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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)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

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)DescriptionActionsGraphical viewLength
Mutagenesisi382Y → F: Loss of activity. 1

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

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

1638
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 29Combined sources13
Beta strandi32 – 34Combined sources3
Beta strandi37 – 44Combined sources8
Beta strandi52 – 55Combined sources4
Beta strandi59 – 66Combined sources8
Beta strandi73 – 78Combined sources6
Turni79 – 82Combined sources4
Beta strandi83 – 89Combined sources7
Helixi92 – 95Combined sources4
Helixi102 – 104Combined sources3
Helixi107 – 112Combined sources6
Helixi116 – 124Combined sources9
Helixi129 – 131Combined sources3
Beta strandi132 – 138Combined sources7
Beta strandi141 – 143Combined sources3
Helixi145 – 147Combined sources3
Beta strandi152 – 155Combined sources4
Beta strandi157 – 159Combined sources3
Helixi167 – 169Combined sources3
Beta strandi175 – 180Combined sources6
Turni181 – 184Combined sources4
Beta strandi185 – 191Combined sources7
Helixi207 – 210Combined sources4
Beta strandi221 – 223Combined sources3
Beta strandi231 – 233Combined sources3
Turni234 – 236Combined sources3
Beta strandi237 – 240Combined sources4
Beta strandi243 – 250Combined sources8
Turni251 – 253Combined sources3
Beta strandi254 – 264Combined sources11
Beta strandi267 – 284Combined sources18
Turni289 – 293Combined sources5
Beta strandi295 – 297Combined sources3
Helixi298 – 302Combined sources5
Helixi304 – 307Combined sources4
Turni313 – 315Combined sources3
Beta strandi322 – 324Combined sources3
Beta strandi327 – 329Combined sources3
Beta strandi335 – 337Combined sources3
Beta strandi342 – 356Combined sources15
Turni358 – 360Combined sources3
Beta strandi363 – 379Combined sources17
Beta strandi382 – 391Combined sources10
Beta strandi396 – 404Combined sources9
Beta strandi417 – 423Combined sources7
Beta strandi426 – 429Combined sources4
Beta strandi431 – 441Combined sources11
Beta strandi448 – 457Combined sources10
Turni462 – 464Combined sources3
Beta strandi470 – 476Combined sources7
Helixi480 – 482Combined sources3
Helixi489 – 491Combined sources3
Beta strandi494 – 503Combined sources10
Beta strandi509 – 516Combined sources8
Helixi529 – 533Combined sources5
Helixi535 – 538Combined sources4
Beta strandi539 – 545Combined sources7
Beta strandi563 – 566Combined sources4
Helixi567 – 571Combined sources5
Beta strandi578 – 580Combined sources3
Beta strandi582 – 592Combined sources11
Helixi596 – 598Combined sources3
Beta strandi599 – 615Combined sources17
Beta strandi617 – 619Combined sources3
Turni621 – 624Combined sources4

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...

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.
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.

Genome annotation databases

KEGGiag:AAA18114.

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...

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.
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...

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: November 2, 2016
This is version 104 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.