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Protein

Primary amine oxidase

Gene

tynA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

The enzyme prefers aromatic over aliphatic amines.

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 PubMed:8647101).Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by 2-hydrazinopyridine.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-phenylalanine degradation

This protein is involved in step 2 of the subpathway that synthesizes phenylacetate from L-phenylalanine.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Primary amine oxidase (tynA)
  3. Phenylacetaldehyde dehydrogenase (feaB)
This subpathway is part of the pathway L-phenylalanine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phenylacetate from L-phenylalanine, the pathway L-phenylalanine degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei413Proton acceptorCombined sources2 Publications1
Active sitei496Schiff-base intermediate with substrate; via topaquinoneCombined sources1 Publication1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi554Copper; via tele nitrogenCombined sources3 Publications1
Metal bindingi556Copper; via tele nitrogenCombined sources3 Publications1
Metal bindingi563Calcium 1Combined sources3 Publications1
Metal bindingi563ManganeseBy similarity1
Metal bindingi564Calcium 1; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi565Calcium 1Combined sources3 Publications1
Metal bindingi565ManganeseBy similarity1
Metal bindingi603Calcium 2Combined sources3 Publications1
Metal bindingi697Calcium 2; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi700Calcium 2Combined sources1 Publication1
Metal bindingi702Calcium 2Combined sources3 Publications1
Metal bindingi708Calcium 1Combined sources3 Publications1
Metal bindingi708ManganeseBy similarity1
Metal bindingi709Calcium 1; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi709Calcium 2; via carbonyl oxygen1
Metal bindingi719Copper; via pros nitrogenCombined sources3 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
LigandCalcium, Copper, Manganese, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:AMINEOXID-MONOMER
MetaCyc:AMINEOXID-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.4.3.21 2026

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00139;UER00723

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Primary amine oxidase (EC:1.4.3.213 Publications)
Alternative name(s):
2-phenylethylamine oxidase
Copper amine oxidase
Tyramine oxidase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:tynA
Synonyms:maoA
Ordered Locus Names:b1386, JW1381
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG13140 tynA

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB01634 2-Oxy-4-Hydroxy-5-(2-Hydrazinopyridine)Phenylalanine
DB04325 2-Phenylethylamine
DB02928 3-Amino-6-Hydroxy-Tyrosine
DB04334 6-hydroxydopa quinone
DB02178 Phenylacetaldehyde

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 303 PublicationsAdd BLAST30
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003567331 – 757Primary amine oxidaseAdd BLAST727

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei4962',4',5'-topaquinoneCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.1 Publication

Keywords - PTMi

TPQ

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P46883

PRoteomics IDEntifications database

More...
PRIDEi
P46883

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4260177, 11 interactors

Database of interacting proteins

More...
DIPi
DIP-11057N

Protein interaction database and analysis system

More...
IntActi
P46883, 6 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_1511

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1757
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P46883

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P46883

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P46883

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni411 – 422Substrate bindingCombined sources1 PublicationAdd BLAST12
Regioni493 – 498Substrate bindingCombined sources2 Publications6

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105F11 Bacteria
COG3733 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000250947

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P46883

KEGG Orthology (KO)

More...
KOi
K00276

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P46883

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.70.98.20, 1 hit
3.30.457.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000269 Cu_amine_oxidase
IPR012854 Cu_amine_oxidase-like_N
IPR015798 Cu_amine_oxidase_C
IPR036460 Cu_amine_oxidase_C_sf
IPR016182 Cu_amine_oxidase_N-reg
IPR015800 Cu_amine_oxidase_N2
IPR015802 Cu_amine_oxidase_N3
IPR036582 Mao_N_sf

The PANTHER Classification System

More...
PANTHERi
PTHR10638 PTHR10638, 1 hit

Pfam protein domain database

More...
Pfami
View protein in 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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49998 SSF49998, 1 hit
SSF54416 SSF54416, 2 hits
SSF55383 SSF55383, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01164 COPPER_AMINE_OXID_1, 1 hit
PS01165 COPPER_AMINE_OXID_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

