ID   A0A0B7NFY2_9FUNG        Unreviewed;       308 AA.
AC   A0A0B7NFY2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=FAD dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF01266};
GN   Name=PARPA_10594.1 scaffold 41210 {ECO:0000313|EMBL:CEP16337.1};
OS   Parasitella parasitica.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX   NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP16337.1, ECO:0000313|Proteomes:UP000054107};
RN   [1] {ECO:0000313|EMBL:CEP16337.1, ECO:0000313|Proteomes:UP000054107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP16337.1,
RC   ECO:0000313|Proteomes:UP000054107};
RA   Ellenberger Sabrina;
RL   Submitted (SEP-2014) 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; LN733060; CEP16337.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B7NFY2; -.
DR   STRING; 35722.A0A0B7NFY2; -.
DR   OrthoDB; 1385925at2759; -.
DR   Proteomes; UP000054107; 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; IPR023209; DAO.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR   PANTHER; PTHR11530:SF11; D-ASPARTATE OXIDASE; 1.
DR   Pfam; PF01266; DAO; 2.
DR   PIRSF; PIRSF000189; D-aa_oxidase; 2.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 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:UP000054107}.
FT   DOMAIN          8..171
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          185..294
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   BINDING         48..49
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ   SEQUENCE   308 AA;  34233 MW;  2FC44D0775A0F845 CRC64;
     MIDTDKPIIV VGAGVIGLSV ALQLREQGYK NITSVAKYIP GDVCIEYTSP YAGAHWRTMA
     PNSDKLLQKF DAVTYDRFMD LAHSSDNTGI MIAPSYDYYD DALSSEVTDP WFKDVVQDFE
     FLTEKEDLPH GAQLGHKYTT VLINTPVYIA WLASKFKSLG GKIVQRNLGH IDEVLSAKEP
     QWTQGINYVI PRSDGTVVLG GTANKHDFNP FPETQTNNTI LEKTFALCPE LKEQPLEIVK
     YNVGLRPSRI GGVRIENEML TSRNRKQTIQ VTHGYGHGGF GVQSSWGSAE YIVQVMENGL
     IKSTAARL
//