UniProtKB - P46883 (AMO_ECOLI)
Protein
Primary amine oxidase
Gene
tynA
Organism
Escherichia coli (strain K12)
Status
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
Catalytic activityi
Cofactori
Protein has several cofactor binding sites:- Cu cation3 Publications, Zn2+By similarityNote: Binds 1 copper ion per subunit. Can also use zinc ion as cofactor (By similarity).By similarity3 Publications
- Ca2+3 PublicationsNote: Binds 2 calcium ions per subunit.3 Publications
- L-topaquinone1 PublicationNote: Contains 1 topaquinone per subunit.1 Publication
- Mn2+By similarityNote: Binds 1 Mn2+ ion per subunit.By similarity
Activity regulationi
Inhibited by 2-hydrazinopyridine.1 Publication
: L-phenylalanine degradation Pathwayi
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:
- no protein annotated in this organism
- Primary amine oxidase (tynA)
- Phenylacetaldehyde dehydrogenase (feaB)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 413 | Proton acceptorCombined sources2 Publications | 1 | |
Active sitei | 496 | Schiff-base intermediate with substrate; via topaquinoneCombined sources1 Publication | 1 | |
Metal bindingi | 554 | Copper; via tele nitrogenCombined sources3 Publications | 1 | |
Metal bindingi | 556 | Copper; via tele nitrogenCombined sources3 Publications | 1 | |
Metal bindingi | 563 | Calcium 1Combined sources3 Publications | 1 | |
Metal bindingi | 563 | ManganeseBy similarity | 1 | |
Metal bindingi | 564 | Calcium 1; via carbonyl oxygenCombined sources3 Publications | 1 | |
Metal bindingi | 565 | Calcium 1Combined sources3 Publications | 1 | |
Metal bindingi | 565 | ManganeseBy similarity | 1 | |
Metal bindingi | 603 | Calcium 2Combined sources3 Publications | 1 | |
Metal bindingi | 697 | Calcium 2; via carbonyl oxygenCombined sources3 Publications | 1 | |
Metal bindingi | 700 | Calcium 2Combined sources1 Publication | 1 | |
Metal bindingi | 702 | Calcium 2Combined sources3 Publications | 1 | |
Metal bindingi | 708 | Calcium 1Combined sources3 Publications | 1 | |
Metal bindingi | 708 | ManganeseBy similarity | 1 | |
Metal bindingi | 709 | Calcium 1; via carbonyl oxygenCombined sources3 Publications | 1 | |
Metal bindingi | 709 | Calcium 2; via carbonyl oxygen | 1 | |
Metal bindingi | 719 | Copper; via pros nitrogenCombined sources3 Publications | 1 |
GO - Molecular functioni
- aliphatic-amine oxidase activity Source: UniProtKB-EC
- aminoacetone:oxygen oxidoreductase(deaminating) activity Source: UniProtKB-EC
- calcium ion binding Source: EcoCyc
- copper ion binding Source: EcoCyc
- phenethylamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC
- primary amine oxidase activity Source: EcoCyc
- quinone binding Source: EcoCyc
- tryptamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC
GO - Biological processi
- amine metabolic process Source: GO_Central
- L-phenylalanine catabolic process Source: UniProtKB-UniPathway
- phenylethylamine catabolic process Source: EcoCyc
Keywordsi
Molecular function | Oxidoreductase |
Ligand | Calcium, Copper, Manganese, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:AMINEOXID-MONOMER MetaCyc:AMINEOXID-MONOMER |
BRENDAi | 1.4.3.21, 2026 |
UniPathwayi | UPA00139;UER00723 |
Names & Taxonomyi
Protein namesi | Recommended name: Primary amine oxidase (EC:1.4.3.213 Publications)Alternative name(s): 2-phenylethylamine oxidase Copper amine oxidase Tyramine oxidase |
Gene namesi | Name:tynA Synonyms:maoA Ordered Locus Names:b1386, JW1381 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Other locations
Other locations
- periplasmic space Source: EcoCyc
Keywords - Cellular componenti
PeriplasmPathology & Biotechi
Chemistry databases
DrugBanki | DB01657, 2-amino-3-[4-hydroxy-6-oxo-3-(2-phenyl-cyclopropylimino)-cyclohexa-1,4-dienyl]-propionic acid DB01634, 2-Oxy-4-Hydroxy-5-(2-Hydrazinopyridine)Phenylalanine DB03631, 3-(4-hydroxy-3-imino-6-oxo-cyclohexa-1,4-dienyl)-alanine DB02928, 3-Amino-6-Hydroxy-Tyrosine DB04334, 6-hydroxydopa quinone DB01576, Dextroamphetamine DB04325, Phenethylamine DB02178, Phenylacetaldehyde |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 30 | 3 PublicationsAdd BLAST | 30 | |
ChainiPRO_0000035673 | 31 – 757 | Primary amine oxidaseAdd BLAST | 727 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 496 | 2',4',5'-topaquinoneCombined sources1 Publication | 1 |
Post-translational modificationi
Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.1 Publication
Keywords - PTMi
TPQProteomic databases
PaxDbi | P46883 |
PRIDEi | P46883 |
Interactioni
Subunit structurei
Homodimer.