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

GALKKDK
Length:757
Mass (Da):84,379
Last modified:November 1, 1995 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i65600BCED35243DB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti33G → E AA sequence (PubMed:8631685).Curated1
Sequence conflicti248K → E in BAA04900 (Ref. 1) Curated1
Sequence conflicti258 – 259GY → VI in BAA04900 (Ref. 1) Curated2
Sequence conflicti276I → II in BAA04900 (Ref. 1) Curated1
Sequence conflicti288Missing (Ref. 1) Curated1
Sequence conflicti290P → I (Ref. 1) Curated1
Sequence conflicti456A → P in BAA04900 (Ref. 1) Curated1
Sequence conflicti659H → D in BAA04900 (Ref. 1) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti42K → E in strain: W. 1
Natural varianti59L → I in strain: W. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
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

Protein sequence database of the Protein Information Resource

More...
PIRi
E64889

NCBI Reference Sequences

More...
RefSeqi
NP_415904.3, NC_000913.3
WP_000535469.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74468; AAC74468; b1386
BAA14996; BAA14996; BAA14996

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945939

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1381
eco:b1386

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.886

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
WP_000535469.1, NZ_LN832404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB 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[»]
6EZZX-ray1.80A/B31-757[»]
ProteinModelPortaliP46883
SMRiP46883
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260177, 11 interactors
DIPiDIP-11057N
IntActiP46883, 6 interactors
STRINGi316385.ECDH10B_1511

Chemistry databases

DrugBankiDB01634 2-Oxy-4-Hydroxy-5-(2-Hydrazinopyridine)Phenylalanine
DB04325 2-Phenylethylamine
DB02928 3-Amino-6-Hydroxy-Tyrosine
DB04334 6-hydroxydopa quinone
DB02178 Phenylacetaldehyde

Proteomic databases

PaxDbiP46883
PRIDEiP46883

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74468; AAC74468; b1386
BAA14996; BAA14996; BAA14996
GeneIDi945939
KEGGiecj:JW1381
eco:b1386
PATRICifig|1411691.4.peg.886

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB2934
EcoGeneiEG13140 tynA

Phylogenomic databases

eggNOGiENOG4105F11 Bacteria
COG3733 LUCA
HOGENOMiHOG000250947
InParanoidiP46883
KOiK00276
PhylomeDBiP46883

Enzyme and pathway databases

UniPathwayi
UPA00139;UER00723

BioCyciEcoCyc:AMINEOXID-MONOMER
MetaCyc:AMINEOXID-MONOMER
BRENDAi1.4.3.21 2026

Miscellaneous databases

EvolutionaryTraceiP46883

Protein Ontology

More...
PROi
PR:P46883

Family and domain databases

Gene3Di2.70.98.20, 1 hit
3.30.457.10, 1 hit
InterProiView protein in InterPro
IPR000269 Cu_amine_oxidase
IPR012854 Cu_amine_oxidase-like_N
IPR015798 Cu_amine_oxidase_C
IPR036460 Cu_amine_oxidase_C_sf
IPR016182 Cu_amine_oxidase_N-reg
IPR015800 Cu_amine_oxidase_N2
IPR015802 Cu_amine_oxidase_N3
IPR036582 Mao_N_sf
PANTHERiPTHR10638 PTHR10638, 1 hit
PfamiView protein in 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
SUPFAMiSSF49998 SSF49998, 1 hit
SSF54416 SSF54416, 2 hits
SSF55383 SSF55383, 1 hit
PROSITEiView protein in PROSITE
PS01164 COPPER_AMINE_OXID_1, 1 hit
PS01165 COPPER_AMINE_OXID_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAMO_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P46883
Secondary accession number(s): O53008, P78153
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: December 5, 2018
This is version 171 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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