ID H6BXT2_EXODN Unreviewed; 424 AA.
AC H6BXT2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=D-amino-acid oxidase {ECO:0000313|EMBL:EHY57424.1};
GN ORFNames=HMPREF1120_05460 {ECO:0000313|EMBL:EHY57424.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY57424.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY57424.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY57424.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC {ECO:0000256|ARBA:ARBA00006730}.
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DR EMBL; JH226133; EHY57424.1; -; Genomic_DNA.
DR RefSeq; XP_009157883.1; XM_009159635.1.
DR AlphaFoldDB; H6BXT2; -.
DR STRING; 858893.H6BXT2; -.
DR GeneID; 20310099; -.
DR VEuPathDB; FungiDB:HMPREF1120_05460; -.
DR eggNOG; KOG3923; Eukaryota.
DR HOGENOM; CLU_647285_0_0_1; -.
DR InParanoid; H6BXT2; -.
DR OMA; VYLQWLQ; -.
DR OrthoDB; 1385925at2759; -.
DR Proteomes; UP000007304; 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:SF16; D-AMINO ACID OXIDASE (AFU_ORTHOLOGUE AFUA_5G11290); 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007304}.
FT DOMAIN 11..301
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 352..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 47656 MW; 8AD8FC67B582696D CRC64;
MTMASSSSPT DFVVLGAGVA GLTTAVELHR AFPSATIAVV AKYMPGYTSA TEYTSPWAGA
NWHSFEKEPN QFAEYDRATY SRFIEIAAQS PESGIEPLPL RVLYDTDETR RKGLWYAEHI
GGVKEVPENE LPPGAVFGLD MASFMINTTV YLSWLQTQLL QSKKVTFLRR HYHHIDALLN
DFPDARAVFN CTGLGARKLG GVDDEAVYPT KGQTLLIAQP KEPLKRMYVQ TSAAWDNEFA
HVFPRPLGGG VIIGGVRRDN DWTAEPDLEL AERIKQRCCA LAPELGRPED LQVISHNVGL
RRRILVTHTH THTMLHDCSL QYFNLHPHPP FSGSAMPMPM IRYHQNIRTF DRHDRVESNS
ARLDWQASEK ERNKTTQTAK DTKDGRWNRN RSRTSRKDER RVHDVMGTGT GTGAGAKCVR
IVEL
//
