P46883 (AMO_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Primary amine oxidase
EC=1.4.3.21

Alternative name(s):
2-phenylethylamine oxidase
Copper amine oxidase
Tyramine oxidase

Gene names

Name:	tynA
Synonyms:	maoA
Ordered Locus Names:	b1386, JW1381

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	757 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)

Function	The enzyme prefers aromatic over aliphatic amines.
Catalytic activity	RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2. 2-phenylethylamine + H2O + O2 = phenylacetaldehyde + NH3 + H2O2.
Cofactor	Binds 1 copper ion per subunit. Binds 2 calcium ions per subunit. Contains 1 topaquinone per subunit.
Pathway	Amino-acid degradation; L-phenylalanine degradation; phenylacetate from L-phenylalanine: step 2/3.
Subunit structure	Homodimer.
Subcellular location	Periplasm.
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.
Caution	When highly overexpressed there can be substoichiometric amounts of TPQ in the enzyme; this may be due to imperfect conversion of tyrosine to TPQ (see Ref.3).

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Calcium Copper Metal-binding
Molecular function	Oxidoreductase
PTM	TPQ
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	L-phenylalanine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway phenylethylamine catabolic process Inferred from direct assay PubMed 3309152. Source: EcoCyc
Cellular_component	periplasmic space Inferred from direct assay PubMed 1334402. Source: EcoCyc
Molecular_function	aliphatic-amine oxidase activity Inferred from electronic annotation. Source: EC aminoacetone:oxygen oxidoreductase(deaminating) activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from direct assay Ref.2. Source: EcoCyc copper ion binding Inferred from direct assay PubMed 1334402. Source: EcoCyc phenethylamine:oxygen oxidoreductase (deaminating) activity Inferred from electronic annotation. Source: EC primary amine oxidase activity Inferred from direct assay PubMed 3309152. Source: EcoCyc quinone binding Inferred from direct assay PubMed 1334402. Source: EcoCyc tryptamine:oxygen oxidoreductase (deaminating) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

30

Ref.3 Ref.9 Ref.10

Chain

31 – 757

727

Primary amine oxidase

PRO_0000035673

Sites

Active site

413

1

Proton acceptor Probable

Active site

496

1

Schiff-base intermediate with substrate; via topaquinone

Metal binding

554

1

Copper

Metal binding

556

1

Copper

Metal binding

563

1

Calcium 1

Metal binding

564

1

Calcium 1; via carbonyl oxygen

Metal binding

565

1

Calcium 1

Metal binding

603

1

Calcium 2

Metal binding

700

1

Calcium 2

Metal binding

702

1

Calcium 2

Metal binding

708

1

Calcium 1

Metal binding

709

1

Calcium 1; via carbonyl oxygen

Metal binding

709

1

Calcium 2; via carbonyl oxygen

Metal binding

719

1

Copper

Amino acid modifications

Modified residue

496

1

2',4',5'-topaquinone

Natural variations

Natural variant

42

1

K → E in strain: W.

Natural variant

59

1

L → I in strain: W.

Experimental info

Sequence conflict

33

1

G → E AA sequence Ref.9

Sequence conflict

248

1

K → E in BAA04900. Ref.1

Sequence conflict

258 – 259

2

GY → VI in BAA04900. Ref.1

Sequence conflict

276

1

I → II in BAA04900. Ref.1

Sequence conflict

288

1

Missing Ref.1

Sequence conflict

290

1

P → I Ref.1

Sequence conflict

456

1

A → P in BAA04900. Ref.1

Sequence conflict

659

1

H → D in BAA04900. Ref.1

Secondary structure

1

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757

Helix Strand Turn

Details...

