Hmdb loader
Identification
HMDB Protein ID HMDBP00206
Secondary Accession Numbers
  • 5438
Name D-amino-acid oxidase
Synonyms
  1. DAAO
  2. DAMOX
  3. DAO
Gene Name DAO
Protein Type Unknown
Biological Properties
General Function Involved in D-amino-acid oxidase activity
Specific Function Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.
Pathways
  • Arginine and proline metabolism
  • Arginine and proline metabolism
  • Arginine: Glycine Amidinotransferase Deficiency (AGAT Deficiency)
  • Creatine deficiency, guanidinoacetate methyltransferase deficiency
  • D-Arginine and D-ornithine metabolism
  • D-Arginine and D-Ornithine Metabolism
  • Glycine, serine and threonine metabolism
  • Guanidinoacetate Methyltransferase Deficiency (GAMT Deficiency)
  • Hyperornithinemia with gyrate atrophy (HOGA)
  • Hyperornithinemia-hyperammonemia-homocitrullinuria [HHH-syndrome]
  • Hyperprolinemia Type I
  • Hyperprolinemia Type II
  • L-arginine:glycine amidinotransferase deficiency
  • Ornithine Aminotransferase Deficiency (OAT Deficiency)
  • Peroxisome
  • Prolidase Deficiency (PD)
  • Prolinemia Type II
Reactions
A D-amino acid + Water + Oxygen → a 2-oxo acid + Ammonia + Hydrogen peroxide details
Glycine + Water + Oxygen → Glyoxylic acid + Ammonia + Hydrogen peroxide details
D-Ornithine + Water + Oxygen → 5-Amino-2-oxopentanoic acid + Ammonia + Hydrogen peroxide details
D-Proline + Oxygen → 1-Pyrroline-2-carboxylic acid + Hydrogen peroxide details
cis-4-Hydroxy-D-proline + Oxygen → 1-Pyrroline-4-hydroxy-2-carboxylate + Hydrogen peroxide details
Cephalosporin C + Water + Oxygen → (7R)-7-(5-Carboxy-5-oxopentanoyl)aminocephalosporinate + Ammonia + Hydrogen peroxide details
GO Classification
Biological Process
cellular nitrogen compound metabolic process
glyoxylate metabolic process
dopamine biosynthetic process
D-alanine catabolic process
D-serine catabolic process
leucine metabolic process
proline catabolic process
Cellular Component
cytosol
peroxisomal matrix
peroxisomal membrane
Function
binding
catalytic activity
oxidoreductase activity, acting on the ch-nh2 group of donors
oxidoreductase activity, acting on the ch-nh2 group of donors, oxygen as acceptor
d-amino-acid oxidase activity
oxidoreductase activity
Molecular Function
D-amino-acid oxidase activity
FAD binding
protein dimerization activity
Process
metabolic process
oxidation reduction
Cellular Location
  1. Peroxisome
Gene Properties
Chromosome Location 12
Locus 12q24
SNPs DAO
Gene Sequence
>1044 bp
ATGCGTGTGGTGGTGATTGGAGCAGGAGTCATCGGGCTGTCCACCGCCCTCTGCATCCAT
GAGCGCTACCACTCAGTCCTGCAGCCACTGCACATAAAGGTCTACGCGGACCGCTTCACC
CCACTCACCACCACCGACGTGGCTGCCGGCCTCTGGCAGCCCTACCTTTCTGACCCCAAC
AACCCACAGGAGGCGGACTGGAGCCAACAGACCTTTGACTATCTCCTGAGCCATGTCCAT
TCTCCCAACGCTGAAAACCTGGGCCTGTTCCTAATCTCGGGCTACAACCTCTTCCATGAA
GCCATTCCGGACCCTTCCTGGAAGGACACAGTTCTGGGATTTCGGAAGCTGACCCCCAGA
GAGCTGGATATGTTCCCAGATTACGGCTATGGCTGGTTCCACACAAGCCTAATTCTGGAG
GGAAAGAACTATCTACAGTGGCTGACTGAAAGGTTAACTGAGAGGGGAGTGAAGTTCTTC
CAGCGGAAAGTGGAGTCTTTTGAGGAGGTGGCAAGAGAAGGCGCAGACGTGATTGTCAAC
TGCACTGGGGTATGGGCTGGGGCGCTACAACGAGACCCCCTGCTGCAGCCAGGCCGGGGG
CAGATCATGAAGGTGGACGCCCCTTGGATGAAGCACTTCATTCTCACCCATGACCCAGAG
AGAGGCATCTACAATTCCCCGTACATCATCCCAGGGACCCAGACAGTTACTCTTGGAGGC
ATCTTCCAGTTGGGAAACTGGAGTGAACTAAACAATATCCAGGACCACAACACCATTTGG
GAAGGCTGCTGCAGACTGGAGCCCACACTGAAGAATGCAAGAATTATTGGTGAAGCAACT
GGCTTCCGGCCAGTACGCCCCCAGATTCGGCTAGAAAGAGAACAGCTTCGCACTGGACCT
TCAAACACAGAGGTCATCCACAACTATGGCCATGGAGGCTACGGGCTCACCATCCACTGG
GGATGTGCCCTGGAGGCAGCCAAGCTCTTTGGGAGAATCCTGGAAGAAAAGAAATTGTCC
AGAATGCCACCATCCCACCTCTGA
Protein Properties
Number of Residues 347
Molecular Weight 39473.75
Theoretical pI 6.844
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>D-amino-acid oxidase
MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAGLWQPYLSDPN
NPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPR
ELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVN
CTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGG
IFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGP
SNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLSRMPPSHL
GenBank ID Protein 30446
UniProtKB/Swiss-Prot ID P14920
UniProtKB/Swiss-Prot Entry Name OXDA_HUMAN
PDB IDs
GenBank Gene ID X13227
GeneCard ID DAO
GenAtlas ID DAO
HGNC ID HGNC:2671
References
General References
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  3. Momoi K, Fukui K, Watanabe F, Miyake Y: Molecular cloning and sequence analysis of cDNA encoding human kidney D-amino acid oxidase. FEBS Lett. 1988 Sep 26;238(1):180-4. [PubMed:2901986 ]
  4. Fukui K, Miyake Y: Molecular cloning and chromosomal localization of a human gene encoding D-amino-acid oxidase. J Biol Chem. 1992 Sep 15;267(26):18631-8. [PubMed:1356107 ]
  5. Kawazoe T, Tsuge H, Pilone MS, Fukui K: Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring. Protein Sci. 2006 Dec;15(12):2708-17. Epub 2006 Nov 6. [PubMed:17088322 ]
  6. Kawazoe T, Tsuge H, Imagawa T, Aki K, Kuramitsu S, Fukui K: Structural basis of D-DOPA oxidation by D-amino acid oxidase: alternative pathway for dopamine biosynthesis. Biochem Biophys Res Commun. 2007 Apr 6;355(2):385-91. Epub 2007 Feb 8. [PubMed:17303072 ]
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