ID A0A2D3UPQ9_9PEZI Unreviewed; 478 AA.
AC A0A2D3UPQ9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=RCC_12029 {ECO:0000313|EMBL:CZT14955.1};
OS Ramularia collo-cygni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT14955.1, ECO:0000313|Proteomes:UP000225277};
RN [1] {ECO:0000313|EMBL:CZT14955.1, ECO:0000313|Proteomes:UP000225277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URUG2 {ECO:0000313|EMBL:CZT14955.1,
RC ECO:0000313|Proteomes:UP000225277};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; FJUY01000001; CZT14955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D3UPQ9; -.
DR STRING; 112498.A0A2D3UPQ9; -.
DR OrthoDB; 5471885at2759; -.
DR Proteomes; UP000225277; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000225277};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..478
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013837525"
FT DOMAIN 34..476
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 478 AA; 50721 MW; 121ACDC230907479 CRC64;
MKTIAFSLLL TLLVTTASSH DDALVDVAIV GAGLSGLAAA KALQDAGKTF TILEARERVG
GRVQNQDLSN GGVTELGAAF VGPTQDYVLD LAASLGLKVF SEYNEGNNVA FLDQQNLTYS
TESPVPPIDD VSIQQLLSAI TFIDTAASAI DVNHPWSHPN ASAWDSINFA TWMEQQNLTT
TLCALFDISI PAIFSLESTE LSLFYALSYV AAAGNATLPG SFLRLISVAG GAQESRIVGG
TGLLATGLAD QIGHDKIQLN SPVRSIIQHP SGIYSVCGTG STVNAKQVII AMSPPLASRI
FYDPPLPAMR DQLTQRMFMG SLGKAIAIYS TPFWREANVS GQAISDSGTV RTTYDVSPED
GSYGAILGFI EADRARAVEE LTDAEIAALV TEDYVKYFGP QAANVSEWAI KRWDHEVYSR
GGPVALAGIG TLSRFGPALR EKSGGIHWAG TEASEYWIGF MDGALRAGER AAKEIISG
//