Beta strand

37 – 39

3

Helix

40 – 46

7

Beta strand

50 – 54

5

Turn

55 – 58

4

Beta strand

59 – 64

6

Beta strand

67 – 71

5

Beta strand

76 – 80

5

Beta strand

83 – 86

4

Beta strand

92 – 96

5

Beta strand

98 – 100

3

Helix

104 – 109

6

Beta strand

110 – 112

3

Beta strand

116 – 118

3

Helix

131 – 142

12

Beta strand

152 – 159

8

Helix

163 – 172

10

Beta strand

181 – 188

8

Beta strand

191 – 198

8

Turn

199 – 202

4

Beta strand

203 – 210

8

Helix

219 – 230

12

Helix

233 – 241

9

Helix

247 – 249

3

Beta strand

250 – 255

6

Turn

261 – 264

4

Beta strand

268 – 270

3

Beta strand

272 – 279

8

Beta strand

282 – 284

3

Helix

286 – 288

3

Beta strand

294 – 299

6

Turn

300 – 303

4

Beta strand

304 – 310

7

Beta strand

323 – 325

3

Beta strand

337 – 339

3

Beta strand

345 – 349

5

Beta strand

352 – 355

4

Beta strand

358 – 365

8

Turn

366 – 368

3

Beta strand

369 – 379

11

Beta strand

382 – 399

18

Turn

404 – 408

5

Beta strand

410 – 412

3

Helix

413 – 417

5

Turn

419 – 422

4

Turn

428 – 430

3

Beta strand

437 – 444

8

Beta strand

450 – 470

21

Beta strand

478 – 493

16

Beta strand

496 – 505

10

Beta strand

510 – 518

9

Beta strand

522 – 524

3

Helix

535 – 538

4

Turn

539 – 541

3

Beta strand

542 – 546

5

Beta strand

549 – 552

4

Beta strand

554 – 564

11

Beta strand

568 – 582

15

Beta strand

590 – 600

11

Helix

603 – 606

4

Beta strand

614 – 624

11

Beta strand

630 – 643

14

Helix

656 – 660

5

Helix

662 – 665

4

Beta strand

667 – 672

6

Helix

694 – 697

4

Turn

698 – 700

3

Beta strand

707 – 719

13

Helix

723 – 725

3

Beta strand

726 – 746

21

Sequences

	Sequence		Length	Mass (Da)
	P46883 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 65600BCED35243DB	FASTA	757	84,379
	10 20 30 40 50 60 MGSPSLYSAR KTTLALAVAL SFAWQAPVFA HGGEAHMVPM DKTLKEFGAD VQWDDYAQLF 70 80 90 100 110 120 TLIKDGAYVK VKPGAQTAIV NGQPLALQVP VVMKDNKAWV SDTFINDVFQ SGLDQTFQVE 130 140 150 160 170 180 KRPHPLNALT ADEIKQAVEI VKASADFKPN TRFTEISLLP PDKEAVWAFA LENKPVDQPR 190 200 210 220 230 240 KADVIMLDGK HIIEAVVDLQ NNKLLSWQPI KDAHGMVLLD DFASVQNIIN NSEEFAAAVK 250 260 270 280 290 300 KRGITDAKKV ITTPLTVGYF DGKDGLKQDA RLLKVISYLD VGDGNYWAHP IENLVAVVDL 310 320 330 340 350 360 EQKKIVKIEE GPVVPVPMTA RPFDGRDRVA PAVKPMQIIE PEGKNYTITG DMIHWRNWDF 370 380 390 400 410 420 HLSMNSRVGP MISTVTYNDN GTKRKVMYEG SLGGMIVPYG DPDIGWYFKA YLDSGDYGMG 430 440 450 460 470 480 TLTSPIARGK DAPSNAVLLN ETIADYTGVP MEIPRAIAVF ERYAGPEYKH QEMGQPNVST 490 500 510 520 530 540 ERRELVVRWI STVGNYDYIF DWIFHENGTI GIDAGATGIE AVKGVKAKTM HDETAKDDTR 550 560 570 580 590 600 YGTLIDHNIV GTTHQHIYNF RLDLDVDGEN NSLVAMDPVV KPNTAGGPRT STMQVNQYNI 610 620 630 640 650 660 GNEQDAAQKF DPGTIRLLSN PNKENRMGNP VSYQIIPYAG GTHPVAKGAQ FAPDEWIYHR 670 680 690 700 710 720 LSFMDKQLWV TRYHPGERFP EGKYPNRSTH DTGLGQYSKD NESLDNTDAV VWMTTGTTHV 730 740 750 ARAEEWPIMP TEWVHTLLKP WNFFDETPTL GALKKDK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the gene for monoamine oxidase (maoA) from Escherichia coli." Azakami H., Yamashita M., Roh J.-H., Suzuki H., Kumagai H., Murooka Y. J. Ferment. Bioeng. 77:315-319(1994) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2-A resolution." Parsons M.R., Convery M.A., Wilmot C.M., Yadav K.D.S., Blakeley V., Corner A.S., Phillips S.E.V., McPherson M.J., Knowles P.F. Structure 3:1171-1184(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). Strain: K12 / K10.
[3]	"Cloning of the maoA gene that encodes aromatic amine oxidase of Escherichia coli W3350 and characterization of the overexpressed enzyme." Steinebach V., Benen J.A.E., Bader R., Postma P.W., De Vries S., Duine J.A. Eur. J. Biochem. 237:584-591(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-35, CHARACTERIZATION. Strain: K12 / W3350 / ATCC 27020.
[4]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway." Ferrandez A., Minambres B., Garcia B., Olivera E.R., Luengo J.M., Garcia J.L., Diaz E. J. Biol. Chem. 273:25974-25986(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59. Strain: W / ATCC 11105 / DSM 1900.
[8]	"Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli." Ferrandez A., Prieto M.A., Garcia J.L., Diaz E. FEBS Lett. 406:23-27(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 477-757. Strain: W / ATCC 11105 / DSM 1900.
[9]	"maoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli." Yamashita M., Azakami H., Yokoro N., Roh J.-H., Suzuki H., Kumagai H., Murooka Y. J. Bacteriol. 178:2941-2947(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-50.
[10]	"2-phenylethylamine catabolism by Escherichia coli K-12: gene organization and expression." Hanlon S.P., Hill T.K., Flavell M.A., Stringfellow J.M., Cooper R.A. Microbiology 143:513-518(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-40. Strain: K12.
[11]	"Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction." Wilmot C.M., Murray J.M., Alton G., Parsons M.R., Convery M.A., Blakeley V., Corner A.S., Palcic M.M., Knowles P.F., McPherson M.J., Phillips S.E.V. Biochemistry 36:1608-1620(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[12]	"The active site base controls cofactor reactivity in Escherichia coli amine oxidase: X-ray crystallographic studies with mutational variants." Murray J.M., Saysell C.G., Wilmot C.M., Tambyrajah W.S., Jaeger J., Knowles P.F., Phillips S.E.V., McPherson M.J. Biochemistry 38:8217-8227(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[13]	"Visualization of dioxygen bound to copper during enzyme catalysis." Wilmot C.M., Hajdu J., McPherson M.J., Knowles P.F., Phillips S.E. Science 286:1724-1728(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D23670 Genomic DNA. Translation: BAA04900.1.
L47571 Genomic DNA. Translation: AAC37012.1.
U00096 Genomic DNA. Translation: AAC74468.1.
AP009048 Genomic DNA. Translation: BAA14996.1.
X97452 Genomic DNA. Translation: CAA66104.1.
X97453 Genomic DNA. Translation: CAA66107.1.

