AMO1_ARTS1
ID AMO1_ARTS1 Reviewed; 648 AA.
AC Q07121;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=MAOXI;
DE Flags: Precursor;
GN Name=maoI;
OS Arthrobacter sp. (strain P1).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=47915;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 10-54; 358-381
RP AND 456-466.
RX PubMed=8366046; DOI=10.1128/jb.175.17.5617-5627.1993;
RA Zhang X., Fuller J.H., McIntire W.S.;
RT "Cloning, sequencing, expression, and regulation of the structural gene for
RT the copper/topa quinone-containing methylamine oxidase from Arthrobacter
RT strain P1, a Gram-positive facultative methylotroph.";
RL J. Bacteriol. 175:5617-5627(1993).
CC -!- FUNCTION: The exact function of MaoXI is not known.
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=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 -!- 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; L12983; AAA22076.1; -; Genomic_DNA.
DR AlphaFoldDB; Q07121; -.
DR SMR; Q07121; -.
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:0009308; P:amine metabolic process; IEA:InterPro.
DR Gene3D; 2.70.98.20; -; 1.
DR InterPro; IPR000269; Cu_amine_oxidase.
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 PANTHER; PTHR10638; PTHR10638; 1.
DR Pfam; PF01179; Cu_amine_oxid; 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 PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Disulfide bond; Manganese;
KW Metal-binding; Oxidoreductase; TPQ.
FT PROPEP 1..9
FT /evidence="ECO:0000269|PubMed:8366046"
FT /id="PRO_0000035675"
FT CHAIN 10..648
FT /note="Primary amine oxidase"
FT /id="PRO_0000035676"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT ACT_SITE 385
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 299..310
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 382..387
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 436
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 438
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT BINDING 445
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 446
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 584
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 595
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT MOD_RES 385
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT DISULFID 320..346
FT /evidence="ECO:0000250|UniProtKB:P12807"
SQ SEQUENCE 648 AA; 72761 MW; B2F9E267492253B5 CRC64;
MTLNAESEAL VGVSHPLDPL SRVEIARAVA ILKEGPAAAE SFRFISVELR EPSKDDLRAG
VAVAREADAV LVDRAQARSF EAVVDLEAGT VDSWKLLAEN IQPPFMLDEF AECEDACRKD
PEVIAALAKR GLTNLDLVCF EPWSVGYFGE DNEGRRLMRA LVFVRDEADD SPYAHPIENF
IVFYDLNAGK VVRLEDDQAI PVPSARGNYL PKYVGEARTD LKPLNITQPE GASFTVTGNH
VTWADWSFRV GFTPREGLVL HQLKFKDQGV DRPVINRASL SEMVVPYGDT APVQAKKNAF
DSGEYNIGNM ANSLTLGCDC LGEIKYFDGH SVDSHGNPWT IENAICMHEE DDSILWKHFD
FREGTAETRR SRKLVISFIA TVANYEYAFY WHLFLDGSIE FLVKATGILS TAGQLPGEKN
PYGQSLNNDG LYAPIHQHMF NVRMDFELDG VKNAVYEVDM EYPEHNPTGT AFMAVDRLLE
TEQKAIRKTN EAKHRFWKIA NHESKNLVNE PVAYRLIPTN GIQLAARDDA YVSKRAQFAR
NNLWVTAYDR TERFAAGEYP NQATGADDGL HIWTQKDRNI VDTDLVVWYT FGMHHVVRLE
DWPVMPRQNI GFMLEPHGFF NQNPTLNLPT STSTTQTGEA DTCCHNGK
