O23349 · AO1_ARATH
- ProteinPrimary amine oxidase 1
- GeneAO1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids650 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Oxidizes preferentially the aliphatic diamine putrescine with production of the corresponding aldehyde, ammonia and hydrogen peroxide. May be involved in the regulation of developmental programmed cell death (PCD) in both vascular tissue and the root cap (PubMed:9681017).
Required for jasmonic acid-(MeJA) mediated early protoxylem differentiation associated with putrescine levels reduction and H2O2 accumulation in roots (PubMed:25883242).
Required for jasmonic acid-(MeJA) mediated early protoxylem differentiation associated with putrescine levels reduction and H2O2 accumulation in roots (PubMed:25883242).
Catalytic activity
- a primary methyl amine + H2O + O2 = an aldehyde + H2O2 + NH4+
Cofactor
Protein has several cofactor binding sites:
Note: Contains 1 topaquinone per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )
Note: Binds 1 copper ion per subunit (By similarity).
Can also use zinc ion as cofactor (By similarity).
Can also use zinc ion as cofactor (By similarity).
Note: Binds 1 Mn2+ ion per subunit.
Activity regulation
Repressed by semi-carbazide, a specific and irreversible inhibitor of copper amine oxidases.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 308-319 | substrate | ||||
Sequence: FMDIGEFGFGRS | ||||||
Active site | 310 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 395-400 | substrate | ||||
Sequence: LGNYDY | ||||||
Active site | 398 | Schiff-base intermediate with substrate; via topaquinone | ||||
Sequence: Y | ||||||
Binding site | 453 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 455 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 462 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 464 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 607 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 608 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 618 | Cu cation (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | aliphatic amine oxidase activity | |
Molecular Function | copper ion binding | |
Molecular Function | primary amine oxidase activity | |
Molecular Function | quinone binding | |
Biological Process | amine metabolic process | |
Biological Process | apoptotic process | |
Biological Process | jasmonic acid mediated signaling pathway | |
Biological Process | protoxylem development | |
Biological Process | regulation of programmed cell death | |
Biological Process | response to jasmonic acid |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePrimary amine oxidase 1
- EC number
- Short namesAtAO1
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionO23349
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Impaired sensitivity to jasmonic acid (MeJA).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 101 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, glycosylation, chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MNTSILAILFLIQCVFTLG | ||||||
Glycosylation | 2 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_5008172703 | 20-650 | Primary amine oxidase 1 | |||
Sequence: LHFHPLDPLTPQEINKTSFIVKKSHLGNLKDLTFHYLDLEEPNKSHVLQWLSPNPSKKPPPPRRRSFVVVRAGGQTYELIIDLTTSKIASSRIYTGHGFPSFTFIELFKASKLPLTYPPFKKSILDRSLNISEVSCIPFTVGWYGETTTRRELKASCFYRDGSVNVFTRPIEGITVTIDVDSMQVIKYSDRFRKPIPDKEGNDFRTKHRPFPFFCNVSDTGFKILGNRVKWANWKFHVGFTARAGVTISTASVLDPRTKRFRRVMYRGHVSETFVPYMDPTYEWYYRTFMDIGEFGFGRSAVNLQPLIDCPQNAAFLDGHVAGPDGTAQKMTNVMCVFEKNGYGASFRHTEINVPGQVITSGEAEISLVVRMVATLGNYDYIVDWEFKKNGAIRVGVDLTGVLEVKATSYTSNDQITENVYGTLVAKNTIAVNHDHYLTYYLDLDVDGNGNSLVKAKLKTVRVTEVNKTSSRRKSYWTVVKETAKTEADGRVRLGSDPVELLIVNPNKKTKIGNTVGYRLIPEHLQATSLLTDDDYPELRAGYTKYPVWVTAYDRSERWAGGFYSDRSRGDDGLAVWSSRNREIENKDIVMWYNVGFHHIPYQEDFPVMPTLHGGFTLRPSNFFDNDPLIG | ||||||
Glycosylation | 34 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 62 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 149 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 155↔176 | |||||
Sequence: CIPFTVGWYGETTTRRELKASC | ||||||
Glycosylation | 235 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 329↔355 | |||||
Sequence: CPQNAAFLDGHVAGPDGTAQKMTNVMC | ||||||
Modified residue | 398 | 2',4',5'-topaquinone | ||||
Sequence: Y | ||||||
Glycosylation | 486 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the vascular tissues at the division/differentiation transition zone.
