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P46883

- AMO_ECOLI

UniProt

P46883 - AMO_ECOLI

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Protein
Primary amine oxidase
Gene
tynA, maoA, b1386, JW1381
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The enzyme prefers aromatic over aliphatic amines.

Catalytic activityi

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.
2-phenylethylamine + H2O + O2 = phenylacetaldehyde + NH3 + H2O2.

Cofactori

Binds 1 copper ion per subunit.
Binds 2 calcium ions per subunit.
Contains 1 topaquinone per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei413 – 4131Proton acceptor Inferred
Active sitei496 – 4961Schiff-base intermediate with substrate; via topaquinone
Metal bindingi554 – 5541Copper
Metal bindingi556 – 5561Copper
Metal bindingi563 – 5631Calcium 1
Metal bindingi564 – 5641Calcium 1; via carbonyl oxygen
Metal bindingi565 – 5651Calcium 1
Metal bindingi603 – 6031Calcium 2
Metal bindingi700 – 7001Calcium 2
Metal bindingi702 – 7021Calcium 2
Metal bindingi708 – 7081Calcium 1
Metal bindingi709 – 7091Calcium 1; via carbonyl oxygen
Metal bindingi709 – 7091Calcium 2; via carbonyl oxygen
Metal bindingi719 – 7191Copper

GO - Molecular functioni

  1. aliphatic-amine oxidase activity Source: UniProtKB-EC
  2. aminoacetone:oxygen oxidoreductase(deaminating) activity Source: UniProtKB-EC
  3. calcium ion binding Source: EcoCyc
  4. copper ion binding Source: EcoCyc
  5. phenethylamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC
  6. primary amine oxidase activity Source: EcoCyc
  7. quinone binding Source: EcoCyc
  8. tryptamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC

GO - Biological processi

  1. L-phenylalanine catabolic process Source: UniProtKB-UniPathway
  2. oxidation-reduction process Source: EcoCyc
  3. phenylethylamine catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Copper, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:AMINEOXID-MONOMER.
ECOL316407:JW1381-MONOMER.
MetaCyc:AMINEOXID-MONOMER.
UniPathwayiUPA00139; UER00723.

Names & Taxonomyi

Protein namesi
Recommended name:
Primary amine oxidase (EC:1.4.3.21)
Alternative name(s):
2-phenylethylamine oxidase
Copper amine oxidase
Tyramine oxidase
Gene namesi
Name:tynA
Synonyms:maoA
Ordered Locus Names:b1386, JW1381
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG13140. tynA.

Subcellular locationi

GO - Cellular componenti

  1. periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 30303 Publications
Add
BLAST
Chaini31 – 757727Primary amine oxidase
PRO_0000035673Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei496 – 49612',4',5'-topaquinone

Post-translational modificationi

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

Keywords - PTMi

TPQ

Proteomic databases

PaxDbiP46883.
PRIDEiP46883.

Expressioni

Gene expression databases

GenevestigatoriP46883.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

DIPiDIP-11057N.
IntActiP46883. 6 interactions.
STRINGi511145.b1386.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 393
Helixi40 – 467
Beta strandi50 – 545
Turni55 – 584
Beta strandi59 – 646
Beta strandi67 – 715
Beta strandi76 – 805
Beta strandi83 – 864
Beta strandi92 – 965
Beta strandi98 – 1003
Helixi104 – 1096
Beta strandi110 – 1123
Beta strandi116 – 1183
Helixi131 – 14212
Beta strandi152 – 1598
Helixi163 – 17210
Beta strandi181 – 1888
Beta strandi191 – 1988
Turni199 – 2024
Beta strandi203 – 2108
Helixi219 – 23012
Helixi233 – 2419
Helixi247 – 2493
Beta strandi250 – 2556
Turni261 – 2644
Beta strandi268 – 2703
Beta strandi272 – 2798
Beta strandi282 – 2843
Helixi286 – 2883
Beta strandi294 – 2996
Turni300 – 3034
Beta strandi304 – 3107
Beta strandi323 – 3253
Beta strandi337 – 3393
Beta strandi345 – 3495
Beta strandi352 – 3554
Beta strandi358 – 3658
Turni366 – 3683
Beta strandi369 – 37911
Beta strandi382 – 39918
Turni404 – 4085
Beta strandi410 – 4123
Helixi413 – 4175
Turni419 – 4224
Turni428 – 4303
Beta strandi437 – 4448
Beta strandi450 – 47021
Beta strandi478 – 49316
Beta strandi496 – 50510
Beta strandi510 – 5189
Beta strandi522 – 5243
Helixi535 – 5384
Turni539 – 5413
Beta strandi542 – 5465
Beta strandi549 – 5524
Beta strandi554 – 56411
Beta strandi568 – 58215
Beta strandi590 – 60011
Helixi603 – 6064
Beta strandi614 – 62411
Beta strandi630 – 64314
Helixi656 – 6605
Helixi662 – 6654
Beta strandi667 – 6726
Helixi694 – 6974
Turni698 – 7003
Beta strandi707 – 71913
Helixi723 – 7253
Beta strandi726 – 74621

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP46883.
SMRiP46883. Positions 35-757.

Miscellaneous databases

EvolutionaryTraceiP46883.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3733.
HOGENOMiHOG000250947.
KOiK00276.
OMAiIENTFHP.
OrthoDBiEOG6FFS27.
PhylomeDBiP46883.

