ID A0A2V1E985_9PLEO Unreviewed; 370 AA.
AC A0A2V1E985;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Nucleotide-binding domain-containing protein {ECO:0000313|EMBL:PVI06732.1};
GN ORFNames=DM02DRAFT_514074 {ECO:0000313|EMBL:PVI06732.1};
OS Periconia macrospinosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX NCBI_TaxID=97972 {ECO:0000313|EMBL:PVI06732.1, ECO:0000313|Proteomes:UP000244855};
RN [1] {ECO:0000313|EMBL:PVI06732.1, ECO:0000313|Proteomes:UP000244855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE2036 {ECO:0000313|EMBL:PVI06732.1,
RC ECO:0000313|Proteomes:UP000244855};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000189-1};
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC {ECO:0000256|ARBA:ARBA00006730}.
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DR EMBL; KZ805307; PVI06732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1E985; -.
DR STRING; 97972.A0A2V1E985; -.
DR Proteomes; UP000244855; Unassembled WGS sequence.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046416; P:D-amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR006181; D-amino_acid_oxidase_CS.
DR InterPro; IPR023209; DAO.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR PANTHER; PTHR11530:SF16; D-AMINO ACID OXIDASE (AFU_ORTHOLOGUE AFUA_5G11290); 1.
DR Pfam; PF01266; DAO; 1.
DR PIRSF; PIRSF000189; D-aa_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS00677; DAO; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000189-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000189-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244855}.
FT DOMAIN 11..359
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 51..52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ SEQUENCE 370 AA; 40780 MW; D28EA9DA57E26F75 CRC64;
MTAPNNPPSF FVLGAGVIGL STALTLRSAY PNSPITIVAK HFPGDRSIEY TSPWAGANWA
TFAHDNGPLE HYDRLTFNKF KKMIDEEGIG EEVGIGRMGM WGIFDEPIEK AGILSDGTGK
LWFRELVGGL RELQEKELPE GAVFGLEFAS TWRINTQVYL NWLQAQVLQK GIKTIRRHYS
SLASLYADFP STTLLINCSA LGSLHLTDVR DTNLYPTRGQ TVLVAEPKVP IERMYFRSPA
RIDPTVSYVF PRPNGGGVIL GGSRQDGNWS AEVDMELSKQ IMEKCCALCP ELGRPEDLQV
ISHNVGLRRE CLALLPSRVG GIRIELERLS NGVPVVHNYG HAGAGYQSSW GTAERAVELV
RKALEPAAKL
//
