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Database: UniProt
Entry: A0A177C690_9PLEO
LinkDB: A0A177C690_9PLEO
Original site: A0A177C690_9PLEO 
ID   A0A177C690_9PLEO        Unreviewed;       497 AA.
AC   A0A177C690;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN   ORFNames=CC84DRAFT_1096824 {ECO:0000313|EMBL:OAG03045.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG03045.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG03045.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG03045.1,
RC   ECO:0000313|Proteomes:UP000077069};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU362067}.
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DR   EMBL; KV441555; OAG03045.1; -; Genomic_DNA.
DR   RefSeq; XP_018033410.1; XM_018174683.1.
DR   AlphaFoldDB; A0A177C690; -.
DR   STRING; 1460663.A0A177C690; -.
DR   GeneID; 28758169; -.
DR   InParanoid; A0A177C690; -.
DR   OrthoDB; 5471885at2759; -.
DR   Proteomes; UP000077069; Unassembled WGS sequence.
DR   GO; GO:0097621; F:monoamine oxidase activity; IEA:RHEA.
DR   Gene3D; 3.90.660.10; -; 2.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001613; Flavin_amine_oxidase.
DR   PANTHER; PTHR10742:SF218; AMINE OXIDASE; 1.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
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:UP000077069}.
FT   DOMAIN          48..479
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   497 AA;  55308 MW;  A0C6DD7B417FA38E CRC64;
     MTSRDGFTWT PSDGLKPGVP SLGVISPSSN ISSTQVEYDV IVIGAGYCGL TAARNAALDG
     LKVLLLEGRD RIGGRSWSSN IGGYPFEMGG TWVHWGQSNS WREITRYRME KDVEMSFDFA
     KGVKHFELNT PESSVTMTHD DEDILLDSAL KKFTNIDGFY GRKTIPLPYT TFHQPSSIPL
     DSLSALDRIN EIADTLSPQE RAVLEASILL ASGGTLETTS FHEFMHWWAM CGYTYQGWLD
     MLITWKFRDG QSTFARRFFD EALATKRLSY AFNTPVQHIS TSPSAVEITS RSNTTYRALR
     AICTIPLNVL SDIKFTPPLP TGKQAAIAIG HVNQTVKVHA EVSNKDLRSW TGINYPNELH
     YAIGDGTTPA GNTHIVCFGG QNRHMDPEVD VDRTKRAVSS LFNPGNYAGQ NVQIERLVFH
     NWSKDEFAKG AWFFAPPGLL SEHLDDMRGR HGNVVFANSD WALGWRSFID GAIEEGTRAE
     LEVREEVVGL RGVKQKL
//
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