3 PublicationsProtein-protein interaction databases
BioGRIDi | 4260177, 11 interactors |
DIPi | DIP-11057N |
IntActi | P46883, 6 interactors |
STRINGi | 511145.b1386 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P46883 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P46883 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 411 – 422 | Substrate bindingCombined sources1 PublicationAdd BLAST | 12 | |
Regioni | 493 – 498 | Substrate bindingCombined sources2 Publications | 6 |
Sequence similaritiesi
Belongs to the copper/topaquinone oxidase family.Curated
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | COG3733, Bacteria |
HOGENOMi | CLU_011500_5_0_6 |
InParanoidi | P46883 |
PhylomeDBi | P46883 |
Family and domain databases
Gene3Di | 2.70.98.20, 1 hit 3.30.457.10, 1 hit |
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 |
PANTHERi | PTHR10638, PTHR10638, 1 hit |
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 |
SUPFAMi | SSF49998, SSF49998, 1 hit SSF54416, SSF54416, 2 hits SSF55383, SSF55383, 1 hit |
PROSITEi | View protein in PROSITE PS01164, COPPER_AMINE_OXID_1, 1 hit PS01165, COPPER_AMINE_OXID_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P46883-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 33 | G → E AA sequence (PubMed:8631685).Curated | 1 | |
Sequence conflicti | 248 | K → E in BAA04900 (Ref. 1) Curated | 1 | |
Sequence conflicti | 258 – 259 | GY → VI in BAA04900 (Ref. 1) Curated | 2 | |
Sequence conflicti | 276 | I → II in BAA04900 (Ref. 1) Curated | 1 | |
Sequence conflicti | 288 | Missing (Ref. 1) Curated | 1 | |
Sequence conflicti | 290 | P → I (Ref. 1) Curated | 1 | |
Sequence conflicti | 456 | A → P in BAA04900 (Ref. 1) Curated | 1 | |
Sequence conflicti | 659 | H → D in BAA04900 (Ref. 1) Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 42 | K → E in strain: W. | 1 | |
Natural varianti | 59 | L → I in strain: W. | 1 |
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 |
PIRi | E64889 |
RefSeqi | NP_415904.3, NC_000913.3 WP_000535469.1, NZ_SSZK01000012.1 |
Genome annotation databases
EnsemblBacteriai | AAC74468; AAC74468; b1386 BAA14996; BAA14996; BAA14996 |
GeneIDi | 945939 |
KEGGi | ecj:JW1381 eco:b1386 |
PATRICi | fig|1411691.4.peg.886 |
Similar proteinsi
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 |
PIRi | E64889 |
RefSeqi | NP_415904.3, NC_000913.3 WP_000535469.1, NZ_SSZK01000012.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
6EZZ | X-ray | 1.80 | A/B | 31-757 | [»] | |
SMRi | P46883 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260177, 11 interactors |
DIPi | DIP-11057N |
IntActi | P46883, 6 interactors |
STRINGi | 511145.b1386 |
Chemistry databases
DrugBanki | DB01657, 2-amino-3-[4-hydroxy-6-oxo-3-(2-phenyl-cyclopropylimino)-cyclohexa-1,4-dienyl]-propionic acid DB01634, 2-Oxy-4-Hydroxy-5-(2-Hydrazinopyridine)Phenylalanine DB03631, 3-(4-hydroxy-3-imino-6-oxo-cyclohexa-1,4-dienyl)-alanine DB02928, 3-Amino-6-Hydroxy-Tyrosine DB04334, 6-hydroxydopa quinone DB01576, Dextroamphetamine DB04325, Phenethylamine DB02178, Phenylacetaldehyde |
Proteomic databases
PaxDbi | P46883 |
PRIDEi | P46883 |
Genome annotation databases
EnsemblBacteriai | AAC74468; AAC74468; b1386 BAA14996; BAA14996; BAA14996 |
GeneIDi | 945939 |
KEGGi | ecj:JW1381 eco:b1386 |
PATRICi | fig|1411691.4.peg.886 |
Organism-specific databases
EchoBASEi | EB2934 |
Phylogenomic databases
eggNOGi | COG3733, Bacteria |
HOGENOMi | CLU_011500_5_0_6 |
InParanoidi | P46883 |
PhylomeDBi | P46883 |
Enzyme and pathway databases
UniPathwayi | UPA00139;UER00723 |
BioCyci | EcoCyc:AMINEOXID-MONOMER MetaCyc:AMINEOXID-MONOMER |
BRENDAi | 1.4.3.21, 2026 |
Miscellaneous databases
EvolutionaryTracei | P46883 |
PROi | PR:P46883 |
Family and domain databases
Gene3Di | 2.70.98.20, 1 hit 3.30.457.10, 1 hit |
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 |
PANTHERi | PTHR10638, PTHR10638, 1 hit |
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 |
SUPFAMi | SSF49998, SSF49998, 1 hit SSF54416, SSF54416, 2 hits SSF55383, SSF55383, 1 hit |
PROSITEi | View protein in PROSITE PS01164, COPPER_AMINE_OXID_1, 1 hit PS01165, COPPER_AMINE_OXID_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | AMO_ECOLI | |
Accessioni | P46883Primary (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: | April 7, 2021 | |
This is version 186 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families