NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 10-54; 358-381 AND 456-466.
PubMed=8366046 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang X., Fuller J.H., McIntire W.S.;
"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.";
J. Bacteriol. 175:5617-5627(1993).

Comments

CATALYTIC ACTIVITY: RCH₂NH₂ + H₂O + O₂ = RCHO + NH₃ + H₂O₂.
COFACTOR: Binds 1 copper ion per subunit.
COFACTOR: Contains 1 topaquinone per subunit (By similarity).
SUBUNIT: Homodimer (By similarity).
INDUCTION: By methylamine.
PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue (By similarity).
SIMILARITY: Belongs to the copper/topaquinone 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

L12990; AAA22074.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A48646; A48646.

3D structure databases

HSSP

P46881; 1IVW. [HSSP ENTRY / PDB]

ModBase

Q07123.

Ontologies

GO:0008131;	Molecular function: amine oxidase activity (inferred from electronic annotation from InterPro).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from InterPro).
GO:0048038;	Molecular function: quinone binding (inferred from electronic annotation from InterPro).
GO:0009308;	Biological process: cellular amine metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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 of domain structure.

Gene3D

G3DSA:3.10.450.40; CuNH_oxidase; 2.
G3DSA:2.70.98.20; Lyase_8_central; 1.

PANTHER

PTHR10638; CuNH_oxidase; 1.

Pfam

PF01179; Cu_amine_oxid; 1.
PF02727; Cu_amine_oxidN2; 1.
PF02728; Cu_amine_oxidN3; 1.
Pfam graphical view of domain structure.

PROSITE

PS01164; COPPER_AMINE_OXID_1; 1.
PS01165; COPPER_AMINE_OXID_2; 1.

ProtoNet

Q07123.

Other

UniRef

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

Keywords

Copper; Direct protein sequencing; Metal-binding; Oxidoreductase; TPQ.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`PROPEP`	`1 9`	`9`		`PRO_0000035677`
`CHAIN`	`10 648`	`639`	`Copper methylamine oxidase.`	`PRO_0000035678`
`ACT_SITE`	`301 301`		`Proton acceptor (By similarity).`
`ACT_SITE`	`385 385`		`Schiff-base intermediate with substrate; via topaquinone (By similarity).`
`METAL`	`436 436`		`Copper (By similarity).`
`METAL`	`438 438`		`Copper (By similarity).`
`METAL`	`595 595`		`Copper (By similarity).`
`MOD_RES`	`385 385`		`2',4',5'-topaquinone (By similarity).`

Sequence information

Length: 648 AA [This is the length of the unprocessed precursor]

Molecular weight: 72806 Da [This is the MW of the unprocessed precursor]

CRC64: B2FB2787492253B5 [This is a checksum on the sequence]

        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 DTCCHTDK

Q07123 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