[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=9589594 [NCBI, ExPASy, EBI, Israel, Japan] Cambridge L.M., Lumsden J.M., Sadhigi M., Galloway S.M.; "A ScaI polymorphism at the ovine monoamine oxidase A locus (MAOA)."; Anim. Genet. 28:457-457(1997).

Comments

FUNCTION: Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine (By similarity).
CATALYTIC ACTIVITY: RCH₂NH₂ + H₂O + O₂ = RCHO + NH₃ + H₂O₂.
COFACTOR: FAD.
SUBUNIT: Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer (By similarity).
SUBCELLULAR LOCATION: Mitochondrion outer membrane.
SIMILARITY: Belongs to the flavin monoamine oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF023613; AAC16911.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P27338; 1GOS. [HSSP ENTRY / PDB]

SMR

O18851; 1-46.

ModBase

O18851.

Ontologies

GO:0005741;	Cellular component: mitochondrial outer membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0008131;	Molecular function: amine oxidase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR002937; Amino_oxidase.
Graphical view of domain structure.

Pfam

PF01593; Amino_oxidase; 1.
Pfam graphical view of domain structure.

BLOCKS

O18851.

Phylogenomic databases

HOVERGEN

O18851; -.

Other

ProtoNet

O18851.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Catecholamine metabolism; FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane; Neurotransmitter degradation; Oxidoreductase; Transmembrane.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 >46`	`>46`	`Amine oxidase [flavin-containing] A.`	`PRO_0000099855`
`NON_TER`	`1 1`
`NON_TER`	`46 46`

Sequence information

Length: 46 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 5349 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: FD06EBDEE44F88BA [This is a checksum on the sequence]

        10         20         30         40 
YVISAIPPTL TSKIHFRPEL PSERNQLIQR LPMGAIIKCM MYYKEA

O18851 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools