H2A0M3 · AMO_PINMG
- ProteinPutative amine oxidase [copper-containing]
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids781 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 copper ion per subunit.
Note: Binds 2 calcium ions per subunit.
Note: Contains 1 topaquinone per subunit.
Note: Binds 1 Mn2+ ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 385-395 | substrate | ||||
Sequence: FFDSSYMIGMN | ||||||
Active site | 387 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 472-477 | substrate | ||||
Sequence: IANYDY | ||||||
Active site | 475 | Schiff-base intermediate with substrate; via topaquinone | ||||
Sequence: Y | ||||||
Binding site | 525 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 527 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 534 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 534 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 536 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 536 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 579 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 671 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 674 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 676 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 682 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 682 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 683 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 693 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | plasma membrane | |
Molecular Function | copper ion binding | |
Molecular Function | primary amine oxidase activity | |
Molecular Function | quinone binding | |
Biological Process | amine metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePutative amine oxidase [copper-containing]
- EC number
Organism names
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Lophotrochozoa > Mollusca > Bivalvia > Autobranchia > Pteriomorphia > Pterioida > Pterioidea > Pteriidae > Pinctada
Accessions
- Primary accessionH2A0M3
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-34 | |||||
Sequence: MSLPKTANGMDKLKLCYLLLFYLGSSSLTEVSGA | ||||||
Chain | PRO_0000418018 | 35-781 | Putative amine oxidase [copper-containing] | |||
Sequence: QTCEIDSVLCTSDLSEPDDPPIFHDLTTKEIKSVQTYLYHQRDLRLLRPGLAKINTSFIQGMELYLPNKKDVIHYLQSKVPTPKPPRAAVVTIFRGDCDPAVVEEYIVFPLPWPTQHRLHRKVPYYLRPFNDVEFATISDFLTKQVDGVLRQFLEESFGGRLINCGNRCLNFQFASPVGPSVSNEPGARKSWYWLHQLVEYSALHPVDFAVLMKIVGCVYTIEKVYFNNMYFNSLQEVALHYRNPSFPRLRIPYPVDSKQLFSKMERRGILFPEKPVSPPRQVEPEGKRYSVKYQEVKYMNWKFNFRLSPGLGPRLHNIRYHDRLIVYELALQDIVVFYSGAEPPHQYANFFDSSYMIGMNLQGMVPGVDCPTGATFIDSHILTESSLKPAKLINAFCVFEQNTGDFLRRHISKTSPDGPFYEGVPSIVLVLRAITTIANYDYTIDFIFHHNGVLQTKVVPTGYILPSLYTKQNENKYGFRLNNKLIGNLHHHLFNFKVDIDINGQHNRYETLDIVLDKTSHPVSKKPYDVWYQNKIKHNLRKTEMEALFKYDFDKPMHHIFYNNNLKSPEGNNMAYRLVNRGMSKSLLPECSGNEGTGAWMRHQIAVTKRKETELTSSSVYSAFGTKNPVVNFRNFYADNENIVDEDLVAWVTMGTYHIPHTEDLPVTHTPGLDLSFFLSPFNYFPEDPAMGSRDSVRIEAVDKNNLKRGIKIDKQTFPEKMTCKAPIGNYFEYILKRPNVIFDIQ | ||||||
Disulfide bond | 199↔203 | |||||
Sequence: CGNRC | ||||||
Disulfide bond | 405↔432 | |||||
Sequence: CPTGATFIDSHILTESSLKPAKLINAFC | ||||||
Modified residue | 475 | 2',4',5'-topaquinone | ||||
Sequence: Y |
Post-translational modification
Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Keywords
- PTM
Expression
Tissue specificity
Prismatic layer of shell (at protein level). Expressed primarily in the mantle with highest level in the mantle edge and lower level in the mantle pallium.
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length781
- Mass (Da)89,950
- Last updated2012-03-21 v1
- Checksum49A8CBC587935AF0
Keywords
- Technical term