ID A0A1B1PVU9_9RHOB Unreviewed; 659 AA.
AC A0A1B1PVU9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=AYJ57_20290 {ECO:0000313|EMBL:ANT62715.1};
OS Salipiger sp. CCB-MM3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1792508 {ECO:0000313|EMBL:ANT62715.1, ECO:0000313|Proteomes:UP000092483};
RN [1] {ECO:0000313|EMBL:ANT62715.1, ECO:0000313|Proteomes:UP000092483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB-MM3 {ECO:0000313|EMBL:ANT62715.1,
RC ECO:0000313|Proteomes:UP000092483};
RA Lau N.-S., Sam K.K., Abdullah A.A.-A., Chong A.S.-C.;
RT "Genome feautures of moderately halophilic polyhydroxyalkanoate-producing
RT Yangia sp. CCB-MM3.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP014596; ANT62715.1; -; Genomic_DNA.
DR RefSeq; WP_066110271.1; NZ_CP014596.1.
DR AlphaFoldDB; A0A1B1PVU9; -.
DR STRING; 1792508.AYJ57_20290; -.
DR KEGG; yan:AYJ57_20290; -.
DR OrthoDB; 9772590at2; -.
DR Proteomes; UP000092483; Chromosome 2.
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 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; COPPER AMINE OXIDASE; 1.
DR PANTHER; PTHR10638:SF94; PRIMARY AMINE OXIDASE; 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; Amine oxidase catalytic domain; 1.
DR SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
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:UP000092483};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 21..105
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 115..212
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 237..639
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 314
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 398
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 398
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 659 AA; 73307 MW; 52D95A0D155E6EC5 CRC64;
MSDTITDTPP AEAAATQPVK HPLDPISAQE VTTLKAVLAA AGFAGESTRY SYVMLREPAR
ETLASFTPGA AIPREIGVLV TDLAAGALTE IIVDIPAEKI IHRRSLDPKV DGWGPVLDED
YVAAEEIAKA DPRFIEALAK RGITDLDTVF CCPLSAGVFG FEEEEGRRML RVLSFQAPSA
DAIHALWAHP IEGVVCHVDL TERKVLRFVD TGFPTVPAQN DDYLDPAIEK RETMKPLNIT
QPQGGSFTME DNVLNWENWS IRVGFNGREG LTLHDIRFKD GDRDRSILNR ASVSEMVVPY
GEPQPTHEWQ NYFDAGEYQF GRLANSLVLG CDCLGEIHYV DATVVDDFCN PIEIKNAICI
HEEDFGTLWK HTDIFTGRSD VRRQRRLVVS FFVTVGNYDY GFYWYFYLDG KIELECKATG
IVFTSGRPEG DYEWATELAP QLGAPQHQHM FSARLDFAID GLKNRVDEID VKRVPMGPGN
PVGNAFTRQI TRLETESDAQ RVARNELGRV WRISSAEATN YLGEPTAYVL APEGLPLLLA
DDDASITQRA GFATKSLWVT KFDRDEMWAA GYTPNQHPGG AGLPAYAAAN RSVDGEDIVV
WHTFGLTHFP RTEDWPVMPV DYAGFKLRPE NFFDRNPTLD VPKDPNGAQC CRSNKIAAE
//
