Reviewed, UniProtKB/Swiss-Prot Q07121 (AMO1_ARTS1)

Names and origin

Protein names

Recommended name:
    Primary amine oxidase
    EC=1.4.3.21
Alternative name(s):
    Copper amine oxidase
    MAOXI

Gene names

Name:

maoI

Organism

Arthrobacter sp. (strain P1)

Taxonomic identifier

47915 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	648 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The exact function of maoXI is not known.
Catalytic activity	RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.
Cofactor	Binds 1 copper ion per subunit. Contains 1 topaquinone per subunit By similarity.
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
	Propeptide	1 – 9	9	Ref.1		PRO_0000035675
	Chain	10 – 648	639	Primary amine oxidase		PRO_0000035676
Sites
	Active site	301	1	Proton acceptor By similarity
	Active site	385	1	Schiff-base intermediate with substrate; via topaquinone By similarity
	Metal binding	436	1	Copper By similarity
	Metal binding	438	1	Copper By similarity
	Metal binding	595	1	Copper By similarity
Amino acid modifications
	Modified residue	385	1	2',4',5'-topaquinone By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q07121-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: B2F9E267492253B5	FASTA	648	72,761
	10 20 30 40 50 60 MTLNAESEAL VGVSHPLDPL SRVEIARAVA ILKEGPAAAE SFRFISVELR EPSKDDLRAG 70 80 90 100 110 120 VAVAREADAV LVDRAQARSF EAVVDLEAGT VDSWKLLAEN IQPPFMLDEF AECEDACRKD 130 140 150 160 170 180 PEVIAALAKR GLTNLDLVCF EPWSVGYFGE DNEGRRLMRA LVFVRDEADD SPYAHPIENF 190 200 210 220 230 240 IVFYDLNAGK VVRLEDDQAI PVPSARGNYL PKYVGEARTD LKPLNITQPE GASFTVTGNH 250 260 270 280 290 300 VTWADWSFRV GFTPREGLVL HQLKFKDQGV DRPVINRASL SEMVVPYGDT APVQAKKNAF 310 320 330 340 350 360 DSGEYNIGNM ANSLTLGCDC LGEIKYFDGH SVDSHGNPWT IENAICMHEE DDSILWKHFD 370 380 390 400 410 420 FREGTAETRR SRKLVISFIA TVANYEYAFY WHLFLDGSIE FLVKATGILS TAGQLPGEKN 430 440 450 460 470 480 PYGQSLNNDG LYAPIHQHMF NVRMDFELDG VKNAVYEVDM EYPEHNPTGT AFMAVDRLLE 490 500 510 520 530 540 TEQKAIRKTN EAKHRFWKIA NHESKNLVNE PVAYRLIPTN GIQLAARDDA YVSKRAQFAR 550 560 570 580 590 600 NNLWVTAYDR TERFAAGEYP NQATGADDGL HIWTQKDRNI VDTDLVVWYT FGMHHVVRLE 610 620 630 640 DWPVMPRQNI GFMLEPHGFF NQNPTLNLPT STSTTQTGEA DTCCHNGK

References

[1]

"Cloning, sequencing, expression, and regulation of the structural gene for the copper/topa quinone-containing methylamine oxidase from Arthrobacter strain P1, a Gram-positive facultative methylotroph." Zhang X., Fuller J.H., McIntire W.S. J. Bacteriol. 175:5617-5627(1993) [PubMed: 8366046] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 10-54; 358-381 AND 456-466.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L12983 Genomic DNA. Translation: AAA22076.1.
3D structure databases
HSSP	HSSP built from PDB template 1IVW based on UniProtKB P46881.
ModBase	Search...
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMO1_ARTS1

Accession

Primary (citable) accession number: Q07121

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)