ID G1R518_NOMLE Unreviewed; 314 AA.
AC G1R518;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=D-amino-acid oxidase {ECO:0000256|ARBA:ARBA00039751};
DE EC=1.4.3.3 {ECO:0000256|ARBA:ARBA00039101};
GN Name=DAO {ECO:0000313|Ensembl:ENSNLEP00000008290.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000008290.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000008290.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000008290.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Regulates the level of the neuromodulator D-serine in the
CC brain. Has high activity towards D-DOPA and contributes to dopamine
CC synthesis. Could act as a detoxifying agent which removes D-amino acids
CC accumulated during aging. Acts on a variety of D-amino acids with a
CC preference for those having small hydrophobic side chains followed by
CC those bearing polar, aromatic, and basic groups. Does not act on acidic
CC amino acids. {ECO:0000256|ARBA:ARBA00037529}.
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 Evidence={ECO:0000256|ARBA:ARBA00036675};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000189-1};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC {ECO:0000256|ARBA:ARBA00006730}.
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DR EMBL; ADFV01052965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01052966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01052967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1R518; -.
DR STRING; 61853.ENSNLEP00000008290; -.
DR Ensembl; ENSNLET00000008681.2; ENSNLEP00000008290.2; ENSNLEG00000006814.2.
DR eggNOG; KOG3923; Eukaryota.
DR GeneTree; ENSGT00390000018635; -.
DR HOGENOM; CLU_034311_0_1_1; -.
DR InParanoid; G1R518; -.
DR OMA; LWWPYRI; -.
DR TreeFam; TF313887; -.
DR Proteomes; UP000001073; Chromosome 10.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:Ensembl.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:Ensembl.
DR GO; GO:0071949; F:FAD binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0055130; P:D-alanine catabolic process; IEA:Ensembl.
DR GO; GO:0036088; P:D-serine catabolic process; IEA:Ensembl.
DR GO; GO:0042416; P:dopamine biosynthetic process; IEA:Ensembl.
DR GO; GO:0006562; P:proline catabolic process; IEA:Ensembl.
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:SF15; D-AMINO-ACID OXIDASE; 1.
DR Pfam; PF01266; DAO; 1.
DR PIRSF; PIRSF000189; D-aa_oxidase; 2.
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 Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..314
FT /note="D-amino-acid oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014172838"
FT DOMAIN 2..270
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 37..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 44..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 49..51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 164
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 279..284
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ SEQUENCE 314 AA; 35559 MW; 2AB1F2747F306CBA CRC64;
MRVVVIGAGV IGLSTALCIH ECYHSLLQPL DIKVYADRFT PLTTTDVAAG LWQPYLSDPS
NPQEADWSQQ TFDYLLSHVH SPNAEKLGLF LISGYNLFHE AIPDPFWKDT VLGFRKLTPR
ELDMFPDYGY GWFHTSLILE GKNYLQWLTE RLTERGVKFF QRKVESFEEV AREGADVIVN
STGVWAGALQ PDPLLQPGRG QIIKVDAPWM KHFILTHDPE RGIYNSPYII PGTQTVTLGG
IFQLGNWSEL NNIQDHNTIW EGCCRLEPTL KVIHNYGHGG YGLTIHWGCA LEAAKLFGRI
LEEKKLSRMP PSHL
//
