AMO_KLEAE
ID AMO_KLEAE Reviewed; 755 AA.
AC P49250;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Primary amine oxidase;
DE EC=1.4.3.21 {ECO:0000250|UniProtKB:P46883};
DE AltName: Full=Copper amine oxidase;
DE AltName: Full=Monamine oxidase;
DE AltName: Full=Tyramine oxidase;
DE Flags: Precursor;
GN Name=maoA; Synonyms=tynA;
OS Klebsiella aerogenes (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=548;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 31-41.
RC STRAIN=W70;
RX PubMed=1556068; DOI=10.1128/jb.174.8.2485-2492.1992;
RA Sugino H., Sasaki M., Azakami H., Yamashita M., Murooka Y.;
RT "A monoamine-regulated Klebsiella aerogenes operon containing the monoamine
RT oxidase structural gene (maoA) and the maoC gene.";
RL J. Bacteriol. 174:2485-2492(1992).
CC -!- FUNCTION: Active on tyramine, tryptamine, beta-phenethylamine and
CC dopamine.
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:0000250|UniProtKB:P46883};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P46883};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P12807};
CC Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc
CC ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807,
CC ECO:0000250|UniProtKB:P46883};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P46883};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:P46883};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000250|UniProtKB:P46883};
CC Note=Contains 1 topaquinone per subunit.
CC {ECO:0000250|UniProtKB:P46883};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q43077};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q43077};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P46883}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: By tyramine and catecholamines.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
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DR EMBL; D10208; BAA01060.1; -; Genomic_DNA.
DR AlphaFoldDB; P49250; -.
DR SMR; P49250; -.
DR STRING; 548.EAG7_01320; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
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:0008131; F:primary amine oxidase 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:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.70.98.20; -; 1.
DR Gene3D; 3.30.457.10; -; 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; PTHR10638; 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; SSF49998; 1.
DR SUPFAM; SSF54416; SSF54416; 2.
DR SUPFAM; SSF55383; SSF55383; 1.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE 1: Evidence at protein level;
KW Catecholamine metabolism; Copper; Direct protein sequencing; Manganese;
KW Metal-binding; Oxidoreductase; Periplasm; Signal; TPQ.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:1556068"
FT CHAIN 31..755
FT /note="Primary amine oxidase"
FT /id="PRO_0000035674"
FT ACT_SITE 413
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 496
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 411..422
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 493..498
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 554
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 556
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 563
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 563
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 564
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 565
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 565
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 603
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 697
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 700
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 702
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 708
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 708
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 719
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT MOD_RES 496
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
SQ SEQUENCE 755 AA; 83577 MW; 7B5552283CD93EFF CRC64;
MANGLKFSPR KTALALAVAV VCAWQSPVFA HGSEAHMVPL DKTLQEFGAD VQWDDYAQMF
TLIKDGAYVK VKPGAKTAIV NGKSLDLPVP VVMKEGKAWV SDTFINDVFQ SGLDQTFQVE
KRPHPLNSLS AAEISKAVTI VKAAPEFQPN TRFTEISLHE PDKAAVWAFA LQGTPVDAPR
TADVVMLDGK HVIEAVVDLQ NKKILSWTPI KGAHGMVLLD DFVSVQNIIN TSSEFAEVLK
KHGITDPGKV VTTPLTVGFF DGKDGLQQDA RLLKVVSYLD TGDGNYWAHP IENLVAVVDL
EAKKIIKIEE GPVIPVPMEP RPYDGRDRNA PAVKPLEITE PEGKNYTITG DTIHWQNWDF
HLRLNSRVGP ILSTVTYNDN GTKRQVMYEG SLGGMIVPYG DPDVGWYFKA YLDSGDYGMG
TLTSPIVRGK DAPSNAVLLD ETIADYTGKP TTIPGAVAIF ERYAGPEYKH LEMGKPNVST
ERRELVVRWI STVGNYDYIF DWVFHDNGTI GIDAGATGIE AVKGVLAKTM HDPSAKEDTR
YGTLIDHNIV GTTHQHIYNF RLDLDVDGEN NTLVAMDPEV KPNTAGGPRT STMQVNQYTI
DSEQKAAQKF DPGTIRLLSN TSKENRMGNP VSYQIIPYAG GTHPAATGAK FAPDEWIYHR
LSFMDKQLWV TRYHPTERYP EGKYPNRSAH DTGLGQYAKD DESLTNHDDV VWITTGTTHV
ARAEEWPIMP TEWALALLKP WNFFDETPTL GEKKK
