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P80324

- OXDA_RHOTO

UniProt

P80324 - OXDA_RHOTO

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
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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

    FAD.

    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

    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-SubCell

    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 – 105
    Helixi14 – 2512
    Beta strandi29 – 368
    Helixi48 – 503
    Turni61 – 633
    Helixi65 – 8117
    Turni82 – 854
    Beta strandi86 – 9914
    Helixi100 – 1067
    Turni107 – 1115
    Beta strandi116 – 1183
    Helixi120 – 1223
    Beta strandi128 – 1369
    Helixi139 – 15214
    Beta strandi156 – 1594
    Helixi165 – 1673
    Beta strandi173 – 1775
    Helixi180 – 1845
    Beta strandi194 – 20512
    Beta strandi212 – 2143
    Beta strandi222 – 2276
    Turni228 – 2303
    Beta strandi231 – 2355
    Helixi249 – 26214
    Helixi264 – 2663
    Beta strandi267 – 2715
    Helixi272 – 2743
    Beta strandi276 – 28813
    Beta strandi293 – 30210
    Turni305 – 3073
    Beta strandi323 – 3319
    Helixi334 – 3363
    Helixi337 – 35923

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MHSQKRVVVL GSGVIGLSSA LILARKGYSV HILARDLPED VSSQTFASPW    50
    AGANWTPFMT LTDGPRQAKW EESTFKKWVE LVPTGHAMWL KGTRRFAQNE 100
    DGLLGHWYKD ITPNYRPLPS SECPPGAIGV TYDTLSVHAP KYCQYLAREL 150
    QKLGATFERR TVTSLEQAFD GADLVVNATG LGAKSIAGID DQAAEPIRGQ 200
    TVLVKSPCKR CTMDSSDPAS PAYIIPRPGG EVICGGTYGV GDWDLSVNPE 250
    TVQRILKHCL RLDPTISSDG TIEGIEVLRH NVGLRPARRG GPRVEAERIV 300
    LPLDRTKSPL SLGRGSARAA KEKEVTLVHA YGFSSAGYQQ SWGAAEDVAQ 350
    LVDEAFQRYH GAARESKL 368
    Length:368
    Mass (Da):40,076
    Last modified:November 1, 1995 - v1
    Checksum:i99940118BCFA886E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 78 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