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Protein

D-amino-acid oxidase

Gene

DAO1

Organism
Rhodosporidium toruloides (Yeast) (Rhodotorula gracilis)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme can effectively convert cephalosporin C into 7-beta-(5-carboxy-5-oxopentanamido)-cephalosporinic acid.

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei162FAD; via amide nitrogen and carbonyl oxygen1
Binding sitei179FAD1
Binding sitei223Substrate1
Binding sitei285Substrate1
Binding sitei335Substrate; via carbonyl oxygen1
Binding sitei339FAD; via amide nitrogen1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi7 – 21FADAdd BLAST15
Nucleotide bindingi35 – 36FAD2
Nucleotide bindingi47 – 48FAD2
Nucleotide bindingi52 – 54FAD3
Nucleotide bindingi334 – 338FAD5

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.4.3.3. 5424.
SABIO-RKP80324.

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:DAO1
OrganismiRhodosporidium toruloides (Yeast) (Rhodotorula gracilis)
Taxonomic identifieri5286 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaPucciniomycotinaMicrobotryomycetesSporidiobolalesSporidiobolaceaeRhodotorula

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001627671 – 368D-amino-acid oxidaseAdd BLAST368

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1368
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Helixi14 – 25Combined sources12
Beta strandi29 – 36Combined sources8
Helixi48 – 50Combined sources3
Turni61 – 63Combined sources3
Helixi65 – 81Combined sources17
Turni82 – 85Combined sources4
Beta strandi86 – 99Combined sources14
Helixi100 – 106Combined sources7
Turni107 – 111Combined sources5
Beta strandi116 – 118Combined sources3
Helixi120 – 122Combined sources3
Beta strandi128 – 136Combined sources9
Helixi139 – 152Combined sources14
Beta strandi156 – 159Combined sources4
Helixi165 – 167Combined sources3
Beta strandi173 – 177Combined sources5
Helixi180 – 184Combined sources5
Beta strandi194 – 205Combined sources12
Beta strandi212 – 214Combined sources3
Beta strandi222 – 227Combined sources6
Turni228 – 230Combined sources3
Beta strandi231 – 235Combined sources5
Helixi249 – 262Combined sources14
Helixi264 – 266Combined sources3
Beta strandi267 – 271Combined sources5
Helixi272 – 274Combined sources3
Beta strandi276 – 288Combined sources13
Beta strandi293 – 302Combined sources10
Turni305 – 307Combined sources3
Beta strandi323 – 331Combined sources9
Helixi334 – 336Combined sources3
Helixi337 – 359Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C0IX-ray1.90A1-361[»]
1C0KX-ray1.46A1-361[»]
1C0LX-ray1.73A1-361[»]
1C0PX-ray1.20A1-361[»]
2DZGmodel-@1-368[»]
ProteinModelPortaliP80324.
SMRiP80324.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80324.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi366 – 368Microbody targeting signalSequence analysis3

Sequence similaritiesi

Belongs to the DAMOX/DASOX family.Curated

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR006181. D-amino_acid_oxidase_CS.
IPR023209. DAO.
IPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PANTHERiPTHR11530. PTHR11530. 2 hits.
PfamiPF01266. DAO. 1 hit.
[Graphical view]
PIRSFiPIRSF000189. D-aa_oxidase. 1 hit.
PROSITEiPS00677. DAO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80324-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSQKRVVVL GSGVIGLSSA LILARKGYSV HILARDLPED VSSQTFASPW
60 70 80 90 100
AGANWTPFMT LTDGPRQAKW EESTFKKWVE LVPTGHAMWL KGTRRFAQNE
110 120 130 140 150
DGLLGHWYKD ITPNYRPLPS SECPPGAIGV TYDTLSVHAP KYCQYLAREL
160 170 180 190 200
QKLGATFERR TVTSLEQAFD GADLVVNATG LGAKSIAGID DQAAEPIRGQ
210 220 230 240 250
TVLVKSPCKR CTMDSSDPAS PAYIIPRPGG EVICGGTYGV GDWDLSVNPE
260 270 280 290 300
TVQRILKHCL RLDPTISSDG TIEGIEVLRH NVGLRPARRG GPRVEAERIV
310 320 330 340 350
LPLDRTKSPL SLGRGSARAA KEKEVTLVHA YGFSSAGYQQ SWGAAEDVAQ
360
LVDEAFQRYH GAARESKL
Length:368
Mass (Da):40,076
Last modified:November 1, 1995 - v1
Checksum:i99940118BCFA886E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60066 mRNA. Translation: AAB51107.1.
Z71657 Genomic DNA. Translation: CAA96323.1.
AF003339 mRNA. Translation: AAB93974.1.
AF003340 Genomic DNA. Translation: AAB93975.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60066 mRNA. Translation: AAB51107.1.
Z71657 Genomic DNA. Translation: CAA96323.1.
AF003339 mRNA. Translation: AAB93974.1.
AF003340 Genomic DNA. Translation: AAB93975.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C0IX-ray1.90A1-361[»]
1C0KX-ray1.46A1-361[»]
1C0LX-ray1.73A1-361[»]
1C0PX-ray1.20A1-361[»]
2DZGmodel-@1-368[»]
ProteinModelPortaliP80324.
SMRiP80324.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.4.3.3. 5424.
SABIO-RKP80324.

Miscellaneous databases

EvolutionaryTraceiP80324.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR006181. D-amino_acid_oxidase_CS.
IPR023209. DAO.
IPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PANTHERiPTHR11530. PTHR11530. 2 hits.
PfamiPF01266. DAO. 1 hit.
[Graphical view]
PIRSFiPIRSF000189. D-aa_oxidase. 1 hit.
PROSITEiPS00677. DAO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiOXDA_RHOTO
AccessioniPrimary (citable) accession number: P80324
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.