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Database: UniProt
Entry: A0A109FJP0_9BASI
LinkDB: A0A109FJP0_9BASI
Original site: A0A109FJP0_9BASI 
ID   A0A109FJP0_9BASI        Unreviewed;       372 AA.
AC   A0A109FJP0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   16-JAN-2019, entry version 15.
DE   SubName: Full=D-amino acid oxidase in complex with Two Anthranylate molecules {ECO:0000313|EMBL:KWU45700.1};
GN   ORFNames=RHOSPDRAFT_32625 {ECO:0000313|EMBL:KWU45700.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU45700.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU45700.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU45700.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L.,
RA   Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000189-1};
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DR   EMBL; KQ954470; KWU45700.1; -; Genomic_DNA.
DR   EnsemblFungi; KWU45700; KWU45700; RHOSPDRAFT_32625.
DR   OrthoDB; 1363414at2759; -.
DR   Proteomes; UP000062823; 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   InterPro; IPR006181; D-amino_acid_oxidase_CS.
DR   InterPro; IPR023209; DAO.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   PANTHER; PTHR11530; PTHR11530; 1.
DR   Pfam; PF01266; DAO; 1.
DR   PIRSF; PIRSF000189; D-aa_oxidase; 1.
DR   PROSITE; PS00677; DAO; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000062823};
KW   FAD {ECO:0000256|PIRSR:PIRSR000189-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000189-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823}.
FT   DOMAIN        6    351       DAO. {ECO:0000259|Pfam:PF01266}.
FT   BINDING     162    162       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000189-
FT                                1}.
FT   BINDING     179    179       FAD. {ECO:0000256|PIRSR:PIRSR000189-1}.
FT   BINDING     223    223       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000189-1}.
FT   BINDING     285    285       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000189-1}.
SQ   SEQUENCE   372 AA;  40261 MW;  88BAA10FCE963FF8 CRC64;
     MTQNKRVVVL GSGVIGLSCA LALAQKGYKV HVVARDLPED TVAQTFASPW AGANWTPFMS
     KEAGPRQAKW EEATFKQWVD FVPQGLAMWL KGTRRFAETE ADLLGHWYKD IVPNYRHLNP
     SDCPPGAIGV TYDTLSVNAP KFCQYLQREA QKLGVTFERR LVTSLEQIAD GADLIVNATG
     LGAKSIAGVE DQEVEPIRGQ TVLIKSNCKR CTMDSSDPKS PAYIIPRPGG EVICGGTYLV
     GNYDLSVDPA TIPRILKHCL RLDPSISTDG TLEGIEILRH NVGLRPARRG GPRVELERVS
     FPLKRGQSLL ALGTAKAAEG KASRTVPVVH AYGFSSAGYQ QGWGAALEVR DLVDQAIGSS
     SSASSGRYLA KL
//
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