ID A0A178B444_9PLEO Unreviewed; 355 AA.
AC A0A178B444;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:OAL04119.1};
DE Flags: Fragment;
GN ORFNames=IQ06DRAFT_215991 {ECO:0000313|EMBL:OAL04119.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL04119.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAL04119.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL04119.1,
RC ECO:0000313|Proteomes:UP000077206};
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|PIRSR:PIRSR000189-1};
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC {ECO:0000256|ARBA:ARBA00006730}.
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DR EMBL; KV441708; OAL04119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178B444; -.
DR STRING; 765868.A0A178B444; -.
DR InParanoid; A0A178B444; -.
DR OrthoDB; 1385925at2759; -.
DR Proteomes; UP000077206; 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:UP000077206}.
FT DOMAIN 1..336
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 186
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OAL04119.1"
SQ SEQUENCE 355 AA; 38707 MW; F8536078D04ABC19 CRC64;
AGVIGLSTAL VLSKYKDIKV TVVSKHMPGD YDIEYASPWA GANSWPVGKP GSTLQKFEKA
TWPELQRICR EVPEAGIHLQ ESRIYGRKKD AGSATGLWFE ELCKEDAWFR EMVPDFRVLP
RSELPEDCDT GTAFTSVCIN TAVYLPWLLG QCFKNGVTFT RGILTHISEA GSFHSSGHAD
VVVNCTGLLA SKLGGVMDSN VYPGRGQIVV VRNKVNQMMT TSGTDDGSDE ATYIMGRAIA
GGTILGGCLQ HGSWESQPDP NLAQRIMQRS IDLCPSLAPK TGKVSELSII RHGVGLRPMR
KGGPRVEKER IEGSWIVHNY GHAGYGYQSG WGSAWAAEKL VLEILQETGR PQAKL
//
