Reviewed, UniProtKB/Swiss-Prot P46881 (PAOX_ARTGO)

Names and origin

Protein names	Recommended name:     Phenylethylamine oxidase     EC=1.4.3.21 Alternative name(s):     Primary amine oxidase
Organism	Arthrobacter globiformis
Taxonomic identifier	1665 [NCBI]
Taxonomic lineage	Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	638 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.
Cofactor	Binds 1 copper ion per subunit. Contains 1 topaquinone per subunit.
Subunit structure	Homodimer.
Induction	By phenethylamine.
Post-translational modification	Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Sequence similarities	Belongs to the copper/topaquinone oxidase family.

Ontologies

Keywords
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond TPQ
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular amine metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	amine oxidase activity Inferred from electronic annotation. Source: EC copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW quinone binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 2

2

PRO_0000035681

Chain

3 – 638

636

Phenylethylamine oxidase

PRO_0000035682

Sites

Active site

298

1

Proton acceptor By similarity

Metal binding

431

1

Copper

Metal binding

433

1

Copper

Metal binding

592

1

Copper

Amino acid modifications

Modified residue

382

1

2',4',5'-topaquinone

Disulfide bond

317 ↔ 343

Experimental info

Mutagenesis

382

1

Y → F: Loss of activity.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

638

Helix Strand Turn

Details...

Helix

17 – 29

13

Beta strand

37 – 44

8

Beta strand

59 – 66

8

Beta strand

73 – 78

6

Turn

79 – 82

4

Beta strand

83 – 89

7

Helix

92 – 95

4

Helix

102 – 112

11

Helix

116 – 123

8

Turn

124 – 126

3

Helix

129 – 131

3

Beta strand

132 – 138

7

Beta strand

152 – 159

8

Helix

167 – 169

3

Beta strand

175 – 180

6

Turn

181 – 184

4

Beta strand

185 – 191

7

Helix

207 – 210

4

Beta strand

221 – 223

3

Beta strand

231 – 233

3

Turn

234 – 236

3

Beta strand

237 – 240

4

Beta strand

243 – 250

8

Turn

251 – 253

3

Beta strand

254 – 264

11

Beta strand

267 – 284

18

Turn

289 – 293

5

Beta strand

295 – 297

3

Helix

298 – 302

5

Helix

304 – 307

4

Turn

314 – 316

3

Beta strand

322 – 324

3

Beta strand

327 – 329

3

Beta strand

335 – 337

3

Beta strand

342 – 356

15

Turn

358 – 360

3

Beta strand

363 – 379

17

Beta strand

382 – 391

10

Beta strand

396 – 404

9

Beta strand

417 – 423

7

Beta strand

426 – 429

4

Beta strand

431 – 441

11

Beta strand

448 – 457

10

Turn

462 – 464

3

Beta strand

470 – 477

8

Helix

480 – 482

3

Helix

489 – 491

3

Beta strand

494 – 503

10

Beta strand

509 – 516

8

Helix

529 – 533

5

Helix

535 – 538

4

Beta strand

539 – 545

7

Helix

567 – 570

4

Helix

571 – 573

3

Beta strand

580 – 592

13

Helix

596 – 598

3

Beta strand

599 – 615

17

Beta strand

617 – 619

3

Turn

621 – 624

4

Sequences

	Sequence		Length	Mass (Da)
	P46881-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 1800396BA7A983F2	FASTA	638	70,646
	10 20 30 40 50 60 MTPSTIQTAS PFRLASAGEI SEVQGILRTA GLLGPEKRIA YLGVLDPARG AGSEAEDRRF 70 80 90 100 110 120 RVFIHDVSGA RPQEVTVSVT NGTVISAVEL DTAATGELPV LEEEFEVVEQ LLATDERWLK 130 140 150 160 170 180 ALAARNLDVS KVRVAPLSAG VFEYAEERGR RILRGLAFVQ DFPEDSAWAH PVDGLVAYVD 190 200 210 220 230 240 VVSKEVTRVI DTGVFPVPAE HGNYTDPELT GPLRTTQKPI SITQPEGPSF TVTGGNHIEW 250 260 270 280 290 300 EKWSLDVGFD VREGVVLHNI AFRDGDRLRP IINRASIAEM VVPYGDPSPI RSWQNYFDTG 310 320 330 340 350 360 EYLVGQYANS LELGCDCLGD ITYLSPVISD AFGNPREIRN GICMHEEDWG ILAKHSDLWS 370 380 390 400 410 420 GINYTRRNRR MVISFFTTIG NYDYGFYWYL YLDGTIEFEA KATGVVFTSA FPEGGSDNIS 430 440 450 460 470 480 QLAPGLGAPF HQHIFSARLD MAIDGFTNRV EEEDVVRQTM GPGNERGNAF SRKRTVLTRE 490 500 510 520 530 540 SEAVREADAR TGRTWIISNP ESKNRLNEPV GYKLHAHNQP TLLADPGSSI ARRAAFATKD 550 560 570 580 590 600 LWVTRYADDE RYPTGDFVNQ HSGGAGLPSY IAQDRDIDGQ DIVVWHTFGL THFPRVEDWP 610 620 630 IMPVDTVGFK LRPEGFFDRS PVLDVPANPS QSGSHCHG

