ID   B7L6A6_ECO55            Unreviewed;       757 AA.
AC   B7L6A6;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   Name=tynA {ECO:0000313|EMBL:CAU97379.1};
GN   OrderedLocusNames=EC55989_1522 {ECO:0000313|EMBL:CAU97379.1};
OS   Escherichia coli (strain 55989 / EAEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585055 {ECO:0000313|EMBL:CAU97379.1, ECO:0000313|Proteomes:UP000000746};
RN   [1] {ECO:0000313|Proteomes:UP000000746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55989 / EAEC {ECO:0000313|Proteomes:UP000000746};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58001; EC=1.4.3.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001138};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000672};
CC       Note=Contains 1 topaquinone per subunit.
CC       {ECO:0000256|RuleBase:RU000672};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC       a specific tyrosyl residue. {ECO:0000256|PIRSR:PIRSR600269-51,
CC       ECO:0000256|RuleBase:RU000672}.
CC   -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC       {ECO:0000256|ARBA:ARBA00007983, ECO:0000256|RuleBase:RU000672}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU928145; CAU97379.1; -; Genomic_DNA.
DR   RefSeq; WP_000535447.1; NC_011748.1.
DR   AlphaFoldDB; B7L6A6; -.
DR   KEGG; eck:EC55989_1522; -.
DR   HOGENOM; CLU_011500_5_0_6; -.
DR   Proteomes; UP000000746; Chromosome.
DR   GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.450.40; -; 2.
DR   Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 1.
DR   Gene3D; 3.30.457.10; Copper amine oxidase-like, N-terminal domain; 1.
DR   InterPro; IPR000269; Cu_amine_oxidase.
DR   InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR   InterPro; IPR015798; Cu_amine_oxidase_C.
DR   InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR   InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR   InterPro; IPR015800; Cu_amine_oxidase_N2.
DR   InterPro; IPR015802; Cu_amine_oxidase_N3.
DR   InterPro; IPR036582; Mao_N_sf.
DR   PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638:SF94; PRIMARY AMINE OXIDASE; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   Pfam; PF07833; Cu_amine_oxidN1; 1.
DR   Pfam; PF02727; Cu_amine_oxidN2; 1.
DR   Pfam; PF02728; Cu_amine_oxidN3; 1.
DR   SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR   SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
DR   SUPFAM; SSF55383; Copper amine oxidase, domain N; 1.
DR   PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR   PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000672};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000672};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000672};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000746};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..757
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002859734"
FT   DOMAIN          36..110
FT                   /note="Copper amine oxidase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07833"
FT   DOMAIN          124..209
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          216..316
FT                   /note="Copper amine oxidase N3-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02728"
FT   DOMAIN          337..750
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   REGION          680..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        413
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        496
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         496
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   757 AA;  84384 MW;  DE5B57E65837A887 CRC64;
     MGSPSLYSAR KTTLALAVAL SFAWQAPVFA HGGEAHMVPM DETLKEFGAD VQWDDYAQIF
     TLIKDGAYVK VKPGAQTAIV NGQPLALQVP VVMKDNKAWV SDTFINDVFQ SGLDQTFQVE
     KRPHPLNALT ADEIKQAVEI VKASADFKPN TRFTEISLLP PDKEAVWAFA LENKPVDQPR
     KADVIMLDGK HIIEAVVDLQ NNKLLSWQPI KDAHGMVLLD DFASVQNIIN NSEEFAAAVK
     KRGITDAKKV ITTPLTVGYF DGKDGLKQDA RLLKVISYLD VGDGNYWAHP IENLVAVVDL
     EQKKIVKIEE GAVVPVPMTA RPFDGRDRVA PAVKPMQIIE PEGKNYTITG DMIHWRNWDF
     HLSMNSRVGP MISTVTYNDN GTKRKVMYEG SLGGMIVPYG DPDIGWYFKA YLDSGDYGMG
     TLTSPIARGK DAPSNAVLLN ETIADYTGVP MEIPRAIAVF ERYAGPEYKH QEMGQPNVST
     ERRELVVRWI STVGNYDYIF DWIFHENGTI GIDAGATGIE AVKGVKAKTM HDETAKDDTR
     YGTLIDHNIV GTTHQHIYNF RLDLDVDGEN NSLVAMDPVV KPNTAGGPRT STMQVNQYNI
     GNEQDAAQKF DPGTIRLLSN LNKENRMGNP VSYQIIPYAG GTHPVAKGAQ FAPDEWIYHR
     LSFMDKQLWV TRYHPGERFP EGKYPNRSTH DTGLGQYSKD NESLDNTDAV IWMTTGTTHV
     ARAEEWPIMP TEWVHTLLKP WNFFDETPTL GALKKDK
//