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P80324

- OXDA_RHOTO

UniProt

P80324 - OXDA_RHOTO

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Protein

D-amino-acid oxidase

Gene

DAO1

Organism
Rhodosporidium toruloides (Yeast) (Rhodotorula gracilis)
Status
Reviewed - Annotation score: 3 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei162 – 1621FAD; via amide nitrogen and carbonyl oxygen
Binding sitei179 – 1791FAD
Binding sitei223 – 2231Substrate
Binding sitei285 – 2851Substrate
Binding sitei335 – 3351Substrate; via carbonyl oxygen
Binding sitei339 – 3391FAD; via amide nitrogen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 2115FADAdd
BLAST
Nucleotide bindingi35 – 362FAD
Nucleotide bindingi47 – 482FAD
Nucleotide bindingi52 – 543FAD
Nucleotide bindingi334 – 3385FAD

GO - Molecular functioni

  1. D-amino-acid oxidase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

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 lineageiEukaryotaFungiDikaryaBasidiomycotaPucciniomycotinaMicrobotryomycetesSporidiobolalesRhodosporidium

Subcellular locationi

Peroxisome Curated

GO - Cellular componenti

  1. peroxisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 368368D-amino-acid oxidasePRO_0000162767Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
368
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Helixi14 – 2512Combined sources
Beta strandi29 – 368Combined sources
Helixi48 – 503Combined sources
Turni61 – 633Combined sources
Helixi65 – 8117Combined sources
Turni82 – 854Combined sources
Beta strandi86 – 9914Combined sources
Helixi100 – 1067Combined sources
Turni107 – 1115Combined sources
Beta strandi116 – 1183Combined sources
Helixi120 – 1223Combined sources
Beta strandi128 – 1369Combined sources
Helixi139 – 15214Combined sources
Beta strandi156 – 1594Combined sources
Helixi165 – 1673Combined sources
Beta strandi173 – 1775Combined sources
Helixi180 – 1845Combined sources
Beta strandi194 – 20512Combined sources
Beta strandi212 – 2143Combined sources
Beta strandi222 – 2276Combined sources
Turni228 – 2303Combined sources
Beta strandi231 – 2355Combined sources
Helixi249 – 26214Combined sources
Helixi264 – 2663Combined sources
Beta strandi267 – 2715Combined sources
Helixi272 – 2743Combined sources
Beta strandi276 – 28813Combined sources
Beta strandi293 – 30210Combined sources
Turni305 – 3073Combined sources
Beta strandi323 – 3319Combined sources
Helixi334 – 3363Combined sources
Helixi337 – 35923Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP80324.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi366 – 3683Microbody targeting signalSequence Analysis

Sequence similaritiesi

Belongs to the DAMOX/DASOX family.Curated

Family and domain databases

InterProiIPR023209. D-aa_oxidase.
IPR006181. D-amino_acid_oxidase_CS.
IPR006076. FAD-dep_OxRdtase.
[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.

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
Entry Method Resolution (Å) Chain Positions PDBsum
1C0I X-ray 1.90 A 1-361 [» ]
1C0K X-ray 1.46 A 1-361 [» ]
1C0L X-ray 1.73 A 1-361 [» ]
1C0P X-ray 1.20 A 1-361 [» ]
2DZG model - @ 1-368 [» ]
ProteinModelPortali P80324.
SMRi P80324. Positions 1-361.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P80324.

Miscellaneous databases

EvolutionaryTracei P80324.

Family and domain databases

InterProi IPR023209. D-aa_oxidase.
IPR006181. D-amino_acid_oxidase_CS.
IPR006076. FAD-dep_OxRdtase.
[Graphical view ]
PANTHERi PTHR11530. PTHR11530. 1 hit.
Pfami PF01266. DAO. 1 hit.
[Graphical view ]
PIRSFi PIRSF000189. D-aa_oxidase. 1 hit.
PROSITEi PS00677. DAO. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

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 26, 2014
This is version 80 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

External Data

Dasty 3