References

[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: 8147851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 8010 / IFO 12137 / DSM 20124 / NCIB 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: 9405045] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 9-628.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U03517 Unassigned DNA. Translation: AAA18114.1.

PIR

JC2139.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AV4	X-ray	2.20	A	1-638	[»]
1AVK	X-ray	2.20	A	1-638	[»]
1AVL	X-ray	2.80	A	1-638	[»]
1IQX	X-ray	2.00	A/B	1-638	[»]
1IQY	X-ray	1.80	A/B	1-638	[»]
1IU7	X-ray	1.80	A/B	1-638	[»]
1IVU	X-ray	1.90	A/B	1-638	[»]
1IVV	X-ray	2.10	A/B	1-638	[»]
1IVW	X-ray	1.80	A/B	1-638	[»]
1IVX	X-ray	2.20	A/B	1-638	[»]
1RJO	X-ray	1.67	A	3-638	[»]
1SIH	X-ray	1.73	A	3-638	[»]
1SII	X-ray	1.70	A	3-638	[»]
1UI7	X-ray	2.00	A/B	1-638	[»]
1UI8	X-ray	1.80	A/B	1-638	[»]
1W4N	X-ray	1.65	A/B	3-638	[»]
1W5Z	X-ray	1.86	A	3-638	[»]
1W6C	X-ray	2.20	A	3-638	[»]
1W6G	X-ray	1.55	A	3-638	[»]
1WMN	X-ray	1.80	A/B	1-638	[»]
1WMO	X-ray	1.80	A/B	1-638	[»]
1WMP	X-ray	2.00	A/B	1-638	[»]
2BT3	X-ray	1.73	A	3-638	[»]
2CFD	X-ray	1.60	A/B	3-638	[»]
2CFG	X-ray	1.55	A/B	3-638	[»]
2CFK	X-ray	1.80	A	3-638	[»]
2CFL	X-ray	1.80	A	3-638	[»]
2CFW	X-ray	1.74	A	3-638	[»]
2CG0	X-ray	1.80	A	3-638	[»]
2CG1	X-ray	1.67	A	3-638	[»]
2CWT	X-ray	1.82	A/B	1-638	[»]
2CWU	X-ray	1.85	A/B	1-638	[»]
2CWV	X-ray	1.85	A/B	1-638	[»]
2D1W	X-ray	1.74	A/B	1-638	[»]
2E2T	X-ray	2.05	A	1-638	[»]
2E2U	X-ray	1.68	A/B	1-628	[»]
2E2V	X-ray	1.80	A/B	1-628	[»]
2YX9	X-ray	1.68	A/B	1-638	[»]
2ZL8	X-ray	1.73	A/B	1-638	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.4.3.6. 1012.

Family and domain databases

InterPro

IPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR015800. Cu_amine_oxidase_N2.
IPR015801. Cu_amine_oxidase_N2/3.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]

Gene3D

G3DSA:3.10.450.40. CuNH_oxidase. 2 hits.
G3DSA:2.70.98.20. Lyase_8_central. 1 hit.

PANTHER

PTHR10638. CuNH_oxidase. 1 hit.

Pfam

PF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]

PROSITE

PS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB01235. Levodopa.

Entry information

Entry name

PAOX_ARTGO

Accession

Primary (citable) accession number: P46881

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)