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Protein

Primary amine oxidase

Gene

tynA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.3 Publications
2-phenylethylamine + H2O + O2 = phenylacetaldehyde + NH3 + H2O2.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by 2-hydrazinopyridine.1 Publication

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
Active sitei413Proton acceptorCombined sources2 Publications1
Active sitei496Schiff-base intermediate with substrate; via topaquinoneCombined sources1 Publication1
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

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

  • L-phenylalanine catabolic process Source: UniProtKB-UniPathway
  • oxidation-reduction process Source: EcoCyc
  • phenylethylamine catabolic process Source: EcoCyc

Keywordsi

Molecular functionOxidoreductase
LigandCalcium, Copper, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:AMINEOXID-MONOMER
MetaCyc:AMINEOXID-MONOMER
BRENDAi1.4.3.21 2026
UniPathwayiUPA00139; 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
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13140 tynA

Subcellular locationi

GO - Cellular componenti

  • periplasmic space Source: EcoCyc

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 303 PublicationsAdd BLAST30
ChainiPRO_000003567331 – 757Primary amine oxidaseAdd BLAST727

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei4962',4',5'-topaquinoneCombined sources1 Publication1

Post-translational modificationi

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

Keywords - PTMi

TPQ

Proteomic databases

PaxDbiP46883
PRIDEiP46883

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

1757
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 39Combined sources3
Helixi40 – 46Combined sources7
Beta strandi50 – 54Combined sources5
Turni55 – 58Combined sources4
Beta strandi59 – 64Combined sources6
Beta strandi67 – 71Combined sources5
Beta strandi76 – 80Combined sources5
Beta strandi83 – 86Combined sources4
Beta strandi92 – 96Combined sources5
Beta strandi98 – 100Combined sources3
Helixi104 – 109Combined sources6
Beta strandi110 – 112Combined sources3
Beta strandi116 – 118Combined sources3
Helixi131 – 142Combined sources12
Beta strandi152 – 159Combined sources8
Helixi163 – 172Combined sources10
Beta strandi181 – 188Combined sources8
Beta strandi191 – 198Combined sources8
Turni199 – 202Combined sources4
Beta strandi203 – 210Combined sources8
Helixi219 – 230Combined sources12
Helixi233 – 241Combined sources9
Helixi247 – 249Combined sources3
Beta strandi250 – 255Combined sources6
Turni261 – 264Combined sources4
Beta strandi268 – 270Combined sources3
Beta strandi272 – 279Combined sources8
Beta strandi282 – 284Combined sources3
Helixi286 – 288Combined sources3
Beta strandi294 – 299Combined sources6
Turni300 – 303Combined sources4
Beta strandi304 – 310Combined sources7
Beta strandi323 – 325Combined sources3
Beta strandi337 – 339Combined sources3
Beta strandi345 – 349Combined sources5
Beta strandi352 – 355Combined sources4
Beta strandi358 – 365Combined sources8
Turni366 – 368Combined sources3
Beta strandi369 – 379Combined sources11
Beta strandi382 – 399Combined sources18
Turni404 – 408Combined sources5
Beta strandi410 – 412Combined sources3
Helixi413 – 417Combined sources5
Turni419 – 422Combined sources4
Turni428 – 430Combined sources3
Beta strandi437 – 444Combined sources8
Beta strandi450 – 470Combined sources21
Beta strandi478 – 493Combined sources16
Beta strandi496 – 505Combined sources10
Beta strandi510 – 518Combined sources9
Beta strandi522 – 524Combined sources3
Helixi535 – 538Combined sources4
Turni539 – 541Combined sources3
Beta strandi542 – 546Combined sources5
Beta strandi549 – 552Combined sources4
Beta strandi554 – 564Combined sources11
Beta strandi568 – 582Combined sources15
Beta strandi590 – 600Combined sources11
Helixi603 – 606Combined sources4
Beta strandi614 – 624Combined sources11
Beta strandi630 – 643Combined sources14
Helixi656 – 660Combined sources5
Helixi662 – 665Combined sources4
Beta strandi667 – 672Combined sources6
Helixi694 – 697Combined sources4
Turni698 – 700Combined sources3
Beta strandi707 – 719Combined sources13
Helixi723 – 725Combined sources3
Beta strandi726 – 746Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP46883
SMRiP46883
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46883

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni411 – 422Substrate bindingCombined sources1 PublicationAdd BLAST12
Regioni493 – 498Substrate bindingCombined sources2 Publications6

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105F11 Bacteria
COG3733 LUCA
HOGENOMiHOG000250947
InParanoidiP46883
KOiK00276
OMAiWQKWKMH
PhylomeDBiP46883

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

Sequencei

Sequence statusi: Complete.

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
Checksum:i65600BCED35243DB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Natural varianti42K → E in strain: W. 1
Natural varianti59L → 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
PIRiE64889
RefSeqiNP_415904.3, NC_000913.3
WP_000535469.1, NZ_LN832404.1

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiAMO_ECOLI
AccessioniPrimary (citable) accession number: P46883
Secondary accession number(s): O53008, P78153
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 28, 2018
This is version 167 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

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