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Protein

D-amino-acid oxidase

Gene

DAO

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

A D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.3 Publications

Cofactori

FAD1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei53Substrate1
Binding sitei164FAD; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei182FAD1 Publication1
Binding sitei217Substrate1
Binding sitei228Substrate1
Binding sitei283Substrate1
Binding sitei313Substrate; via carbonyl oxygen1
Binding sitei317FAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi3 – 17FAD1 PublicationAdd BLAST15
Nucleotide bindingi37 – 38FAD1 Publication2
Nucleotide bindingi44 – 45FAD1 Publication2
Nucleotide bindingi49 – 51FAD1 Publication3
Nucleotide bindingi312 – 316FAD1 Publication5

GO - Molecular functioni

  • D-amino-acid oxidase activity Source: UniProtKB
  • FAD binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.4.3.3. 6170.
ReactomeiR-SSC-389661. Glyoxylate metabolism and glycine degradation.
SABIO-RKP00371.

Names & Taxonomyi

Protein namesi
Recommended name:
D-amino-acid oxidase (EC:1.4.3.3)
Short name:
DAAO
Short name:
DAMOX
Short name:
DAO
Gene namesi
Name:DAO
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 14

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi55Y → F: No effect. 1 Publication1
Mutagenesisi110M → L: No effect. 1 Publication1
Mutagenesisi217H → L: No effect. 1 Publication1
Mutagenesisi228Y → F: Reduces activity. 1 Publication1
Mutagenesisi307H → L: Reduces activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL6172.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001627631 – 347D-amino-acid oxidaseAdd BLAST347

Proteomic databases

PaxDbiP00371.
PeptideAtlasiP00371.
PRIDEiP00371.

Miscellaneous databases

PMAP-CutDBP00371.

Expressioni

Gene expression databases

BgeeiENSSSCG00000009942.
GenevisibleiP00371. SS.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000010609.

Chemistry databases

BindingDBiP00371.

Structurei

Secondary structure

1347
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi10 – 23Combined sources14
Turni24 – 26Combined sources3
Beta strandi27 – 29Combined sources3
Beta strandi31 – 37Combined sources7
Helixi40 – 42Combined sources3
Helixi44 – 47Combined sources4
Helixi63 – 77Combined sources15
Turni78 – 80Combined sources3
Turni82 – 84Combined sources3
Helixi85 – 87Combined sources3
Beta strandi89 – 100Combined sources12
Turni106 – 110Combined sources5
Beta strandi111 – 116Combined sources6
Helixi119 – 122Combined sources4
Beta strandi125 – 127Combined sources3
Beta strandi129 – 139Combined sources11
Helixi141 – 154Combined sources14
Beta strandi158 – 161Combined sources4
Helixi167 – 172Combined sources6
Beta strandi176 – 180Combined sources5
Helixi183 – 188Combined sources6
Beta strandi196 – 206Combined sources11
Beta strandi212 – 216Combined sources5
Turni219 – 221Combined sources3
Turni222 – 224Combined sources3
Beta strandi228 – 231Combined sources4
Beta strandi233 – 239Combined sources7
Helixi253 – 266Combined sources14
Helixi268 – 272Combined sources5
Beta strandi274 – 285Combined sources12
Beta strandi290 – 298Combined sources9
Beta strandi301 – 309Combined sources9
Helixi312 – 314Combined sources3
Helixi315 – 336Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AN9X-ray2.50A/B1-340[»]
1DAOX-ray3.20A/B/C/D/E/F/G/H1-347[»]
1DDOX-ray3.10A/B/C/D/E/F/G/H1-347[»]
1EVIX-ray2.50A/B1-340[»]
1KIFX-ray2.60A/B/C/D/E/F/G/H1-347[»]
1VE9X-ray2.50A/B1-347[»]
3WGTX-ray1.88A/B1-347[»]
4YJDX-ray2.30A/B1-340[»]
4YJFX-ray2.20A1-341[»]
B1-339[»]
4YJGX-ray2.50A1-341[»]
B1-340[»]
4YJHX-ray2.70A/B1-340[»]
ProteinModelPortaliP00371.
SMRiP00371.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00371.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi345 – 347Microbody targeting signal3

Sequence similaritiesi

Belongs to the DAMOX/DASOX family.Curated

Phylogenomic databases

eggNOGiKOG3923. Eukaryota.
COG0665. LUCA.
GeneTreeiENSGT00390000018635.
HOGENOMiHOG000046303.
HOVERGENiHBG003493.
InParanoidiP00371.
KOiK00273.
OMAiRARCIHN.
OrthoDBiEOG091G0G0Y.
TreeFamiTF313887.

