Peroxisomal primary amine oxidase - Pichia angusta (Yeast)

Names and origin

Protein names

Recommended name:
    Peroxisomal primary amine oxidase
    EC=1.4.3.21
Alternative name(s):
    Copper amine oxidase
    Methylamine oxidase

Gene names

Name:

AMO

Organism

Pichia angusta (Yeast) (Hansenula polymorpha)

Taxonomic identifier

4905 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Pichia

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Protein attributes

Sequence length	692 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	RCH₂NH₂ + H₂O + O₂ = RCHO + NH₃ + H₂O₂.
Cofactor	Binds 1 copper ion per subunit. Ref.2 Contains 1 topaquinone per subunit. Ref.2
Subunit structure	Homodimer. Ref.2 Ref.3
Subcellular location	Peroxisome.
Induction	By methylamine.
Post-translational modification	Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Sequence similarities	Belongs to the copper/topaquinone oxidase family.

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Ontologies

Keywords
Cellular component	Peroxisome
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein TPQ
Technical term	3D-structure 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
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 692

692

Peroxisomal primary amine oxidase

PRO_0000064106

Sites

Active site

319

1

Proton acceptor Ref.3

Active site

405

1

Schiff-base intermediate with substrate; via topaquinone By similarity

Metal binding

456

1

Copper

Metal binding

458

1

Copper

Metal binding

624

1

Copper

Amino acid modifications

Modified residue

405

1

2',4',5'-topaquinone

Glycosylation

243

1

N-linked (GlcNAc...) Ref.3

Disulfide bond

338 ↔ 364

Experimental info

Mutagenesis

319

1

D → E: Strongly reduced activity. Ref.3

Mutagenesis

319

1

D → N: Loss of activity. Ref.3

Secondary structure

1

.

692

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P12807-1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 65B13F0EF5656027
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FASTA

692

77,534

        10         20         30         40         50         60 
MERLRQIASQ ATAASAAPAR PAHPLDPLST AEIKAATNTV KSYFAGKKIS FNTVTLREPA 

        70         80         90        100        110        120 
RKAYIQWKEQ GGPLPPRLAY YVILEAGKPG VKEGLVDLAS LSVIETRALE TVQPILTVED 

       130        140        150        160        170        180 
LCSTEEVIRN DPAVIEQCVL SGIPANEMHK VYCDPWTIGY DERWGTGKRL QQALVYYRSD 

       190        200        210        220        230        240 
EDDSQYSHPL DFCPIVDTEE KKVIFIDIPN RRRKVSKHKH ANFYPKHMIE KVGAMRPEAP 

       250        260        270        280        290        300 
PINVTQPEGV SFKMTGNVME WSNFKFHIGF NYREGIVLSD VSYNDHGNVR PIFHRISLSE 

       310        320        330        340        350        360 
MIVPYGSPEF PHQRKHALDI GEYGAGYMTN PLSLGCDCKG VIHYLDAHFS DRAGDPITVK 

       370        380        390        400        410        420 
NAVCIHEEDD GLLFKHSDFR DNFATSLVTR ATKLVVSQIF TAANYEYCLY WVFMQDGAIR 

       430        440        450        460        470        480 
LDIRLTGILN TYILGDDEEA GPWGTRVYPN VNAHNHQHLF SLRIDPRIDG DGNSAAACDA 

       490        500        510        520        530        540 
KSSPYPLGSP ENMYGNAFYS EKTTFKTVKD SLTNYESATG RSWDIFNPNK VNPYSGKPPS 

       550        560        570        580        590        600 
YKLVSTQCPP LLAKEGSLVA KRAPWASHSV NVVPYKDNRL YPSGDHVPQW SGDGVRGMRE 

       610        620        630        640        650        660 
WIGDGSENID NTDILFFHTF GITHFPAPED FPLMPAEPIT LMLRPRHFFT ENPGLDIQPS 

       670        680        690 
YAMTTSEAKR AVHKETKDKT SRLAFEGSCC GK

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References

[1]	"Cloning and sequencing of the peroxisomal amine oxidase gene from Hansenula polymorpha." Bruinenberg P.G., Evers M., Waterham H.R., Kuipers J., Arnberg A.C., Ab G. Biochim. Biophys. Acta 1008:157-167(1989) [PubMed: 2500147] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 34438 / CBS 4732 / DSM 70277 / IFO 1476 / NRRL Y-5445.
[2]	"Limited proteolysis of Hansenula polymorpha yeast amine oxidase: isolation of a C-terminal fragment containing both a copper and quino-cofactor." Plastino J., Klinman J.P. FEBS Lett. 371:276-278(1995) [PubMed: 7556609] [Abstract] Cited for: PROTEIN SEQUENCE OF 231-238, COFACTOR, SUBUNIT.
[3]	"Copper amine oxidase from Hansenula polymorpha: the crystal structure determined at 2.4-A resolution reveals the active conformation." Li R., Klinman J.P., Mathews F.S. Structure 6:293-307(1998) [PubMed: 9551552] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH COPPER IONS, GLYCOSYLATION AT ASN-243, MUTAGENESIS OF ASP-319, ACTIVE SITE, SUBUNIT.
[4]	"Crystal structure at 2.5 A resolution of zinc-substituted copper amine oxidase of Hansenula polymorpha expressed in Escherichia coli." Chen Z.-W., Schwartz B., Williams N.K., Li R., Klinman J.P., Mathews F.S. Biochemistry 39:9709-9717(2000) [PubMed: 10933787] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 17-672 IN COMPLEX WITH ZINC IONS.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X15111 Genomic DNA. Translation: CAA33209.1.

PIR

S04963.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A2V	X-ray	2.40	A/B/C/D/E/F	18-672	[»]
1EKM	X-ray	2.50	A/B/C	17-672	[»]
2OOV	X-ray	1.70	A/B	13-672	[»]
			C/D/E/F	13-672	[»]
2OQE	X-ray	1.60	A/B	13-672	[»]
			C/D/E/F	13-672	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.4.3.6. 276392.

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...

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Entry information

Entry name

AMO_PICAN

Accession

Primary (citable) accession number: P12807

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	June 16, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families