ID G7Y096_ASPKW Unreviewed; 464 AA.
AC G7Y096;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=AKAW_10701 {ECO:0000313|EMBL:GAA92587.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA92587.1};
RN [1] {ECO:0000313|EMBL:GAA92587.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA92587.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary aliphatic amine + H2O + O2 = a primary amine + an
CC aldehyde + H2O2; Xref=Rhea:RHEA:26414, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:58855, ChEBI:CHEBI:65296; EC=1.4.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000205};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362067};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995, ECO:0000256|RuleBase:RU362067}.
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DR EMBL; DF126497; GAA92587.1; -; Genomic_DNA.
DR AlphaFoldDB; G7Y096; -.
DR STRING; 1033177.G7Y096; -.
DR VEuPathDB; FungiDB:AKAW_10701; -.
DR eggNOG; KOG0029; Eukaryota.
DR InParanoid; G7Y096; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0097621; F:monoamine oxidase activity; IEA:RHEA.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR PANTHER; PTHR43563:SF14; AMINE OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU362067};
KW Flavoprotein {ECO:0000256|RuleBase:RU362067};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067}.
FT DOMAIN 21..457
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 464 AA; 50989 MW; EBC2CAB160053863 CRC64;
MTASKDPTTK LYDVVIVGAG LSGLQAAHSI QAAGFSVCIL EATDRVGGKT LTVKSSEKGY
NDLGAAWVND TNQSEIFKLH QRYGLEGVVQ YTRGDDILES GEGVIRNIPY GWPLTGLARK
LLNILRDESL RMDLDNPKGF PEAKEVDNMT FEEFCVDRSG SQDAVHMADA ISSGLLGVDS
KEVSALYMLY YFKSGSGIDN LLSDEKDGAQ YLRTRQGTQT IARKMADELD QSDIFLGMPV
TSINQSPGNS PCVVQTLDGS SFSCQRVIVS IPTNLYQSIS FCPPLPQAKH VLSNHTIMGY
YSKMIFVFQE PWWRNARLTG IIDSAGGPIT FTRDTSVPTD DQWSITCFMV GSRGRAWSEL
SKGDRFNQVW EQFCRCFGKF VKDIPKPNNT LEMEWSKEPF FLGAPCPVMT PGLLTTVGSD
LAAPHGKVHF IGTETSTVWR GYMEGAIRAG QRGAAEVVTA LQED
//
