OXDA_PIG
ID OXDA_PIG Reviewed; 347 AA.
AC P00371;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=D-amino-acid oxidase;
DE Short=DAAO;
DE Short=DAMOX;
DE Short=DAO;
DE EC=1.4.3.3;
GN Name=DAO;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Kidney;
RX PubMed=6124543; DOI=10.1016/s0021-9258(18)34204-2;
RA Ronchi S., Minchiotti L., Galliano M., Curti B., Swenson R.P.,
RA Williams C.H. Jr., Massey V.;
RT "The primary structure of D-amino acid oxidase from pig kidney. II.
RT Isolation and sequence of overlap peptides and the complete sequence.";
RL J. Biol. Chem. 257:8824-8834(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=2888479; DOI=10.1021/bi00386a054;
RA Fukui K., Watanabe F., Shibata T., Miyake Y.;
RT "Molecular cloning and sequence analysis of cDNAs encoding porcine kidney
RT D-amino acid oxidase.";
RL Biochemistry 26:3612-3618(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2893757; DOI=10.1016/0378-1119(87)90266-6;
RA Jacobs P., Brockly F., Massaer M., Loriau R., Guillaume J.P.,
RA Ciccarelli E., Heinderyckx M., Cravador A., Biemans R., van Elsen A.,
RA Herzog A., Bollen A.;
RT "Porcine D-amino acid oxidase: determination of the mRNA nucleotide
RT sequence by the characterization of genomic and cDNA clones.";
RL Gene 59:55-61(1987).
RN [4]
RP PROTEIN SEQUENCE.
RC TISSUE=Kidney;
RX PubMed=2905598; DOI=10.1042/bj2550907;
RA Nicholson B.H., Batra S.P.;
RT "Structural interpretation of the binding of 9-azidoacridine to D-amino
RT acid oxidase.";
RL Biochem. J. 255:907-912(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 1-14.
RX PubMed=2575382; DOI=10.1016/0006-291x(89)92762-9;
RA Watanabe F., Fukui K., Momoi K., Miyake Y.;
RT "Expression of normal and abnormal porcine kidney D-amino acid oxidase in
RT Escherichia coli: purification and characterization of the enzymes.";
RL Biochem. Biophys. Res. Commun. 165:1422-1427(1989).
RN [6]
RP CATALYTIC ACTIVITY, COFACTOR, AND INHIBITION BY CHEMICAL MODIFICATION.
RX PubMed=6120171; DOI=10.1016/s0021-9258(19)68129-9;
RA Swenson R.P., Williams C.H. Jr., Massey V.;
RT "Chemical modification of D-amino acid oxidase. Amino acid sequence of the
RT tryptic peptides containing tyrosine and lysine residues modified by
RT fluorodinitrobenzene.";
RL J. Biol. Chem. 257:1937-1944(1982).
RN [7]
RP CATALYTIC ACTIVITY, AND INHIBITION BY CHEMICAL MODIFICATION.
RX PubMed=6129252; DOI=10.1016/s0021-9258(18)33283-6;
RA Swenson R.P., Williams C.H. Jr., Massey V.;
RT "Identification of the histidine residue in D-amino acid oxidase that is
RT covalently modified during inactivation by 5-dimethylaminonaphthalene-1-
RT sulfonyl chloride.";
RL J. Biol. Chem. 258:497-502(1983).
RN [8]
RP MUTAGENESIS OF TYR-55; MET-110 AND HIS-217.
RX PubMed=2901989; DOI=10.1016/0014-5793(88)80494-0;
RA Watanabe F., Fukui K., Momoi K., Miyake Y.;
RT "Effect of site-specific mutagenesis of tyrosine-55, methionine-110 and
RT histidine-217 in porcine kidney D-amino acid oxidase on its catalytic
RT function.";
RL FEBS Lett. 238:269-272(1988).
RN [9]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-228 AND HIS-307.
RX PubMed=1673125; DOI=10.1093/oxfordjournals.jbchem.a123340;
RA Miyano M., Fukui K., Watanabe F., Takahashi S., Tada M., Kanashiro M.,
RA Miyake Y.;
RT "Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney D-
RT amino acid oxidase: expression, purification, and characterization.";
RL J. Biochem. 109:171-177(1991).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=8864836; DOI=10.1093/oxfordjournals.jbchem.a021376;
RA Mizutani H., Miyahara I., Hirotsu K., Nishima Y., Shiga K., Setoyama C.,
RA Miura R.;
RT "Three-dimensional structure of porcine kidney D-amino acid oxidase at 3.0-
RT A resolution.";
RL J. Biochem. 120:14-17(1996).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FAD AND BENZOATE.
