ID A0A1S9DAB8_ASPOZ Unreviewed; 683 AA.
AC A0A1S9DAB8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=OAory_01016920 {ECO:0000313|EMBL:OOO06031.1};
OS Aspergillus oryzae (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5062 {ECO:0000313|EMBL:OOO06031.1, ECO:0000313|Proteomes:UP000190312};
RN [1] {ECO:0000313|EMBL:OOO06031.1, ECO:0000313|Proteomes:UP000190312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC7051 {ECO:0000313|EMBL:OOO06031.1,
RC ECO:0000313|Proteomes:UP000190312};
RA Thammarongtham C., Vorapreeda T., Nookaew I., Srisuk T., Land M.,
RA Jeennor S., Laoteng K.;
RT "Genome sequencing of Aspergillus oryzae BCC7051.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OOO06031.1}.
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DR EMBL; MKZY01000008; OOO06031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9DAB8; -.
DR VEuPathDB; FungiDB:AO090701000307; -.
DR eggNOG; KOG1186; Eukaryota.
DR Proteomes; UP000190312; Unassembled WGS sequence.
DR GO; GO:0052595; F:aliphatic amine oxidase activity; IEA:RHEA.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
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:SF86; COPPER AMINE OXIDASE 1-RELATED; 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 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:UP000190312};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 21..104
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 111..212
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 238..651
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 315
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 399
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 399
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 683 AA; 76549 MW; AF5DDEB4CC52C2F6 CRC64;
MVLDRLQQLT LQVSASSPPP HPFDPLSTVE IDTAVALVRE AHGKVNFNAV TLWEPRKAEM
MAWLADPQKA PRPMRAADVV AIAPGGKIYD GVVDLDQKKV IEWKHTPGVQ PLITMEDLQE
VEHIVRQDPK VIEQCAIIGI PKEDMHKVYC DPWTIGYDER FGTDVRLQQA LMYYRPHVDD
SQYTYPLDFC PIFNAETKQI IHIDVPPVRR PLSKAPPNNY HPAAIEKEGG FRTDLKPIHI
TQPEGVSFTV NGRHIEWQNW NIHVGFNYRE GIVLNNITFN DKGNVRPIFY RLSLGEMVVP
YGNPEHPHQR KHAFDLGEYG GGYMTNSLSL GCDCKGAIHY MDAAFVNRAG ASTIVKNAIC
IHEEDAGILF KHTDFRDESI IVTRGRKLII SHIFTAANYE YCVYWIFHQD GTVQLDIKLT
GILNTYAMNP GEDTKGWGTE VYPGVNAHNH QHLFCLRVDA NIDGPNNTVF QVDAVRGEGE
VGSAENKYGN AFYAKKTKFT TPLEAMSDYD GFTGRTWEIA NTNKLNAYSK KPVCYKLVSR
EVPPLLPKEG SLVWKRAGFA RHAVHVTKYS DDQIHPAGRH VPQTSGEPSQ GLPAWIEEAG
PNSSIDNTDV VLWHTFGLTH FPAPEDYPIM PAEPMTLLLR PRHFFTRNPV LDVPPSYART
PSQIAAGASS CSCKKNDGSS VLV
//
