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Reviewed, UniProtKB/Swiss-Prot Q43077 (AMO_PEA)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Primary amine oxidase
    EC=1.4.3.21
Alternative name(s):
    Amine oxidase [copper-containing]
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

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Protein attributes

Sequence length674 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Binds 1 manganese ion per subunit.

Contains 1 topaquinone per subunit.

Subunit structure

Homodimer.

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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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 674649Primary amine oxidase
PRO_0000035680

Sites

Active site3251Proton acceptor By similarity
Active site4121Schiff-base intermediate with substrate; via topaquinone By similarity
Metal binding4671Copper
Metal binding4691Copper
Metal binding4761Manganese
Metal binding4771Manganese; via carbonyl oxygen
Metal binding4781Manganese
Metal binding6171Manganese
Metal binding6181Manganese; via carbonyl oxygen
Metal binding6281Copper

Amino acid modifications

Modified residue41212',4',5'-topaquinone
Glycosylation1561N-linked (GlcNAc...)
Glycosylation3891N-linked (GlcNAc...) Probable
Glycosylation5831N-linked (GlcNAc...)
Disulfide bond162 ↔ 183
Disulfide bond344 ↔ 370

Secondary structure

1 ................................................................................................................. 674
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q43077-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 30735390071DD18E

FASTA67476,358
        10         20         30         40         50         60 
MASTTTMRLA LFSVLTLLSF HAVVSVTPLH VQHPLDPLTK EEFLAVQTIV QNKYPISNNR 

        70         80         90        100        110        120 
LAFHYIGLDD PEKDHVLRYE THPTLVSIPR KIFVVAIINS QTHEILINLR IRSIVSDNIH 

       130        140        150        160        170        180 
NGYGFPILSV DEQSLAIKLP LKYPPFIDSV KKRGLNLSEI VCSSFTMGWF GEEKNVRTVR 

       190        200        210        220        230        240 
LDCFMKESTV NIYVRPITGI TIVADLDLMK IVEYHDRDIE AVPTAENTEY QVSKQSPPFG 

       250        260        270        280        290        300 
PKQHSLTSHQ PQGPGFQING HSVSWANWKF HIGFDVRAGI VISLASIYDL EKHKSRRVLY 

       310        320        330        340        350        360 
KGYISELFVP YQDPTEEFYF KTFFDSGEFG FGLSTVSLIP NRDCPPHAQF IDTYVHSANG 

       370        380        390        400        410        420 
TPILLKNAIC VFEQYGNIMW RHTENGIPNE SIEESRTEVN LIVRTIVTVG NYDNVIDWEF 

       430        440        450        460        470        480 
KASGSIKPSI ALSGILEIKG TNIKHKDEIK EDLHGKLVSA NSIGIYHDHF YIYYLDFDID 

       490        500        510        520        530        540 
GTHNSFEKTS LKTVRIKDGS SKRKSYWTTE TQTAKTESDA KITIGLAPAE LVVVNPNIKT 

       550        560        570        580        590        600 
AVGNEVGYRL IPAIPAHPLL TEDDYPQIRG AFTNYNVWVT AYNRTEKWAG GLYVDHSRGD 

       610        620        630        640        650        660 
DTLAVWTKQN REIVNKDIVM WHVVGIHHVP AQEDFPIMPL LSTSFELRPT NFFERNPVLK 

       670 
TLSPRDVAWP GCSN

« Hide

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References

[1]Tipping A.J., McPherson M.J.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2-A resolution."
Kumar V., Dooley D.M., Freeman H.C., Guss J.M., Harvey I., McGuirl M.A., Wilce M.C., Zubak V.M.
Structure 4:943-955(1996) [PubMed: 8805580] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Tissue: Seedling.
+Additional computationally mapped references.

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Cross-references

Sequence databases

L39931 Genomic DNA. Translation: AAA62490.1.
PIRC44239. A57327.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1KSIX-ray2.20A/B31-672[»]
1W2ZX-ray2.24A/B/C/D26-674[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.4.3.6. 287.

Family and domain databases

InterProIPR000269. 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]
Gene3DG3DSA:3.10.450.40. CuNH_oxidase. 2 hits.
G3DSA:2.70.98.20. Lyase_8_central. 1 hit.
PANTHERPTHR10638. CuNH_oxidase. 1 hit.
PfamPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
PROSITEPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAMO_PEA
AccessionPrimary (citable) accession number: Q43077
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents