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P80324 (OXDA_RHOTO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
D-amino-acid oxidase

Short name=DAAO
Short name=DAMOX
Short name=DAO
EC=1.4.3.3
Gene names
Name:DAO1
OrganismRhodosporidium toruloides (Yeast) (Rhodotorula gracilis)
Taxonomic identifier5286 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaPucciniomycotinaMicrobotryomycetesSporidiobolalesRhodosporidium

Protein attributes

Sequence length368 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

FAD.

Subunit structure

Homodimer.

Subcellular location

Peroxisome Potential.

Sequence similarities

Belongs to the DAMOX/DASOX family.

Ontologies

Keywords
   Cellular componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionD-amino-acid oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 368368D-amino-acid oxidase
PRO_0000162767

Regions

Nucleotide binding7 – 2115FAD
Nucleotide binding35 – 362FAD
Nucleotide binding47 – 482FAD
Nucleotide binding52 – 543FAD
Nucleotide binding334 – 3385FAD
Motif366 – 3683Microbody targeting signal Potential

Sites

Binding site1621FAD; via amide nitrogen and carbonyl oxygen
Binding site1791FAD
Binding site2231Substrate
Binding site2851Substrate
Binding site3351Substrate; via carbonyl oxygen
Binding site3391FAD; via amide nitrogen

Secondary structure

.......................................................... 368
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80324 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 99940118BCFA886E

FASTA36840,076
        10         20         30         40         50         60 
MHSQKRVVVL GSGVIGLSSA LILARKGYSV HILARDLPED VSSQTFASPW AGANWTPFMT 

        70         80         90        100        110        120 
LTDGPRQAKW EESTFKKWVE LVPTGHAMWL KGTRRFAQNE DGLLGHWYKD ITPNYRPLPS 

       130        140        150        160        170        180 
SECPPGAIGV TYDTLSVHAP KYCQYLAREL QKLGATFERR TVTSLEQAFD GADLVVNATG 

       190        200        210        220        230        240 
LGAKSIAGID DQAAEPIRGQ TVLVKSPCKR CTMDSSDPAS PAYIIPRPGG EVICGGTYGV 

       250        260        270        280        290        300 
GDWDLSVNPE TVQRILKHCL RLDPTISSDG TIEGIEVLRH NVGLRPARRG GPRVEAERIV 

       310        320        330        340        350        360 
LPLDRTKSPL SLGRGSARAA KEKEVTLVHA YGFSSAGYQQ SWGAAEDVAQ LVDEAFQRYH 


GAARESKL 

« Hide

References

[1]"The primary structure of D-amino acid oxidase from Rhodotorula gracilis."
Faotto L., Pollegioni L., Ceciliani F., Ronchi S., Pilone M.S.
Biotechnol. Lett. 17:193-198(1995)
Cited for: PROTEIN SEQUENCE.
[2]Pilone M.S., Pollegioni L., Molla G., Campaner S., Martegani E.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 26217 / Pan.
[3]"D-amino-acid oxidase gene from Rhodotorula gracilis (Rhodosporidium toruloides) ATCC 26217."
Alonso J., Barredo J.L., Diez B., Salto F., Garcia J.L., Cortes E.
Microbiology 144:1095-1101(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 26217 / Pan.
[4]Liaw G.J., Lee Y.J., Lee Y.H., Chen L.L., Chu W.S.
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 10788 / CBS 14 / IAM 13469 / JCM 10020 / NBRC 0559 / NRRL Y-1091.
[5]"Studies on the structural and functional aspects of Rhodotorula gracilis D-amino acid oxidase by limited trypsinolysis."
Pollegioni L., Ceciliani F., Curti B., Ronchi S., Pilone M.S.
Biochem. J. 310:577-583(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"The X-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation."
Umhau S., Pollegioni L., Molla G., Diederichs K., Welte W., Pilone M.S., Ghisla S.
Proc. Natl. Acad. Sci. U.S.A. 97:12463-12468(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 1-361 IN COMPLEXES WITH FAD; D-ALANINE; 2-AMINOBENZOIC ACID AND LACTATE, ENZYME MECHANISM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C0IX-ray1.90A1-361[»]
1C0KX-ray1.46A1-361[»]
1C0LX-ray1.73A1-361[»]
1C0PX-ray1.20A1-361[»]
2DZGmodel-@1-368[»]
ProteinModelPortalP80324.
SMRP80324. Positions 1-361.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP80324.

Family and domain databases

InterProIPR023209. D-aa_oxidase.
IPR006181. D-amino_acid_oxidase_CS.
IPR006076. FAD-dep_OxRdtase.
[Graphical view]
PANTHERPTHR11530. PTHR11530. 1 hit.
PfamPF01266. DAO. 1 hit.
[Graphical view]
PIRSFPIRSF000189. D-aa_oxidase. 1 hit.
PROSITEPS00677. DAO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP80324.

Entry information

Entry nameOXDA_RHOTO
AccessionPrimary (citable) accession number: P80324
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 16, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references