RX PubMed=8755502; DOI=10.1073/pnas.93.15.7496;
RA Mattevi A., Vanoni M.A., Todone F., Rizzi M., Teplyakov A., Coda A.,
RA Bolognesi M., Curti B.;
RT "Crystal structure of D-amino acid oxidase: a case of active site mirror-
RT image convergent evolution with flavocytochrome b2.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7496-7501(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEXES WITH FAD; D-ARGININE;
RP IMINO-TRYPTOPHAN AND 3-METHYL-2-OXOBUTYRIC ACID, SUBUNIT, AND ENZYME
RP MECHANISM.
RX PubMed=9153426; DOI=10.1021/bi9630570;
RA Todone F., Vanoni M.A., Mozzarelli A., Bolognesi M., Coda A., Curti B.,
RA Mattevi A.;
RT "Active site plasticity in D-amino acid oxidase: a crystallographic
RT analysis.";
RL Biochemistry 36:5853-5860(1997).
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.
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; Evidence={ECO:0000269|PubMed:1673125,
CC ECO:0000269|PubMed:6120171, ECO:0000269|PubMed:6129252};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:6120171};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8755502,
CC ECO:0000269|PubMed:9153426}.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/DAOFF/";
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DR EMBL; M16972; AAA30985.1; -; mRNA.
DR EMBL; M18447; AAA31025.1; -; Genomic_DNA.
DR EMBL; M18444; AAA31025.1; JOINED; Genomic_DNA.
DR EMBL; M18445; AAA31025.1; JOINED; Genomic_DNA.
DR EMBL; M18446; AAA31025.1; JOINED; Genomic_DNA.
DR EMBL; M18448; AAA31026.1; -; mRNA.
DR PIR; A29598; OXPGDA.
DR PIR; A33798; A33798.
DR RefSeq; NP_999231.1; NM_214066.2.
DR PDB; 1AN9; X-ray; 2.50 A; A/B=1-340.
DR PDB; 1DAO; X-ray; 3.20 A; A/B/C/D/E/F/G/H=1-347.
DR PDB; 1DDO; X-ray; 3.10 A; A/B/C/D/E/F/G/H=1-347.
DR PDB; 1EVI; X-ray; 2.50 A; A/B=1-340.
DR PDB; 1KIF; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-347.
DR PDB; 1VE9; X-ray; 2.50 A; A/B=1-347.
DR PDB; 3WGT; X-ray; 1.88 A; A/B=1-347.
DR PDB; 4YJD; X-ray; 2.30 A; A/B=1-340.
DR PDB; 4YJF; X-ray; 2.20 A; A=1-341, B=1-339.
DR PDB; 4YJG; X-ray; 2.50 A; A=1-341, B=1-340.
DR PDB; 4YJH; X-ray; 2.70 A; A/B=1-340.
DR PDB; 5WWV; X-ray; 3.20 A; A/B/C/D/E/F/G/H=1-347.
DR PDB; 5WX2; X-ray; 3.00 A; A/B/C/D/E/F/G/H=1-347.
DR PDBsum; 1AN9; -.
DR PDBsum; 1DAO; -.
DR PDBsum; 1DDO; -.
DR PDBsum; 1EVI; -.
DR PDBsum; 1KIF; -.
DR PDBsum; 1VE9; -.
DR PDBsum; 3WGT; -.
DR PDBsum; 4YJD; -.
DR PDBsum; 4YJF; -.
DR PDBsum; 4YJG; -.
DR PDBsum; 4YJH; -.
DR PDBsum; 5WWV; -.
DR PDBsum; 5WX2; -.
DR AlphaFoldDB; P00371; -.
DR SMR; P00371; -.
DR BioGRID; 1149269; 1.
DR STRING; 9823.ENSSSCP00000010609; -.
DR BindingDB; P00371; -.
DR ChEMBL; CHEMBL6172; -.
DR DrugCentral; P00371; -.
DR PaxDb; P00371; -.
DR PeptideAtlas; P00371; -.
DR PRIDE; P00371; -.
DR Ensembl; ENSSSCT00005072766; ENSSSCP00005045526; ENSSSCG00005045054.
DR Ensembl; ENSSSCT00015010951; ENSSSCP00015004305; ENSSSCG00015008169.
DR Ensembl; ENSSSCT00070005965; ENSSSCP00070004870; ENSSSCG00070003140.
DR GeneID; 397134; -.
DR KEGG; ssc:397134; -.
DR CTD; 1610; -.
