ID A0A2U3X2B5_ODORO Unreviewed; 347 AA.
AC A0A2U3X2B5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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|RefSeq:XP_004416224.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004416224.1};
RN [1] {ECO:0000313|RefSeq:XP_004416224.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_004416224.1; XM_004416167.1.
DR AlphaFoldDB; A0A2U3X2B5; -.
DR STRING; 9708.A0A2U3X2B5; -.
DR GeneID; 101364868; -.
DR KEGG; oro:101364868; -.
DR CTD; 1610; -.
DR InParanoid; A0A2U3X2B5; -.
DR OrthoDB; 5359at2759; -.
DR Proteomes; UP000245340; Unplaced.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProt.
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; 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 Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000245340}.
FT DOMAIN 2..329
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 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 283
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 312..317
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ SEQUENCE 347 AA; 39240 MW; E3AF5CAED51324A1 CRC64;
MRVVVIGAGV IGLSTALCIH ERYHSVLPSL DVRVYSDRFT PFTNSNVAAG LCQAYLADPS
NPQEVHWNQQ TFDYLLSHIH SPNAANMGLA LISGYNLFRE DFPDPSWRDT VLGFRKLTCR
ELDMFPDYSY GWFNTSLIVE GRRYLPWLTE RLTERGVKFF QQKVESFEEV ARGGADVIIN
CTGVWAGALQ PDPLLKPGRG QIIKVDAPWM KHFILTHDAE KGIYQSPYII PGIQAVTLGG
IFQLGNWSEV NNIQDHNTIW EGCCRLEPSL KDAKIIAELT GLRPVRPQIR LEREKLRFGS
LNTEVIHNYG HGGYGLTIHW GCALEAAKLF GKILEERKLL RMPPPHL
//
