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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)DescriptionActionsGraphical viewLength
Active sitei325Proton acceptorBy similarity1
Active sitei412Schiff-base intermediate with substrate; via topaquinoneBy similarity1
Metal bindingi467Copper; via tele nitrogenCombined sources1 Publication1
Metal bindingi469Copper; via tele nitrogenCombined sources1 Publication1
Metal bindingi476ManganeseCombined sources1 Publication1
Metal bindingi477Manganese; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi478ManganeseCombined sources1 Publication1
Metal bindingi617ManganeseCombined sources1 Publication1
Metal bindingi618Manganese; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi628Copper; via pros nitrogenCombined sources1 Publication1

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 databases

ChEMBLiCHEMBL5534.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000003568026 – 674Primary amine oxidaseAdd BLAST649

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi156N-linked (GlcNAc...)Combined sources1 Publication1
Disulfide bondi162 ↔ 183Combined sources1 Publication
Disulfide bondi344 ↔ 370Combined sources1 Publication
Glycosylationi389N-linked (GlcNAc...)Curated1
Modified residuei4122',4',5'-topaquinoneCombined sources1 Publication1
Glycosylationi583N-linked (GlcNAc...)Combined sources1

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 databases

BindingDBiQ43077.

Structurei

Secondary structure

1674
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi40 – 53Combined sources14
Turni56 – 58Combined sources3
Beta strandi61 – 68Combined sources8
Helixi73 – 81Combined sources9
Helixi83 – 85Combined sources3
Beta strandi91 – 98Combined sources8
Beta strandi101 – 108Combined sources8
Turni109 – 112Combined sources4
Beta strandi113 – 119Combined sources7
Helixi130 – 136Combined sources7
Helixi137 – 142Combined sources6
Helixi144 – 152Combined sources9
Helixi157 – 159Combined sources3
Beta strandi160 – 165Combined sources6
Beta strandi178 – 185Combined sources8
Helixi192 – 194Combined sources3
Beta strandi195 – 197Combined sources3
Beta strandi199 – 205Combined sources7
Turni206 – 209Combined sources4
Beta strandi210 – 216Combined sources7
Helixi232 – 234Combined sources3
Beta strandi246 – 249Combined sources4
Beta strandi257 – 259Combined sources3
Beta strandi262 – 265Combined sources4
Beta strandi268 – 275Combined sources8
Turni276 – 278Combined sources3
Beta strandi279 – 289Combined sources11
Turni290 – 293Combined sources4
Beta strandi294 – 311Combined sources18
Turni316 – 320Combined sources5
Helixi325 – 329Combined sources5
Turni331 – 334Combined sources4
Turni340 – 342Combined sources3
Beta strandi349 – 356Combined sources8
Beta strandi362 – 384Combined sources23
Beta strandi392 – 409Combined sources18
Beta strandi412 – 420Combined sources9
Beta strandi426 – 434Combined sources9
Beta strandi438 – 440Combined sources3
Helixi446 – 448Combined sources3
Beta strandi454 – 459Combined sources6
Beta strandi462 – 465Combined sources4
Beta strandi467 – 477Combined sources11
Beta strandi484 – 495Combined sources12
Beta strandi498 – 500Combined sources3
Beta strandi504 – 513Combined sources10
Helixi517 – 520Combined sources4
Beta strandi529 – 539Combined sources11
Beta strandi545 – 551Combined sources7
Helixi565 – 569Combined sources5
Helixi571 – 574Combined sources4
Beta strandi576 – 581Combined sources6
Beta strandi599 – 602Combined sources4
Helixi603 – 606Combined sources4
Helixi607 – 609Combined sources3
Beta strandi614 – 616Combined sources3
Beta strandi618 – 628Combined sources11
Helixi632 – 634Combined sources3
Beta strandi635 – 637Combined sources3
Beta strandi641 – 644Combined sources4
Beta strandi646 – 651Combined sources6
Beta strandi653 – 655Combined sources3
Turni657 – 660Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ43077.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni323 – 334Substrate bindingBy similarityAdd BLAST12
Regioni409 – 414Substrate bindingBy similarity6

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KOiK00276.

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.

Genome annotation databases

KEGGiag:AAA62490.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KSIX-ray2.20A/B31-672[»]
1W2ZX-ray2.24A/B/C/D26-674[»]
ProteinModelPortaliQ43077.
SMRiQ43077.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiQ43077.
ChEMBLiCHEMBL5534.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA62490.

Phylogenomic databases

KOiK00276.

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...

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: November 2, 2016
This is version 96 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.