P80695 (AMO_KLEOX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Primary amine oxidase
EC=1.4.3.21

Alternative name(s):
Monamine oxidase
Tyramine oxidase

Gene names

Name:	maoA
Synonyms:	tynA

Organism

Klebsiella oxytoca

Taxonomic identifier

571 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella

Protein attributes

Sequence length	56 AA.
Sequence status	Fragments.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Active on tyramine, tryptamine, beta-phenethylamine and dopamine.
Catalytic activity	RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.
Cofactor	Binds 1 copper ion per subunit. Contains 1 topaquinone per subunit By similarity.
Subunit structure	Homodimer.
Subcellular location	Periplasm.
Post-translational modification	Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue By similarity.
Sequence similarities	Belongs to the copper/topaquinone oxidase family.

Ontologies

Keywords
Biological process	Catecholamine metabolism
Cellular component	Periplasm
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	TPQ
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	catecholamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aliphatic-amine oxidase activity Inferred from electronic annotation. Source: EC aminoacetone:oxygen oxidoreductase(deaminating) activity Inferred from electronic annotation. Source: EC copper ion binding Inferred from electronic annotation. Source: InterPro phenethylamine:oxygen oxidoreductase (deaminating) activity Inferred from electronic annotation. Source: EC primary amine oxidase activity Inferred from electronic annotation. Source: EC quinone binding Inferred from electronic annotation. Source: InterPro tryptamine:oxygen oxidoreductase (deaminating) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›56	›56	Primary amine oxidase		PRO_0000064108
Experimental info
	Non-adjacent residues	20 – 21	2
	Non-terminal residue	56	1

Sequences

	Sequence		Length	Mass (Da)
	P80695 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 69D96CBC32561840	FASTA	56	6,443
	10 20 30 40 50 HGGEAHMVPM DKTLQDFGAD DKQLWVTRYH PTERFPEGKY PNRSIHDTGL GQYAKD

References

[1]	"Distribution of amine oxidases and amine dehydrogenases in bacteria grown on primary amines and characterization of the amine oxidase from Klebsiella oxytoca." Hacisalihoglu A., Jongejan J.A., Duine J.A. Microbiology 143:505-512(1997) [PubMed: 9043125] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: ATCC 8724 / LMD 72.65.
+	Additional computationally mapped references.

Cross-references

3D structure databases
ProteinModelPortal	P80695.
SMR	P80695. Positions 21-56.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	1.4.3.6. 2811.
Family and domain databases
InterPro	IPR015798. Cu_amine_oxidase_C. [Graphical view]
Gene3D	G3DSA:2.70.98.20. Lyase_8_central. 1 hit.
Pfam	PF01179. Cu_amine_oxid. 1 hit. [Graphical view]
PROSITE	PS01164. COPPER_AMINE_OXID_1. Partial match. PS01165. COPPER_AMINE_OXID_2. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMO_KLEOX

Accession

Primary (citable) accession number: P80695

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 28, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program