Reviewed, UniProtKB/Swiss-Prot Q12556 (AMO1_ASPNG)

Names and origin

Protein names

Recommended name:
    Copper amine oxidase 1
    EC=1.4.3.22

Gene names

Name:

AO-I

Organism

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	671 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2.
Cofactor	Binds 1 copper ion per dimer. Contains 1 topaquinone per subunit By similarity.
Subunit structure	Homodimer.
Induction	By N-butylamine.
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
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	TPQ
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular amine metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	amine oxidase activity Inferred from electronic annotation. Source: EC copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW quinone binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 671	671	Copper amine oxidase 1		PRO_0000064110
Regions
	Region	3 – 106	104	N2
	Region	107 – 211	105	N3
Sites
	Active site	321	1	Proton acceptor By similarity
	Active site	405	1	Schiff-base intermediate with substrate; via topaquinone By similarity
	Metal binding	455	1	Copper By similarity
	Metal binding	457	1	Copper By similarity
	Metal binding	617	1	Copper By similarity
Amino acid modifications
	Modified residue	405	1	2',4',5'-topaquinone By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q12556-1 [UniParc]. Last modified July 11, 2001. Version 2. Checksum: 7413DF262A1BAE82	FASTA	671	75,303
	10 20 30 40 50 60 MLPHPLAILS EEETNIARNV ILAQHPNTVI DFREIYLSEP PKAQLLEFLA LEHSGRLSPT 70 80 90 100 110 120 SPRPPRLALC QYDVIGNDRI PSFEESVVDV GTRQRVQHRV VGKEHHASLT LSEFDTLVER 130 140 150 160 170 180 CFASPLFQKA LADFDLPEGF EVVIEPWPYG GLDYVEEKRR YFQGLCFATD KRKNNPDANF 190 200 210 220 230 240 YSYPLPLIPV MDALTQEIIR VDRPATGGKG EGLTEQTFKR DIIGHCKDSD YVPELNPGGT 250 260 270 280 290 300 RKDLKPLNVV QPEGPSFRIT EESLVEWQKW RFRVAFNPRE GATIHDVWYD GRSVLYRLSV 310 320 330 340 350 360 SEMTVPYADP RPPFHRKQAF DFGDGGGGNM ANNLSIGCDC LGVIKYFDAV MTGADGSAKK 370 380 390 400 410 420 MPNAICLHEQ DNGIGWKHSN WRTGRAVVTR HRELVVQFII TLANYEYIFA YKFDQSGGIT 430 440 450 460 470 480 VESRATGILN VVNIDAGKVS EYGNVVSGGV LAQNHQHIFC VRIDPAIDGP NNSVQVEESH 490 500 510 520 530 540 PVPMNAVTNP NGNFYKVNTE TMERAGFFDA APELNRTVKM VNPHKKNPIS QKPVGYKFIP 550 560 570 580 590 600 LATQRLLADP NSIQARRAQF AQHHVWVTKY RDGELYAGGR YTLQSQEEIE GVSDAVKRGD 610 620 630 640 650 660 SVVDTDVVVW STFGITHNPR VEDWPVMPVE IFQLMIRPAD FFTANPSLDV PSDKNISSRV 670 VGNDCCRNAH I

References

[1]

"Two distinct quinoprotein amine oxidases are induced by n-butylamine in the mycelia of Aspergillus niger AKU 3302. Purification, characterization, cDNA cloning and sequencing." Frebort I., Tamaki H., Ishida H., Pec P., Luhova L., Tsuno H., Halata M., Asano Y., Kato Y., Matsushita K., Toyama H., Kumagai H., Adachi O. Eur. J. Biochem. 237:255-265(1996) [PubMed: 8620882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-35; 538-565; 570-597 AND 635-654. Strain: AKU 3302 / M-62.

[2]

"Reassessment of the active site and the primary structure of the amine oxidase AO-I from Aspergillus niger AKU 3302." Frebort I., Cernikova V., Hirota S., Yamada M., Adachi O., Pec P. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. Strain: AKU 3302 / M-62.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U31869 mRNA. Translation: AAB03385.2.
PIR	S71320.
3D structure databases
HSSP	HSSP built from PDB template 1A2V based on UniProtKB P12807.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.4.3.6. 277.
Family and domain databases
InterPro	IPR000269. Cu_amine_oxidase. IPR015798. Cu_amine_oxidase_C. IPR015800. Cu_amine_oxidase_N2. IPR015801. Cu_amine_oxidase_N2/3. IPR015802. Cu_amine_oxidase_N3. [Graphical view]
Gene3D	G3DSA:3.10.450.40. CuNH_oxidase. 2 hits. G3DSA:2.70.98.20. Lyase_8_central. 1 hit.
PANTHER	PTHR10638. CuNH_oxidase. 1 hit.
Pfam	PF01179. Cu_amine_oxid. 1 hit. PF02727. Cu_amine_oxidN2. 1 hit. PF02728. Cu_amine_oxidN3. 1 hit. [Graphical view]
PROSITE	PS01164. COPPER_AMINE_OXID_1. 1 hit. PS01165. COPPER_AMINE_OXID_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMO1_ASPNG

Accession

Primary (citable) accession number: Q12556

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 11, 2001
Last modified:	June 16, 2009
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)