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Protein

Primary amine oxidase

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.By similarity

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei325 – 3251Proton acceptorBy similarity
Active sitei412 – 4121Schiff-base intermediate with substrate; via topaquinoneBy similarity
Metal bindingi467 – 4671Copper; via tele nitrogenCombined sources1 Publication
Metal bindingi469 – 4691Copper; via tele nitrogenCombined sources1 Publication
Metal bindingi476 – 4761ManganeseCombined sources1 Publication
Metal bindingi477 – 4771Manganese; via carbonyl oxygenCombined sources1 Publication
Metal bindingi478 – 4781ManganeseCombined sources1 Publication
Metal bindingi617 – 6171ManganeseCombined sources1 Publication
Metal bindingi618 – 6181Manganese; via carbonyl oxygenCombined sources1 Publication
Metal bindingi628 – 6281Copper; via pros nitrogenCombined sources1 Publication

GO - Molecular functioni

GO - Biological processi

  • amine metabolic process Source: InterPro
  • cellular response to azide Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi1.4.3.21. 4872.
SABIO-RKQ43077.

Names & Taxonomyi

Protein namesi
Recommended name:
Primary amine oxidase (EC:1.4.3.21By similarity)
Alternative name(s):
Amine oxidase [copper-containing]
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5534.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 674649Primary amine oxidasePRO_0000035680Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi156 – 1561N-linked (GlcNAc...)Combined sources1 Publication
Disulfide bondi162 ↔ 183Combined sources1 Publication
Disulfide bondi344 ↔ 370Combined sources1 Publication
Glycosylationi389 – 3891N-linked (GlcNAc...)Curated
Modified residuei412 – 41212',4',5'-topaquinoneCombined sources1 Publication
Glycosylationi583 – 5831N-linked (GlcNAc...)Combined sources

Post-translational modificationi

Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, TPQ

Interactioni

Subunit structurei

Homodimer.1 Publication

Chemistry

BindingDBiQ43077.

