ID   OXDA_FUSVN              Reviewed;         361 AA.
AC   P24552;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=D-amino-acid oxidase;
DE            Short=DAAO;
DE            Short=DAMOX;
DE            Short=DAO;
DE            EC=1.4.3.3;
OS   Fusarium vanettenii (Neocosmospora pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2747968;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=M-0718 / FERM P-2688;
RX   PubMed=1982443; DOI=10.1093/oxfordjournals.jbchem.a123306;
RA   Isogai T., Ono H., Ishitani Y., Kojo H., Ueda Y., Kohsaka M.;
RT   "Structure and expression of cDNA for D-amino acid oxidase active against
RT   cephalosporin C from Fusarium solani.";
RL   J. Biochem. 108:1063-1069(1990).
CC   -!- FUNCTION: This enzyme can effectively convert cephalosporin C into 7-
CC       beta-(5-carboxy-5-oxopentanamido)-cephalosporinic acid.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC         ChEBI:CHEBI:59871; EC=1.4.3.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000305}.
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DR   EMBL; D00809; BAA00692.1; -; mRNA.
DR   PIR; JX0152; JX0152.
DR   AlphaFoldDB; P24552; -.
DR   SMR; P24552; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:UniProtKB-EC.
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   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase; Peroxisome.
FT   CHAIN           1..361
FT                   /note="D-amino-acid oxidase"
FT                   /id="PRO_0000162766"
FT   MOTIF           359..361
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   BINDING         5..19
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         34..35
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         45..46
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         50..52
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         332..336
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   361 AA;  39696 MW;  148119480E2A67A5 CRC64;
     MSNTIVVVGA GVIGLTSALL LSKNKGNKIT VVAKHMPGDY DVEYASPFAG ANHSPMATEE
     SSEWERRTWY EFKRLVEEVP EAGVHFQKSR IQRRNVDTEK AQRSGFPDAL FSKEPWFKNM
     FEDFREQHPS EVIPGYDSGC EFTSVCINTA IYLPWLLGQC IKNGVIVKRA ILNDISEAKK
     LSHAGKTPNI IVNATGLGSY KLGGVEDKTM APARGQIVVV RNESSPMLLT SGVEDGGADV
     MYLMQRAAGG GTILGGTYDV GNWESQPDPN IANRIMQRIV EVRPEIANGK GVKGLSVIRH
     AVGMRPWRKD GVRIEEEKLD DETWIVHNYG HSGWGYQGSY GCAENVVQLV DKVGKAAKSK
     L