DR eggNOG; KOG3923; Eukaryota.
DR HOGENOM; CLU_034311_0_1_1; -.
DR InParanoid; P00371; -.
DR OMA; LWWPYRI; -.
DR OrthoDB; 1363414at2759; -.
DR TreeFam; TF313887; -.
DR BRENDA; 1.4.3.3; 6170.
DR Reactome; R-SSC-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-SSC-9033241; Peroxisomal protein import.
DR SABIO-RK; P00371; -.
DR EvolutionaryTrace; P00371; -.
DR PRO; PR:P00371; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 14.
DR Genevisible; P00371; SS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0055130; P:D-alanine catabolic process; IBA:GO_Central.
DR GO; GO:0019478; P:D-amino acid catabolic process; IDA:UniProtKB.
DR GO; GO:0036088; P:D-serine catabolic process; IBA:GO_Central.
DR GO; GO:0006562; P:proline catabolic process; IBA:GO_Central.
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 3D-structure; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase;
KW Peroxisome; Reference proteome.
FT CHAIN 1..347
FT /note="D-amino-acid oxidase"
FT /id="PRO_0000162763"
FT MOTIF 345..347
FT /note="Microbody targeting signal"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8755502"
FT BINDING 37..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8755502"
FT BINDING 44..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8755502"
FT BINDING 49..51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8755502"
FT BINDING 53
FT /ligand="substrate"
FT BINDING 164
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8755502"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8755502"
FT BINDING 217
FT /ligand="substrate"
FT BINDING 228
FT /ligand="substrate"
FT BINDING 283
FT /ligand="substrate"
FT BINDING 312..316
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8755502"
FT BINDING 313
FT /ligand="substrate"
FT BINDING 317
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8755502"
FT MUTAGEN 55
FT /note="Y->F: No effect."
FT /evidence="ECO:0000269|PubMed:2901989"
FT MUTAGEN 110
FT /note="M->L: No effect."
FT /evidence="ECO:0000269|PubMed:2901989"
FT MUTAGEN 217
FT /note="H->L: No effect."
FT /evidence="ECO:0000269|PubMed:2901989"
FT MUTAGEN 228
FT /note="Y->F: Reduces activity."
FT /evidence="ECO:0000269|PubMed:1673125"
FT MUTAGEN 307
FT /note="H->L: Reduces activity."
FT /evidence="ECO:0000269|PubMed:1673125"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3WGT"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:3WGT"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:3WGT"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1AN9"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:3WGT"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1AN9"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:3WGT"
FT HELIX 63..77
FT /evidence="ECO:0007829|PDB:3WGT"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:3WGT"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:3WGT"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3WGT"
FT STRAND 89..100
FT /evidence="ECO:0007829|PDB:3WGT"
FT TURN 106..110
FT /evidence="ECO:0007829|PDB:3WGT"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:3WGT"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3WGT"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1DDO"
FT STRAND 129..139
FT /evidence="ECO:0007829|PDB:3WGT"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:3WGT"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:3WGT"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:3WGT"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3WGT"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:3WGT"
FT STRAND 196..206
FT /evidence="ECO:0007829|PDB:3WGT"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:3WGT"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:3WGT"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:1DDO"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:3WGT"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:3WGT"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:3WGT"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:3WGT"
FT STRAND 274..285
FT /evidence="ECO:0007829|PDB:3WGT"
FT STRAND 290..298
FT /evidence="ECO:0007829|PDB:3WGT"
FT STRAND 301..309
FT /evidence="ECO:0007829|PDB:3WGT"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:4YJF"
FT HELIX 315..336
FT /evidence="ECO:0007829|PDB:3WGT"
SQ SEQUENCE 347 AA; 39336 MW; 0EC6577BDB2BF46C CRC64;
MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DVKVYADRFT PFTTTDVAAG LWQPYTSEPS
NPQEANWNQQ TFNYLLSHIG SPNAANMGLT PVSGYNLFRE AVPDPYWKDM VLGFRKLTPR
ELDMFPDYRY GWFNTSLILE GRKYLQWLTE RLTERGVKFF LRKVESFEEV ARGGADVIIN
CTGVWAGVLQ PDPLLQPGRG QIIKVDAPWL KNFIITHDLE RGIYNSPYII PGLQAVTLGG
TFQVGNWNEI NNIQDHNTIW EGCCRLEPTL KDAKIVGEYT GFRPVRPQVR LEREQLRFGS
SNTEVIHNYG HGGYGLTIHW GCALEVAKLF GKVLEERNLL TMPPSHL