Structurei

Secondary structure

1
674
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 5314Combined sources
Turni56 – 583Combined sources
Beta strandi61 – 688Combined sources
Helixi73 – 819Combined sources
Helixi83 – 853Combined sources
Beta strandi91 – 988Combined sources
Beta strandi101 – 1088Combined sources
Turni109 – 1124Combined sources
Beta strandi113 – 1197Combined sources
Helixi130 – 1367Combined sources
Helixi137 – 1426Combined sources
Helixi144 – 1529Combined sources
Helixi157 – 1593Combined sources
Beta strandi160 – 1656Combined sources
Beta strandi178 – 1858Combined sources
Helixi192 – 1943Combined sources
Beta strandi195 – 1973Combined sources
Beta strandi199 – 2057Combined sources
Turni206 – 2094Combined sources
Beta strandi210 – 2167Combined sources
Helixi232 – 2343Combined sources
Beta strandi246 – 2494Combined sources
Beta strandi257 – 2593Combined sources
Beta strandi262 – 2654Combined sources
Beta strandi268 – 2758Combined sources
Turni276 – 2783Combined sources
Beta strandi279 – 28911Combined sources
Turni290 – 2934Combined sources
Beta strandi294 – 31118Combined sources
Turni316 – 3205Combined sources
Helixi325 – 3295Combined sources
Turni331 – 3344Combined sources
Turni340 – 3423Combined sources
Beta strandi349 – 3568Combined sources
Beta strandi362 – 38423Combined sources
Beta strandi392 – 40918Combined sources
Beta strandi412 – 4209Combined sources
Beta strandi426 – 4349Combined sources
Beta strandi438 – 4403Combined sources
Helixi446 – 4483Combined sources
Beta strandi454 – 4596Combined sources
Beta strandi462 – 4654Combined sources
Beta strandi467 – 47711Combined sources
Beta strandi484 – 49512Combined sources
Beta strandi498 – 5003Combined sources
Beta strandi504 – 51310Combined sources
Helixi517 – 5204Combined sources
Beta strandi529 – 53911Combined sources
Beta strandi545 – 5517Combined sources
Helixi565 – 5695Combined sources
Helixi571 – 5744Combined sources
Beta strandi576 – 5816Combined sources
Beta strandi599 – 6024Combined sources
Helixi603 – 6064Combined sources
Helixi607 – 6093Combined sources
Beta strandi614 – 6163Combined sources
Beta strandi618 – 62811Combined sources
Helixi632 – 6343Combined sources
Beta strandi635 – 6373Combined sources
Beta strandi641 – 6444Combined sources
Beta strandi646 – 6516Combined sources
Beta strandi653 – 6553Combined sources
Turni657 – 6604Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KSIX-ray2.20A/B31-672[»]
1W2ZX-ray2.24A/B/C/D26-674[»]
ProteinModelPortaliQ43077.
SMRiQ43077. Positions 31-672.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ43077.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni323 – 33412Substrate bindingBy similarityAdd
BLAST
Regioni409 – 4146Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.70.98.20. 1 hit.
InterProiIPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
PANTHERiPTHR10638. PTHR10638. 1 hit.
PfamiPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
SUPFAMiSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEiPS01164. COPPER_AMINE_OXID_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q43077-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTTTMRLA LFSVLTLLSF HAVVSVTPLH VQHPLDPLTK EEFLAVQTIV
60 70 80 90 100
QNKYPISNNR LAFHYIGLDD PEKDHVLRYE THPTLVSIPR KIFVVAIINS
110 120 130 140 150
QTHEILINLR IRSIVSDNIH NGYGFPILSV DEQSLAIKLP LKYPPFIDSV
160 170 180 190 200
KKRGLNLSEI VCSSFTMGWF GEEKNVRTVR LDCFMKESTV NIYVRPITGI
210 220 230 240 250
TIVADLDLMK IVEYHDRDIE AVPTAENTEY QVSKQSPPFG PKQHSLTSHQ
260 270 280 290 300
PQGPGFQING HSVSWANWKF HIGFDVRAGI VISLASIYDL EKHKSRRVLY
310 320 330 340 350
KGYISELFVP YQDPTEEFYF KTFFDSGEFG FGLSTVSLIP NRDCPPHAQF
360 370 380 390 400
IDTYVHSANG TPILLKNAIC VFEQYGNIMW RHTENGIPNE SIEESRTEVN
410 420 430 440 450
LIVRTIVTVG NYDNVIDWEF KASGSIKPSI ALSGILEIKG TNIKHKDEIK
460 470 480 490 500
EDLHGKLVSA NSIGIYHDHF YIYYLDFDID GTHNSFEKTS LKTVRIKDGS
510 520 530 540 550
SKRKSYWTTE TQTAKTESDA KITIGLAPAE LVVVNPNIKT AVGNEVGYRL
560 570 580 590 600
IPAIPAHPLL TEDDYPQIRG AFTNYNVWVT AYNRTEKWAG GLYVDHSRGD
610 620 630 640 650
DTLAVWTKQN REIVNKDIVM WHVVGIHHVP AQEDFPIMPL LSTSFELRPT
660 670
NFFERNPVLK TLSPRDVAWP GCSN
Length:674
Mass (Da):76,358
Last modified:November 1, 1996 - v1
Checksum:i30735390071DD18E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39931 Genomic DNA. Translation: AAA62490.1.
PIRiA57327. C44239.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39931 Genomic DNA. Translation: AAA62490.1.
PIRiA57327. C44239.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KSIX-ray2.20A/B31-672[»]
1W2ZX-ray2.24A/B/C/D26-674[»]
ProteinModelPortaliQ43077.
SMRiQ43077. Positions 31-672.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ43077.
ChEMBLiCHEMBL5534.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.4.3.21. 4872.
SABIO-RKQ43077.

Miscellaneous databases

EvolutionaryTraceiQ43077.

Family and domain databases

Gene3Di2.70.98.20. 1 hit.
InterProiIPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
PANTHERiPTHR10638. PTHR10638. 1 hit.
PfamiPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
SUPFAMiSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEiPS01164. COPPER_AMINE_OXID_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 31-672 IN COMPLEX WITH COPPER AND MANGANESE, TOPAQUINONE AT TYR-412, GLYCOSYLATION AT ASN-156, DISULFIDE BOND, SUBUNIT.
    Tissue: Seedling.

Entry informationi

Entry nameiAMO_PEA
AccessioniPrimary (citable) accession number: Q43077
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 20, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.