Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P46883 (AMO_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length757 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Ref.3 Ref.9 Ref.10
Chain31 – 757727Primary amine oxidase
PRO_0000035673

Sites

Active site4131Proton acceptor Probable
Active site4961Schiff-base intermediate with substrate; via topaquinone
Metal binding5541Copper
Metal binding5561Copper
Metal binding5631Calcium 1
Metal binding5641Calcium 1; via carbonyl oxygen
Metal binding5651Calcium 1
Metal binding6031Calcium 2
Metal binding7001Calcium 2
Metal binding7021Calcium 2
Metal binding7081Calcium 1
Metal binding7091Calcium 1; via carbonyl oxygen
Metal binding7091Calcium 2; via carbonyl oxygen
Metal binding7191Copper

Amino acid modifications

Modified residue49612',4',5'-topaquinone

Natural variations

Natural variant421K → E in strain: W.
Natural variant591L → I in strain: W.

Experimental info

Sequence conflict331G → E AA sequence Ref.9
Sequence conflict2481K → E in BAA04900. Ref.1
Sequence conflict258 – 2592GY → VI in BAA04900. Ref.1
Sequence conflict2761I → II in BAA04900. Ref.1
Sequence conflict2881Missing Ref.1
Sequence conflict2901P → I Ref.1
Sequence conflict4561A → P in BAA04900. Ref.1
Sequence conflict6591H → D in BAA04900. Ref.1

Secondary structure

........................................................................................................................... 757
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46883 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 65600BCED35243DB

FASTA75784,379
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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 277:1453-1462(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.
PIRE64889.
RefSeqNP_415904.3. NC_000913.3.
YP_489655.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D6UX-ray2.40A/B31-757[»]
1D6YX-ray2.40A/B31-757[»]
1D6ZX-ray2.10A/B31-757[»]
1DYUX-ray2.04A/B31-757[»]
1JRQX-ray2.15A/B31-757[»]
1LVNX-ray2.40A/B31-757[»]
1OACX-ray2.00A/B31-757[»]
1QAFX-ray2.20A/B36-756[»]
1QAKX-ray2.00A/B36-757[»]
1QALX-ray2.20A/B36-756[»]
1SPUX-ray2.00A/B31-757[»]
2W0QX-ray2.48A/B31-757[»]
2WGQX-ray2.50A/B31-757[»]
2WO0X-ray2.60A/B31-757[»]
2WOFX-ray2.25A/B31-757[»]
2WOHX-ray2.70A/B31-757[»]
ProteinModelPortalP46883.
SMRP46883. Positions 35-757.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-11057N.
IntActP46883. 6 interactions.
STRING511145.b1386.

Proteomic databases

PaxDbP46883.
PRIDEP46883.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74468; AAC74468; b1386.
BAA14996; BAA14996; BAA14996.
GeneID12931183.
945939.
KEGGecj:Y75_p1363.
eco:b1386.
PATRIC32118058. VBIEscCol129921_1449.

Organism-specific databases

EchoBASEEB2934.
EcoGeneEG13140. tynA.

Phylogenomic databases

eggNOGCOG3733.
HOGENOMHOG000250947.
KOK00276.
OMAIENTFHP.
OrthoDBEOG6FFS27.
PhylomeDBP46883.

Enzyme and pathway databases

BioCycEcoCyc:AMINEOXID-MONOMER.
ECOL316407:JW1381-MONOMER.
MetaCyc:AMINEOXID-MONOMER.
UniPathwayUPA00139; UER00723.

Gene expression databases

GenevestigatorP46883.

Family and domain databases

Gene3D2.70.98.20. 1 hit.
3.10.450.40. 2 hits.
3.30.457.10. 1 hit.
InterProIPR000269. 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]
PANTHERPTHR10638. PTHR10638. 1 hit.
PfamPF01179. 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]
SUPFAMSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
SSF55383. SSF55383. 1 hit.
PROSITEPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP46883.
PROP46883.

Entry information

Entry nameAMO_ECOLI
AccessionPrimary (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 14, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene