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Protein

Coenzyme A disulfide reductase

Gene

cdr

Organism
Staphylococcus aureus (strain NCTC 8325)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide. Is also active with other disulfide substrates containing at least one 4'-phosphopantethienyl moiety such as 4,4'-diphosphopantethine, but is not able to reduce oxidized glutathione, cystine, pantethine, or H2O2.

Catalytic activityi

2 CoA + NADP+ = CoA-disulfide + NADPH.

Cofactori

FADNote: Binds 1 FAD per subunit.

Kineticsi

  1. KM=2 µM for NADPH
  2. KM=11 µM for CoA disulfide
  3. KM=140 µM for 3'-dephospho-CoA disulfide
  4. KM=80 µM for 4,4'-diphosphopantethine
  5. KM=1100 µM for CoA glutathione mixed disulfide

    pH dependencei

    Optimum pH is 7.0-8.0.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei15 – 151Substrate1 Publication
    Binding sitei19 – 191Substrate1 Publication
    Binding sitei22 – 221Substrate1 Publication
    Binding sitei39 – 391Substrate1 Publication
    Binding sitei42 – 421Substrate1 Publication
    Active sitei43 – 431Nucleophile1 Publication
    Active sitei43 – 431Redox-active1 Publication
    Binding sitei71 – 711Substrate1 Publication
    Binding sitei299 – 2991Substrate1 Publication
    Binding sitei419 – 4191FAD; via carbonyl oxygen1 Publication
    Binding sitei427 – 4271Substrate1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi8 – 3326FAD1 PublicationAdd
    BLAST
    Nucleotide bindingi151 – 16616NADPBy similarityAdd
    BLAST
    Nucleotide bindingi267 – 27711FAD1 PublicationAdd
    BLAST

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyciSAUR93061:GIWJ-872-MONOMER.
    BRENDAi1.8.1.14. 3352.
    SABIO-RKO52582.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Coenzyme A disulfide reductase (EC:1.8.1.14)
    Short name:
    CoA-disulfide reductase
    Short name:
    CoADR
    Gene namesi
    Name:cdr
    Ordered Locus Names:SAOUHSC_00908
    OrganismiStaphylococcus aureus (strain NCTC 8325)
    Taxonomic identifieri93061 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
    Proteomesi
    • UP000008816 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi43 – 431C → S: Loss of activity. 1 Publication
    Mutagenesisi361 – 3611Y → F: Reduces activity by 92%. Loss of activity; when associated with F-419. 1 Publication
    Mutagenesisi419 – 4191Y → F: Reduces activity by 80%. Loss of activity; when associated with F-361. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 438437Coenzyme A disulfide reductasePRO_0000184688Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi93061.SAOUHSC_00908.

    Structurei

    Secondary structure

    1
    438
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 74Combined sources
    Helixi13 – 2311Combined sources
    Beta strandi25 – 273Combined sources
    Beta strandi29 – 368Combined sources
    Beta strandi38 – 403Combined sources
    Helixi42 – 443Combined sources
    Helixi45 – 495Combined sources
    Helixi56 – 594Combined sources
    Helixi64 – 718Combined sources
    Beta strandi74 – 774Combined sources
    Beta strandi79 – 857Combined sources
    Turni86 – 894Combined sources
    Beta strandi90 – 956Combined sources
    Turni96 – 994Combined sources
    Beta strandi100 – 1056Combined sources
    Beta strandi107 – 1115Combined sources
    Beta strandi115 – 1173Combined sources
    Helixi133 – 14614Combined sources
    Beta strandi150 – 1545Combined sources
    Helixi158 – 17013Combined sources
    Beta strandi173 – 1819Combined sources
    Helixi189 – 1924Combined sources
    Helixi193 – 2019Combined sources
    Beta strandi206 – 2094Combined sources
    Beta strandi212 – 2165Combined sources
    Beta strandi219 – 2224Combined sources
    Beta strandi227 – 2293Combined sources
    Beta strandi231 – 2355Combined sources
    Beta strandi239 – 2424Combined sources
    Helixi244 – 2463Combined sources
    Beta strandi272 – 2743Combined sources
    Helixi276 – 2783Combined sources
    Beta strandi279 – 29012Combined sources
    Helixi295 – 31016Combined sources
    Beta strandi324 – 3285Combined sources
    Beta strandi331 – 3388Combined sources
    Helixi340 – 3456Combined sources
    Beta strandi348 – 35811Combined sources
    Beta strandi362 – 3643Combined sources
    Beta strandi367 – 3759Combined sources
    Turni376 – 3783Combined sources
    Beta strandi380 – 39112Combined sources
    Helixi392 – 40413Combined sources
    Helixi410 – 4145Combined sources
    Turni421 – 4233Combined sources
    Helixi429 – 4357Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YQZX-ray1.54A/B1-438[»]
    ProteinModelPortaliO52582.
    SMRiO52582. Positions 2-438.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO52582.