Family and domain databases

Gene3Di3.40.50.720. 3 hits.
InterProiIPR006181. D-amino_acid_oxidase_CS.
IPR023209. DAO.
IPR006076. FAD-dep_OxRdtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11530. PTHR11530. 1 hit.
PfamiPF01266. DAO. 1 hit.
[Graphical view]
PIRSFiPIRSF000189. D-aa_oxidase. 1 hit.
PROSITEiPS00677. DAO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00371-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DVKVYADRFT PFTTTDVAAG
60 70 80 90 100
LWQPYTSEPS NPQEANWNQQ TFNYLLSHIG SPNAANMGLT PVSGYNLFRE
110 120 130 140 150
AVPDPYWKDM VLGFRKLTPR ELDMFPDYRY GWFNTSLILE GRKYLQWLTE
160 170 180 190 200
RLTERGVKFF LRKVESFEEV ARGGADVIIN CTGVWAGVLQ PDPLLQPGRG
210 220 230 240 250
QIIKVDAPWL KNFIITHDLE RGIYNSPYII PGLQAVTLGG TFQVGNWNEI
260 270 280 290 300
NNIQDHNTIW EGCCRLEPTL KDAKIVGEYT GFRPVRPQVR LEREQLRFGS
310 320 330 340
SNTEVIHNYG HGGYGLTIHW GCALEVAKLF GKVLEERNLL TMPPSHL
Length:347
Mass (Da):39,336
Last modified:July 1, 1989 - v2
Checksum:i0EC6577BDB2BF46C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16972 mRNA. Translation: AAA30985.1.
M18447
, M18444, M18445, M18446 Genomic DNA. Translation: AAA31025.1.
M18448 mRNA. Translation: AAA31026.1.
PIRiA29598. OXPGDA.
A33798.
RefSeqiNP_999231.1. NM_214066.2.
UniGeneiSsc.232.

Genome annotation databases

EnsembliENSSSCT00000010894; ENSSSCP00000010609; ENSSSCG00000009942.
GeneIDi397134.
KEGGissc:397134.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16972 mRNA. Translation: AAA30985.1.
M18447
, M18444, M18445, M18446 Genomic DNA. Translation: AAA31025.1.
M18448 mRNA. Translation: AAA31026.1.
PIRiA29598. OXPGDA.
A33798.
RefSeqiNP_999231.1. NM_214066.2.
UniGeneiSsc.232.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AN9X-ray2.50A/B1-340[»]
1DAOX-ray3.20A/B/C/D/E/F/G/H1-347[»]
1DDOX-ray3.10A/B/C/D/E/F/G/H1-347[»]
1EVIX-ray2.50A/B1-340[»]
1KIFX-ray2.60A/B/C/D/E/F/G/H1-347[»]
1VE9X-ray2.50A/B1-347[»]
3WGTX-ray1.88A/B1-347[»]
4YJDX-ray2.30A/B1-340[»]
4YJFX-ray2.20A1-341[»]
B1-339[»]
4YJGX-ray2.50A1-341[»]
B1-340[»]
4YJHX-ray2.70A/B1-340[»]
ProteinModelPortaliP00371.
SMRiP00371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000010609.

Chemistry databases

BindingDBiP00371.
ChEMBLiCHEMBL6172.

Proteomic databases

PaxDbiP00371.
PeptideAtlasiP00371.
PRIDEiP00371.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000010894; ENSSSCP00000010609; ENSSSCG00000009942.
GeneIDi397134.
KEGGissc:397134.

Organism-specific databases

CTDi1610.

Phylogenomic databases

eggNOGiKOG3923. Eukaryota.
COG0665. LUCA.
GeneTreeiENSGT00390000018635.
HOGENOMiHOG000046303.
HOVERGENiHBG003493.
InParanoidiP00371.
KOiK00273.
OMAiRARCIHN.
OrthoDBiEOG091G0G0Y.
TreeFamiTF313887.

Enzyme and pathway databases

BRENDAi1.4.3.3. 6170.
ReactomeiR-SSC-389661. Glyoxylate metabolism and glycine degradation.
SABIO-RKP00371.

Miscellaneous databases

EvolutionaryTraceiP00371.
PMAP-CutDBP00371.
PROiP00371.

Gene expression databases

BgeeiENSSSCG00000009942.
GenevisibleiP00371. SS.

Family and domain databases

Gene3Di3.40.50.720. 3 hits.
InterProiIPR006181. D-amino_acid_oxidase_CS.
IPR023209. DAO.
IPR006076. FAD-dep_OxRdtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11530. PTHR11530. 1 hit.
PfamiPF01266. DAO. 1 hit.
[Graphical view]
PIRSFiPIRSF000189. D-aa_oxidase. 1 hit.
PROSITEiPS00677. DAO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiOXDA_PIG
AccessioniPrimary (citable) accession number: P00371
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.