ID A0A0A2K3L1_PENEN Unreviewed; 602 AA.
AC A0A0A2K3L1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=PEX2_090470 {ECO:0000313|EMBL:KGO54794.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO54794.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO54794.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO54794.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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}.
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:KGO54794.1}.
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DR EMBL; JQFZ01000214; KGO54794.1; -; Genomic_DNA.
DR RefSeq; XP_016597106.1; XM_016746317.1.
DR AlphaFoldDB; A0A0A2K3L1; -.
DR STRING; 27334.A0A0A2K3L1; -.
DR GeneID; 27681737; -.
DR HOGENOM; CLU_004498_0_3_1; -.
DR OrthoDB; 5471885at2759; -.
DR PhylomeDB; A0A0A2K3L1; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0097621; F:monoamine oxidase activity; IEA:RHEA.
DR CDD; cd00448; YjgF_YER057c_UK114_family; 1.
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 Gene3D; 3.30.1330.40; RutC-like; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR InterPro; IPR035959; RutC-like_sf.
DR InterPro; IPR006175; YjgF/YER057c/UK114.
DR PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR PANTHER; PTHR43563:SF14; AMINE OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF01042; Ribonuc_L-PSP; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55298; YjgF-like; 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:UP000030143}.
FT DOMAIN 153..590
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 602 AA; 64869 MW; A6D59D650B865A9E CRC64;
MPKTVETVDL SNTAGAYYAP ATVAPAGKII HIAGQPGSTK NGVVPADYES QIHLALLNLR
KLIIAAGSSI ENIVKLQLFI VDYDAANRKH TRHIQRFLNG HRPAITLVPV PKLAVASWLL
EIDAIIALPE PSLPPVLPSA NENTDVVIIG AGLAGLSAAH DVLRAGLSCV VLEARDRVGG
KTWSSPLNGG GVIDLGAGWI NDTNQSKVYA LAKRYGAEVI VQNTQGNAVL QDFDGNCSPF
VYGDLPSFDK ATQAHLAEIR DMCEADCQAL DTWRPQDTSL DSITFEAYLR SRGASEVAIA
TGMVWTRAML GQDPQDISAL YFLNYCKSGG GLLQMRSDRK DGGQYLRIRQ GTQHFSLGLA
SSLPENTVRL SSPVHSIIQN ADKSVKVQAG GVVYGARKVI ITVPSPAMKT ISFHPKLPPS
KQAWIDSTTY GYYTKAMMEF RSPFWVKAGF CGLAQSFVGP ASVVRDSCSP EDKKYVLTCF
MSGDPGRAWS ALSQKEREQS LLQQLGKLFG VANLDKEFIQ LTAYEWVNDE WAGWGCPCTA
LTPGVLDTLG PDALRESSGN LHFAGTETAG EWKGYMEGAI RSGERAAAEV VKTLNAGIVS
RL
//
