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Protein

Phenylethylamine oxidase

Gene
N/A
Organism
Arthrobacter globiformis
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 sitei298 – 2981Proton acceptorBy similarity
Active sitei382 – 3821Schiff-base intermediate with substrate; via topaquinoneBy similarity
Metal bindingi431 – 4311Copper; via tele nitrogenCombined sources1 Publication
Metal bindingi433 – 4331Copper; via tele nitrogenCombined sources1 Publication
Metal bindingi592 – 5921Copper; via pros nitrogenCombined sources1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi382 – 3821Y → F: Loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22PRO_0000035681
Chaini3 – 638636Phenylethylamine oxidasePRO_0000035682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi317 ↔ 343Combined sources1 Publication
Modified residuei382 – 38212',4',5'-topaquinone

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, TPQ

Expressioni

Inductioni

By phenethylamine.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
638
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 2913Combined sources
Beta strandi32 – 343Combined sources
Beta strandi37 – 448Combined sources
Beta strandi52 – 554Combined sources
Beta strandi59 – 668Combined sources
Beta strandi73 – 786Combined sources
Turni79 – 824Combined sources
Beta strandi83 – 897Combined sources
Helixi92 – 954Combined sources
Helixi102 – 1043Combined sources
Helixi107 – 1126Combined sources
Helixi116 – 1249Combined sources
Helixi129 – 1313Combined sources
Beta strandi132 – 1387Combined sources
Beta strandi141 – 1433Combined sources
Helixi145 – 1473Combined sources
Beta strandi152 – 1554Combined sources
Beta strandi157 – 1593Combined sources
Helixi167 – 1693Combined sources
Beta strandi175 – 1806Combined sources
Turni181 – 1844Combined sources
Beta strandi185 – 1917Combined sources
Helixi207 – 2104Combined sources
Beta strandi221 – 2233Combined sources
Beta strandi231 – 2333Combined sources
Turni234 – 2363Combined sources
Beta strandi237 – 2404Combined sources
Beta strandi243 – 2508Combined sources
Turni251 – 2533Combined sources
Beta strandi254 – 26411Combined sources
Beta strandi267 – 28418Combined sources
Turni289 – 2935Combined sources
Beta strandi295 – 2973Combined sources
Helixi298 – 3025Combined sources
Helixi304 – 3074Combined sources
Turni313 – 3153Combined sources
Beta strandi322 – 3243Combined sources
Beta strandi327 – 3293Combined sources
Beta strandi335 – 3373Combined sources
Beta strandi342 – 35615Combined sources
Turni358 – 3603Combined sources
Beta strandi363 – 37917Combined sources
Beta strandi382 – 39110Combined sources
Beta strandi396 – 4049Combined sources
Beta strandi417 – 4237Combined sources
Beta strandi426 – 4294Combined sources
Beta strandi431 – 44111Combined sources
Beta strandi448 – 45710Combined sources
Turni462 – 4643Combined sources
Beta strandi470 – 4767Combined sources
Helixi480 – 4823Combined sources
Helixi489 – 4913Combined sources
Beta strandi494 – 50310Combined sources
Beta strandi509 – 5168Combined sources
Helixi529 – 5335Combined sources
Helixi535 – 5384Combined sources
Beta strandi539 – 5457Combined sources
Beta strandi563 – 5664Combined sources
Helixi567 – 5715Combined sources
Beta strandi578 – 5803Combined sources
Beta strandi582 – 59211Combined sources
Helixi596 – 5983Combined sources
Beta strandi599 – 61517Combined sources
Beta strandi617 – 6193Combined sources
Turni621 – 6244Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 9-628.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46881.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni296 – 30712Substrate bindingBy similarityAdd
BLAST
Regioni379 – 3846Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

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.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
PANTHERiPTHR10638. PTHR10638. 1 hit.
PfamiPF01179. Cu_amine_oxid. 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.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]

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.

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
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. Positions 9-628.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.4.3.21. 444.

Miscellaneous databases

EvolutionaryTraceiP46881.

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.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
PANTHERiPTHR10638. PTHR10638. 1 hit.
PfamiPF01179. Cu_amine_oxid. 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.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequencing of phenylethylamine oxidase from Arthrobacter globiformis and implication of Tyr-382 as the precursor to its covalently bound quinone cofactor."
    Tanizawa K., Matsuzaki R., Shimizu E., Yorifuji T., Fukui T.
    Biochem. Biophys. Res. Commun. 199:1096-1102(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 8010 / DSM 20124 / JCM 1332 / NBRC 12137 / NCIMB 8907.
  2. "Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone."
    Wilce M.C., Dooley D.M., Freeman H.C., Guss J.M., Matsunami H., McIntire W.S., Ruggiero C.E., Tanizawa K., Yamaguchi H.
    Biochemistry 36:16116-16133(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH COPPER AND SUBSTRATE, TOPAQUINONE AT TYR-382, SUBUNIT, DISULFIDE BOND.

Entry informationi

Entry nameiPAOX_ARTGO
AccessioniPrimary (citable) accession number: P46881
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 20, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.