PIR

E64889.

RefSeq

NP_415904.3. NC_000913.2.
YP_489655.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D6U	X-ray	2.40	A/B	31-757	[»]
1D6Y	X-ray	2.40	A/B	31-757	[»]
1D6Z	X-ray	2.10	A/B	31-757	[»]
1DYU	X-ray	2.04	A/B	31-757	[»]
1JRQ	X-ray	2.15	A/B	31-757	[»]
1LVN	X-ray	2.40	A/B	31-757	[»]
1OAC	X-ray	2.00	A/B	31-757	[»]
1QAF	X-ray	2.20	A/B	36-756	[»]
1QAK	X-ray	2.00	A/B	36-757	[»]
1QAL	X-ray	2.20	A/B	36-756	[»]
1SPU	X-ray	2.00	A/B	31-757	[»]
2W0Q	X-ray	2.48	A/B	31-757	[»]
2WGQ	X-ray	2.50	A/B	31-757	[»]
2WO0	X-ray	2.60	A/B	31-757	[»]
2WOF	X-ray	2.25	A/B	31-757	[»]
2WOH	X-ray	2.70	A/B	31-757	[»]

ProteinModelPortal

P46883.

SMR

P46883. Positions 35-757.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-11057N.

IntAct

P46883. 6 interactions.

STRING

511145.b1386.

Proteomic databases

PaxDb

P46883.

PRIDE

P46883.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74468; AAC74468; b1386.
BAA14996; BAA14996; BAA14996.

GeneID

12931183.
945939.

KEGG

ecj:Y75_p1363.
eco:b1386.

PATRIC

32118058. VBIEscCol129921_1449.

Organism-specific databases

EchoBASE

EB2934.

EcoGene

EG13140. tynA.

Phylogenomic databases

eggNOG

COG3733.

HOGENOM

HOG000250947.

KO

K00276.

OMA

TSKENRM.

ProtClustDB

PRK14696.

Enzyme and pathway databases

BioCyc

EcoCyc:AMINEOXID-MONOMER.
ECOL316407:JW1381-MONOMER.
MetaCyc:AMINEOXID-MONOMER.

UniPathway

UPA00139; UER00723.

Gene expression databases

Genevestigator

P46883.

Family and domain databases

Gene3D

2.70.98.20. 1 hit.
3.10.450.40. 2 hits.
3.30.457.10. 1 hit.

InterPro

IPR000269. Cu_amine_oxidase.
IPR012854. Cu_amine_oxidase-like_N.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015801. Cu_amine_oxidase_N2/3.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]

PANTHER

PTHR10638. PTHR10638. 1 hit.

Pfam

PF01179. Cu_amine_oxid. 1 hit.
PF07833. Cu_amine_oxidN1. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]

SUPFAM

SSF55383. Cu_amine_oxidase-like_N. 1 hit.
SSF54416. Cu_amine_oxidase_N-reg. 2 hits.
SSF49998. CuNH_oxidase. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

P46883.

Entry information

Entry name

AMO_ECOLI

Accession

Primary (citable) accession number: P46883
Secondary accession number(s): O53008, P78153

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 139 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program