 | Paraoxonase | |||
Sequence: SREVEPVEPENCHLIEELETGSEDMEILPNGLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTFTDEDNAMYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLDPYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPPASEVLRIQNILTEEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCEL | ||||||
Disulfide bond | 42↔353 | In form B | ||||
Sequence: CHLIEELETGSEDMEILPNGLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTFTDEDNAMYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLDPYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPPASEVLRIQNILTEEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYC | ||||||
Glycosylation | 253 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 270 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 324 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Glycosylated.
Keywords
- PTM
Structure
Sequence
- Sequence statusComplete
- Length355
- Mass (Da)39,721
- Last updated2008-09-23 v1
- ChecksumB579F535E44B59E2