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Database: UniProt
Entry: C5E1J7_ZYGRC
LinkDB: C5E1J7_ZYGRC
Original site: C5E1J7_ZYGRC 
ID   C5E1J7_ZYGRC            Unreviewed;       369 AA.
AC   C5E1J7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=ZYRO0G21538p {ECO:0000313|EMBL:CAR29981.1};
GN   OrderedLocusNames=ZYRO0G21538g {ECO:0000313|EMBL:CAR29981.1};
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS   / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR29981.1, ECO:0000313|Proteomes:UP000008536};
RN   [1] {ECO:0000313|Proteomes:UP000008536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC   Y-229 {ECO:0000313|Proteomes:UP000008536};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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; CU928179; CAR29981.1; -; Genomic_DNA.
DR   RefSeq; XP_002498914.1; XM_002498869.1.
DR   AlphaFoldDB; C5E1J7; -.
DR   STRING; 559307.C5E1J7; -.
DR   GeneID; 8206750; -.
DR   KEGG; zro:ZYRO0G21538g; -.
DR   HOGENOM; CLU_034311_2_0_1; -.
DR   InParanoid; C5E1J7; -.
DR   Proteomes; UP000008536; Chromosome G.
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:SF26; FAD DEPENDENT OXIDOREDUCTASE SUPERFAMILY (AFU_ORTHOLOGUE AFUA_5G13940); 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:UP000008536}.
FT   DOMAIN          18..358
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   BINDING         62..63
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         212
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ   SEQUENCE   369 AA;  41061 MW;  662A0AB5047C0DE1 CRC64;
     MSKPHLISLS LIPPPMSHVV VAGAGVIGLS IAHQLLLQNS KIQKVTIIAK DFPHDLLTCE
     YTSPWAGAHF RPYPHKPESW ENDAREANYT RVTQQFFEKF AALNPDSTIK FSKGTDFLEA
     PSKEYLELGS GYNADSLKEF KVLEKLPDGV KFGAEYLTFC LDAPEYLKFL QNAIEQLCKL
     QNIQLQFVKL TLPSLKYIKE LYPDVSLIFN ATANGLQYNG SYDPACFKIR GQTLLLNVTQ
     PTPYNRKTIT HQSKDGHWTF VIRRSATHYI LGGTKQPGDD YPLPRESDTV KILSRASKVF
     PDLDTSDIIR VNVGFRPARR GGSRVDKSLH EGLPVVHAYG LGGSGFETSV GVAKHALELA
     GLGRLESKL
//
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