Family and domain databases

Gene3Di2.70.98.20. 1 hit.
3.10.450.40. 2 hits.
3.30.457.10. 1 hit.
InterProiIPR000269. 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]
PANTHERiPTHR10638. PTHR10638. 1 hit.
PfamiPF01179. 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]
SUPFAMiSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
SSF55383. SSF55383. 1 hit.
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.

P46883-1 [UniParc]FASTAAdd to Basket

« Hide

MGSPSLYSAR KTTLALAVAL SFAWQAPVFA HGGEAHMVPM DKTLKEFGAD    50
VQWDDYAQLF TLIKDGAYVK VKPGAQTAIV NGQPLALQVP VVMKDNKAWV 100
SDTFINDVFQ SGLDQTFQVE KRPHPLNALT ADEIKQAVEI VKASADFKPN 150
TRFTEISLLP PDKEAVWAFA LENKPVDQPR KADVIMLDGK HIIEAVVDLQ 200
NNKLLSWQPI KDAHGMVLLD DFASVQNIIN NSEEFAAAVK KRGITDAKKV 250
ITTPLTVGYF DGKDGLKQDA RLLKVISYLD VGDGNYWAHP IENLVAVVDL 300
EQKKIVKIEE GPVVPVPMTA RPFDGRDRVA PAVKPMQIIE PEGKNYTITG 350
DMIHWRNWDF HLSMNSRVGP MISTVTYNDN GTKRKVMYEG SLGGMIVPYG 400
DPDIGWYFKA YLDSGDYGMG TLTSPIARGK DAPSNAVLLN ETIADYTGVP 450
MEIPRAIAVF ERYAGPEYKH QEMGQPNVST ERRELVVRWI STVGNYDYIF 500
DWIFHENGTI GIDAGATGIE AVKGVKAKTM HDETAKDDTR YGTLIDHNIV 550
GTTHQHIYNF RLDLDVDGEN NSLVAMDPVV KPNTAGGPRT STMQVNQYNI 600
GNEQDAAQKF DPGTIRLLSN PNKENRMGNP VSYQIIPYAG GTHPVAKGAQ 650
FAPDEWIYHR LSFMDKQLWV TRYHPGERFP EGKYPNRSTH DTGLGQYSKD 700
NESLDNTDAV VWMTTGTTHV ARAEEWPIMP TEWVHTLLKP WNFFDETPTL 750
GALKKDK 757
Length:757
Mass (Da):84,379
Last modified:November 1, 1995 - v1
Checksum:i65600BCED35243DB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421K → E in strain: W.
Natural varianti59 – 591L → I in strain: W.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331G → E AA sequence 1 Publication
Sequence conflicti248 – 2481K → E in BAA04900. 1 Publication
Sequence conflicti258 – 2592GY → VI in BAA04900. 1 Publication
Sequence conflicti276 – 2761I → II in BAA04900. 1 Publication
Sequence conflicti288 – 2881Missing1 Publication
Sequence conflicti290 – 2901P → I1 Publication
Sequence conflicti456 – 4561A → P in BAA04900. 1 Publication
Sequence conflicti659 – 6591H → D in BAA04900. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiE64889.
RefSeqiNP_415904.3. NC_000913.3.
YP_489655.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74468; AAC74468; b1386.
BAA14996; BAA14996; BAA14996.
GeneIDi12931183.
945939.
KEGGiecj:Y75_p1363.
eco:b1386.
PATRICi32118058. VBIEscCol129921_1449.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi E64889.
RefSeqi NP_415904.3. NC_000913.3.
YP_489655.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P46883.
SMRi P46883. Positions 35-757.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-11057N.
IntActi P46883. 6 interactions.
STRINGi 511145.b1386.

Proteomic databases

PaxDbi P46883.
PRIDEi P46883.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74468 ; AAC74468 ; b1386 .
BAA14996 ; BAA14996 ; BAA14996 .
GeneIDi 12931183.
945939.
KEGGi ecj:Y75_p1363.
eco:b1386.
PATRICi 32118058. VBIEscCol129921_1449.

Organism-specific databases

EchoBASEi EB2934.
EcoGenei EG13140. tynA.

Phylogenomic databases

eggNOGi COG3733.
HOGENOMi HOG000250947.
KOi K00276.
OMAi IENTFHP.
OrthoDBi EOG6FFS27.
PhylomeDBi P46883.

Enzyme and pathway databases

UniPathwayi UPA00139 ; UER00723 .
BioCyci EcoCyc:AMINEOXID-MONOMER.
ECOL316407:JW1381-MONOMER.
MetaCyc:AMINEOXID-MONOMER.

Miscellaneous databases

EvolutionaryTracei P46883.
PROi P46883.

Gene expression databases

Genevestigatori P46883.

Family and domain databases

Gene3Di 2.70.98.20. 1 hit.
3.10.450.40. 2 hits.
3.30.457.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR10638. PTHR10638. 1 hit.
Pfami 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 ]
SUPFAMi SSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
SSF55383. SSF55383. 1 hit.
PROSITEi PS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. 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).

Entry informationi

Entry nameiAMO_ECOLI
AccessioniPrimary (citable) accession number: P46883
Secondary accession number(s): O53008, P78153
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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 1 Publication).

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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