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Protein

Phenylethylamine oxidase

Gene
N/A
Organism
Arthrobacter globiformis
Status
Reviewed-Annotation score: -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 sitei298Proton acceptorBy similarity1
Active sitei382Schiff-base intermediate with substrate; via topaquinoneBy similarity1
Metal bindingi431Copper; via tele nitrogenCombined sources1 Publication1
Metal bindingi433Copper; via tele nitrogenCombined sources1 Publication1
Metal bindingi592Copper; via pros nitrogenCombined sources1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandCopper, Metal-binding

Enzyme and pathway databases

BRENDAi1.4.3.21 444

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylethylamine oxidase (EC:1.4.3.21By similarity)
Alternative name(s):
Primary amine oxidase
OrganismiArthrobacter globiformis
Taxonomic identifieri1665 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeArthrobacter

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi382Y → F: Loss of activity. 1

Chemistry databases

DrugBankiDB02511 2-Hydroxy-5-({1-[(2-Naphthyloxy)Methyl]-3-Oxoprop-1-Enyl}Amino)Tyrosine
DB02537 2-Hydroxy-5-({1-[(4-Methylphenoxy)Methyl]-3-Oxoprop-1-Enyl}Amino)-L-Tyrosine
DB06988 2-HYDROXY-5-{[(1E)-2-PHENYLETHYLIDENE]AMINO}-L-TYROSINE
DB04334 6-hydroxydopa quinone

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000356811 – 22
ChainiPRO_00000356823 – 638Phenylethylamine oxidaseAdd BLAST636

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi317 ↔ 343Combined sources1 Publication
Modified residuei3822',4',5'-topaquinone1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, TPQ

Proteomic databases

PRIDEiP46881

Expressioni

Inductioni

By phenethylamine.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1638
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP46881
SMRiP46881
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46881

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni296 – 307Substrate bindingBy similarityAdd BLAST12
Regioni379 – 384Substrate bindingBy similarity6

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Phylogenomic databases

KOiK00276

Family and domain databases

Gene3Di2.70.98.20, 1 hit
InterProiView protein in InterPro
IPR000269 Cu_amine_oxidase
IPR015798 Cu_amine_oxidase_C
IPR036460 Cu_amine_oxidase_C_sf
IPR016182 Cu_amine_oxidase_N-reg
IPR015802 Cu_amine_oxidase_N3
PANTHERiPTHR10638 PTHR10638, 1 hit
PfamiView protein in Pfam
PF01179 Cu_amine_oxid, 1 hit
PF02728 Cu_amine_oxidN3, 1 hit
SUPFAMiSSF49998 SSF49998, 1 hit
SSF54416 SSF54416, 2 hits
PROSITEiView protein in PROSITE
PS01164 COPPER_AMINE_OXID_1, 1 hit
PS01165 COPPER_AMINE_OXID_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P46881-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTPSTIQTAS PFRLASAGEI SEVQGILRTA GLLGPEKRIA YLGVLDPARG
60 70 80 90 100
AGSEAEDRRF RVFIHDVSGA RPQEVTVSVT NGTVISAVEL DTAATGELPV
110 120 130 140 150
LEEEFEVVEQ LLATDERWLK ALAARNLDVS KVRVAPLSAG VFEYAEERGR
160 170 180 190 200
RILRGLAFVQ DFPEDSAWAH PVDGLVAYVD VVSKEVTRVI DTGVFPVPAE
210 220 230 240 250
HGNYTDPELT GPLRTTQKPI SITQPEGPSF TVTGGNHIEW EKWSLDVGFD
260 270 280 290 300
VREGVVLHNI AFRDGDRLRP IINRASIAEM VVPYGDPSPI RSWQNYFDTG
310 320 330 340 350
EYLVGQYANS LELGCDCLGD ITYLSPVISD AFGNPREIRN GICMHEEDWG
360 370 380 390 400
ILAKHSDLWS GINYTRRNRR MVISFFTTIG NYDYGFYWYL YLDGTIEFEA
410 420 430 440 450
KATGVVFTSA FPEGGSDNIS QLAPGLGAPF HQHIFSARLD MAIDGFTNRV
460 470 480 490 500
EEEDVVRQTM GPGNERGNAF SRKRTVLTRE SEAVREADAR TGRTWIISNP
510 520 530 540 550
ESKNRLNEPV GYKLHAHNQP TLLADPGSSI ARRAAFATKD LWVTRYADDE
560 570 580 590 600
RYPTGDFVNQ HSGGAGLPSY IAQDRDIDGQ DIVVWHTFGL THFPRVEDWP
610 620 630
IMPVDTVGFK LRPEGFFDRS PVLDVPANPS QSGSHCHG
Length:638
Mass (Da):70,646
Last modified:November 1, 1995 - v1
Checksum:i1800396BA7A983F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03517 Unassigned DNA Translation: AAA18114.1
PIRiJC2139

Genome annotation databases

KEGGiag:AAA18114

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03517 Unassigned DNA Translation: AAA18114.1
PIRiJC2139

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AV4X-ray2.20A1-638[»]
1AVKX-ray2.20A1-638[»]
1AVLX-ray2.80A1-638[»]
1IQXX-ray2.00A/B1-638[»]
1IQYX-ray1.80A/B1-638[»]
1IU7X-ray1.80A/B1-638[»]
1IVUX-ray1.90A/B1-638[»]
1IVVX-ray2.10A/B1-638[»]
1IVWX-ray1.80A/B1-638[»]
1IVXX-ray2.20A/B1-638[»]
1RJOX-ray1.67A3-638[»]
1SIHX-ray1.73A3-638[»]
1SIIX-ray1.70A3-638[»]
1UI7X-ray2.00A/B1-638[»]
1UI8X-ray1.80A/B1-638[»]
1W4NX-ray1.65A/B3-638[»]
1W5ZX-ray1.86A3-638[»]
1W6CX-ray2.20A3-638[»]
1W6GX-ray1.55A3-638[»]
1WMNX-ray1.80A/B1-638[»]
1WMOX-ray1.80A/B1-638[»]
1WMPX-ray2.00A/B1-638[»]
2BT3X-ray1.73A3-638[»]
2CFDX-ray1.60A/B3-638[»]
2CFGX-ray1.55A/B3-638[»]
2CFKX-ray1.80A3-638[»]
2CFLX-ray1.80A3-638[»]
2CFWX-ray1.74A3-638[»]
2CG0X-ray1.80A3-638[»]
2CG1X-ray1.67A3-638[»]
2CWTX-ray1.82A/B1-638[»]
2CWUX-ray1.85A/B1-638[»]
2CWVX-ray1.85A/B1-638[»]
2D1WX-ray1.74A/B1-638[»]
2E2TX-ray2.05A1-638[»]
2E2UX-ray1.68A/B1-628[»]
2E2VX-ray1.80A/B1-628[»]
2YX9X-ray1.68A/B1-638[»]
2ZL8X-ray1.73A/B1-638[»]
3AMOX-ray2.10A/B1-638[»]
3KIIX-ray1.90A/B3-638[»]
3KN4X-ray2.05A3-638[»]
3WA2X-ray1.08X9-629[»]
3WA3X-ray1.55A/B9-629[»]
3X3XX-ray1.57A/B9-628[»]
3X3YX-ray1.50A/B9-628[»]
3X3ZX-ray1.51A/B9-628[»]
3X40X-ray1.85A/B9-628[»]
3X41X-ray1.87A/B9-628[»]
3X42X-ray1.88A/B9-629[»]
ProteinModelPortaliP46881
SMRiP46881
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB02511 2-Hydroxy-5-({1-[(2-Naphthyloxy)Methyl]-3-Oxoprop-1-Enyl}Amino)Tyrosine
DB02537 2-Hydroxy-5-({1-[(4-Methylphenoxy)Methyl]-3-Oxoprop-1-Enyl}Amino)-L-Tyrosine
DB06988 2-HYDROXY-5-{[(1E)-2-PHENYLETHYLIDENE]AMINO}-L-TYROSINE
DB04334 6-hydroxydopa quinone

Proteomic databases

PRIDEiP46881

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA18114

Phylogenomic databases

KOiK00276

Enzyme and pathway databases

BRENDAi1.4.3.21 444

Miscellaneous databases

EvolutionaryTraceiP46881

Family and domain databases

Gene3Di2.70.98.20, 1 hit
InterProiView protein in InterPro
IPR000269 Cu_amine_oxidase
IPR015798 Cu_amine_oxidase_C
IPR036460 Cu_amine_oxidase_C_sf
IPR016182 Cu_amine_oxidase_N-reg
IPR015802 Cu_amine_oxidase_N3
PANTHERiPTHR10638 PTHR10638, 1 hit
PfamiView protein in Pfam
PF01179 Cu_amine_oxid, 1 hit
PF02728 Cu_amine_oxidN3, 1 hit
SUPFAMiSSF49998 SSF49998, 1 hit
SSF54416 SSF54416, 2 hits
PROSITEiView protein in PROSITE
PS01164 COPPER_AMINE_OXID_1, 1 hit
PS01165 COPPER_AMINE_OXID_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPAOX_ARTGO
AccessioniPrimary (citable) accession number: P46881
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 108 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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