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Database: UniProt
Entry: A0A167DMB8_9PEZI
LinkDB: A0A167DMB8_9PEZI
Original site: A0A167DMB8_9PEZI 
ID   A0A167DMB8_9PEZI        Unreviewed;       461 AA.
AC   A0A167DMB8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Fructosyl amino acid oxidase {ECO:0000313|EMBL:KZL84069.1};
DE   Flags: Fragment;
GN   ORFNames=CI238_10100 {ECO:0000313|EMBL:KZL84069.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL84069.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL84069.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL84069.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KZL84069.1}.
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DR   EMBL; LFIW01000969; KZL84069.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A167DMB8; -.
DR   STRING; 1573173.A0A167DMB8; -.
DR   Proteomes; UP000076584; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR045170; MTOX.
DR   PANTHER; PTHR10961; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR   PANTHER; PTHR10961:SF7; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076584}.
FT   DOMAIN          20..404
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KZL84069.1"
SQ   SEQUENCE   461 AA;  52052 MW;  B24BB405FFC05EEE CRC64;
     LRNYYYQLCL SAQEMAEPTV LIIGAGTFGT STAYHLAQTY KDPSRVTIID RWDSSSPAKA
     AAAIDVNRII YTDYVSPLYC NLANEAIHPW FWSLDLGHFF HKTGLMVLDD HNSGFPERVR
     NTLQQRGSDY TKDVDVLHPA KRWEVLGGMK TDGLGKSYFN PEAGWADAAL ATANFMTVAE
     RKGVKRVTGE VEELVFDIRR QKLVGARTSN NRTFTADQIV LAAGAWTSSI LTSIEDVLHV
     QAQDRIERQI KAVGRLSVYY TLSAEATNRL CEADMPIIVY RHQAILTPPS RENRTLKIND
     LSTEFVNMVT TKAGHQISVP SNRFQEDVPD KLKAATSELL RLFIPHFARE QKPERWRVCW
     DTKTPTGDWL LCKHPHPQLQ NLHLVVGGNF SSYKSMPIVG KYVCNVLNGK SNGEEKDLAW
     GWKSEETLRG GERKEELGCK EARALRPDFK AFEEETLTSK L
//
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