Induction
Induced by jasmonic acid (MeJA) in vascular tissues, especially at the transition and elongation zones.
Developmental stage
Levels peak 3-4 days after germination. Expressed following temporally and spatially discrete patterns of gene expression in lateral root cap cells, vascular tissue of roots, developing leaves, the hypocotyl, and in the style/stigmatal tissue (PubMed:9681017).
Expressed at the early stages of vascular tissue differentiation in roots; strong accumulation in the protoxylem at the transition, elongation, and maturation zones (PubMed:25883242).
Accumulates in developing tracheary elements before lignification. Present in cells destined to undergo programmed cell death (PCD) in both vascular tissue and the root cap. In flowers, restricted spatial and temporal distribution; at stage 11-13, after papillae formation, accumulates in tracheary elements of style and stigmate (PubMed:9681017).
Expressed at the early stages of vascular tissue differentiation in roots; strong accumulation in the protoxylem at the transition, elongation, and maturation zones (PubMed:25883242).
Accumulates in developing tracheary elements before lignification. Present in cells destined to undergo programmed cell death (PCD) in both vascular tissue and the root cap. In flowers, restricted spatial and temporal distribution; at stage 11-13, after papillae formation, accumulates in tracheary elements of style and stigmate (PubMed:9681017).
Gene expression databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length650
- Mass (Da)73,783
- Last updated1998-01-01 v1
- Checksum28741CEB3A43FF5D
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 103 | in Ref. 1; AAB87690 | ||||
Sequence: T → I | ||||||
Sequence conflict | 195 | in Ref. 1; AAB87690 | ||||
Sequence: V → I | ||||||
Sequence conflict | 205 | in Ref. 1; AAB87690 | ||||
Sequence: I → V | ||||||
Sequence conflict | 215-217 | in Ref. 1; AAB87690 | ||||
Sequence: IPD → LPE | ||||||
Sequence conflict | 225-233 | in Ref. 1; AAB87690 | ||||
Sequence: TKHRPFPFF → KKHKPFPFS | ||||||
Sequence conflict | 336 | in Ref. 1; AAB87690 | ||||
Sequence: L → F | ||||||
Sequence conflict | 382 | in Ref. 1; AAB87690 | ||||
Sequence: E → A | ||||||
Sequence conflict | 409 | in Ref. 1; AAB87690 | ||||
Sequence: N → S | ||||||
Sequence conflict | 433 | in Ref. 1; AAB87690 | ||||
Sequence: D → E | ||||||
Sequence conflict | 443 | in Ref. 1; AAB87690 | ||||
Sequence: L → Q | ||||||
Sequence conflict | 484 | in Ref. 1; AAB87690 | ||||
Sequence: E → D | ||||||
Sequence conflict | 516 | in Ref. 1; AAB87690 | ||||
Sequence: D → E | ||||||
Sequence conflict | 545 | in Ref. 1; AAB87690 | ||||
Sequence: Q → P | ||||||
Sequence conflict | 558 | in Ref. 1; AAB87690 | ||||
Sequence: L → I |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF034579 EMBL· GenBank· DDBJ | AAB87690.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
Z97337 EMBL· GenBank· DDBJ | CAB10273.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL161540 EMBL· GenBank· DDBJ | CAB78536.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE83525.1 EMBL· GenBank· DDBJ | Genomic DNA |