GenomeNet

Database: UniProt
Entry: Q2UR81_ASPOR
LinkDB: Q2UR81_ASPOR
Original site: Q2UR81_ASPOR 
ID   Q2UR81_ASPOR            Unreviewed;       356 AA.
AC   Q2UR81;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=FAD dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF01266};
GN   ORFNames=AO090005000932 {ECO:0000313|EMBL:BAE55934.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE55934.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE55934.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP007151; BAE55934.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UR81; -.
DR   STRING; 510516.Q2UR81; -.
DR   EnsemblFungi; BAE55934; BAE55934; AO090005000932.
DR   VEuPathDB; FungiDB:AO090005000932; -.
DR   HOGENOM; CLU_034311_2_0_1; -.
DR   OMA; KAPHIME; -.
DR   OrthoDB; 930761at2759; -.
DR   Proteomes; UP000006564; Chromosome 1.
DR   GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:EnsemblFungi.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0046436; P:D-alanine metabolic process; IEA:EnsemblFungi.
DR   GO; GO:1902114; P:D-valine metabolic process; IEA:EnsemblFungi.
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:SF11; D-ASPARTATE OXIDASE; 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:UP000006564}.
FT   DOMAIN          6..342
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   BINDING         47..48
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         176
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         326
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ   SEQUENCE   356 AA;  38471 MW;  4A3A53F44B2AF90E CRC64;
     MAHNNIVVLG AGIIGLNVAL ELSKRGYGQH ITIMAEHLPG DESIDYTSPW AGANFSGISG
     SDANALRWDQ SGYSAMMSLI DAGAEEAKYL CKTESTEYWD QAPSQDKINS MTEYLRDIRP
     YQSILVIIPP SDLPKGVAFG IRFTTVTLNA PAHCEHLKHL LSQPRYGGVK FVRRKVSSLQ
     DAFLHGTQIV FNCVGNAALN LAGVADSKCY PTRGQIILVK APSVKVNVMR HGKDYETYII
     PRPRSDGTVV LGGYLQPGDH FSQARPVETE SILSRTIGLL RILGNEETEI IRVAVGLRPS
     RQGGARVELE TTPEGNTVVH NYGAGGTGFQ AGMGMAKDAV DLASGILVHL QAQSKL
//
DBGET integrated database retrieval system