AMO_KLEOK
ID AMO_KLEOK Reviewed; 752 AA.
AC P80695; G8WBD9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Primary amine oxidase;
DE EC=1.4.3.21 {ECO:0000269|PubMed:9043125};
DE AltName: Full=Monamine oxidase;
DE AltName: Full=Tyramine oxidase;
DE Flags: Precursor;
GN Name=maoA; Synonyms=tynA; OrderedLocusNames=KOX_19410;
OS Klebsiella oxytoca (strain ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 /
OS NRRL B-199 / KCTC 1686 / BUCSAV 143 / CCM 1901).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1006551;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC
RC 1686 / BUCSAV 143 / CCM 1901;
RX PubMed=22493189; DOI=10.1128/jb.00026-12;
RA Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J.,
RA Yang K.S.;
RT "Complete genome sequence of Klebsiella oxytoca KCTC 1686, used in
RT production of 2,3-butanediol.";
RL J. Bacteriol. 194:2371-2372(2012).
RN [2]
RP PROTEIN SEQUENCE OF 28-47 AND 662-697, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC
RC 1686 / BUCSAV 143 / CCM 1901;
RX PubMed=9043125; DOI=10.1099/00221287-143-2-505;
RA Hacisalihoglu A., Jongejan J.A., Duine J.A.;
RT "Distribution of amine oxidases and amine dehydrogenases in bacteria grown
RT on primary amines and characterization of the amine oxidase from Klebsiella
RT oxytoca.";
RL Microbiology 143:505-512(1997).
CC -!- FUNCTION: Active on tyramine, tryptamine, beta-phenethylamine and
CC dopamine. {ECO:0000269|PubMed:9043125}.
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:0000269|PubMed:9043125};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:9043125};
CC Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:9043125};
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:0000269|PubMed:9043125}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:9043125}.
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; CP003218; AEX05604.1; -; Genomic_DNA.
DR RefSeq; WP_014229178.1; NC_016612.1.
DR AlphaFoldDB; P80695; -.
DR SMR; P80695; -.
DR EnsemblBacteria; AEX05604; AEX05604; KOX_19410.
DR KEGG; kox:KOX_19410; -.
DR PATRIC; fig|1006551.4.peg.3881; -.
DR HOGENOM; CLU_011500_5_0_6; -.
DR OMA; TNKLNPY; -.
DR Proteomes; UP000007843; Chromosome.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..27
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:9043125"
FT CHAIN 28..752
FT /note="Primary amine oxidase"
FT /id="PRO_0000064108"
FT ACT_SITE 410
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 493
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 408..419
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 490..495
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 551
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 553
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 560
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 560
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 561
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 562
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 562
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 600
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 694
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 699
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 705
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 705
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 716
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT MOD_RES 493
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
SQ SEQUENCE 752 AA; 83624 MW; 956A1D24B3963A9C CRC64;
MAILSPRKTA LALAVALSCA WQSPAFAHGG EAHMVPMDKT LQDFGADVQW DDYAQMFTLI
KDGAYVKVKP GAKTAIVNGK TLELQVPVVM KDGKAWVSDT FINDVFQSGL DQTFQVEKRP
HPLNSLSAAE ISAAVAIVKA AADFKPNTRF TEISLREPDK KAVWDFALNG TPVNAPRAAD
VIMLDGKHVI EAVVDLQNKK VLSWTPIKDA HGMVLLDDFA SVQNIINASS EFAEVLKKHG
IDDPSKVITT PLTVGYFDGK DGLKQDARLL KVVSYLDVGD GNYWAHPIEN LVAVVDLEQK
KIIKIEEGPT IPVPMAARPY DGRDRVAPKI KPLDIIEPEG KNYTITGDMI HWQNWDFHLR
MNSRVGPILS TVTYNDNGKK RQVMYEGSLG GMIVPYGDPD VGWYFKAYLD SGDYGMGTLT
SPIVRGKDAP SNAVLLDETI ADYTGTPTTI PRAIAIFERY AGPEYKHQEM GKPNVSTERR
ELVVRWISTV GNYDYIFDWV FHENGTIGID AGATGIEAVK GVQAKTMHDP SAKEDTRYGT
LIDHNIVGTT HQHIYNFRLD LDVDGENNTL VAMDPEVKPN TAGGPRTSTM QINQYTIDSE
QKAAQKFDPG TIRLLSNITK ENRMGNPVSY QIIPYAGGTH PVATGAKFAP DEWIYHRLSF
MDKQLWVTRY HPTERFPEGK YPNRSIHDTG LGQYAKDDES LDNHDDVVWI TTGTTHVARA
EEWPIMPTEW AHALLKPWNF FDETPTLGEK KE