    Family & Domainsi

    Domaini

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiENOG4107QMW. Bacteria.
    COG0446. LUCA.
    HOGENOMiHOG000276710.
    KOiK08255.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    3.50.50.60. 2 hits.
    HAMAPiMF_01608. CoA_diS_reduct. 1 hit.
    InterProiIPR017758. CoA_disulphide_reductase.
    IPR023536. CoA_disulphide_reductase_staph.
    IPR023753. FAD/NAD-binding_dom.
    IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    [Graphical view]
    PfamiPF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 1 hit.
    SSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR03385. CoA_CoA_reduc. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O52582-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPKIVVVGAV AGGATCASQI RRLDKESDII IFEKDRDMSF ANCALPYVIG
    60 70 80 90 100
    EVVEDRRYAL AYTPEKFYDR KQITVKTYHE VIAINDERQT VSVLNRKTNE
    110 120 130 140 150
    QFEESYDKLI LSPGASANSL GFESDITFTL RNLEDTDAID QFIKANQVDK
    160 170 180 190 200
    VLVVGAGYVS LEVLENLNER GLHPTLIHRS DKINKLMDAD MNQPILDELD
    210 220 230 240 250
    KREIPYRLNE EINAINGNEI TFKSGKVEHY DMIIEGVGTH PNSKFIESSN
    260 270 280 290 300
    IKLDRKGFIP VNDKFETNVP NIYAIGDIAT SHYRHVDLPA SVPLAWGAHR
    310 320 330 340 350
    AASIVAEQIA GNDTIEFKGF LGNNIVKFFD YTFASVGVKP NELKQFDYKM
    360 370 380 390 400
    VEVTQGAHAN YYPGNSPLHL RVYYDTSNRQ ILRAAAVGKE GADKRIDVLS
    410 420 430
    MAMMNQLTVD ELTEFEVAYA PPYSHPKDLI NMIGYKAK
    Length:438
    Mass (Da):49,241
    Last modified:January 23, 2007 - v3
    Checksum:i3A9B643BD8D44402
    GO

    Mass spectrometryi

    Molecular mass is 49153 Da from positions 2 - 438. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF041467 Genomic DNA. Translation: AAB97073.1.
    CP000253 Genomic DNA. Translation: ABD30033.1.
    RefSeqiYP_499461.1. NC_007795.1.

    Genome annotation databases

    EnsemblBacteriaiABD30033; ABD30033; SAOUHSC_00908.
    GeneIDi3920795.
    KEGGisao:SAOUHSC_00908.
    PATRICi19579336. VBIStaAur99865_0829.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF041467 Genomic DNA. Translation: AAB97073.1.
    CP000253 Genomic DNA. Translation: ABD30033.1.
    RefSeqiYP_499461.1. NC_007795.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YQZX-ray1.54A/B1-438[»]
    ProteinModelPortaliO52582.
    SMRiO52582. Positions 2-438.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi93061.SAOUHSC_00908.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABD30033; ABD30033; SAOUHSC_00908.
    GeneIDi3920795.
    KEGGisao:SAOUHSC_00908.
    PATRICi19579336. VBIStaAur99865_0829.

    Phylogenomic databases

    eggNOGiENOG4107QMW. Bacteria.
    COG0446. LUCA.
    HOGENOMiHOG000276710.
    KOiK08255.

    Enzyme and pathway databases

    BioCyciSAUR93061:GIWJ-872-MONOMER.
    BRENDAi1.8.1.14. 3352.
    SABIO-RKO52582.

    Miscellaneous databases

    EvolutionaryTraceiO52582.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    3.50.50.60. 2 hits.
    HAMAPiMF_01608. CoA_diS_reduct. 1 hit.
    InterProiIPR017758. CoA_disulphide_reductase.
    IPR023536. CoA_disulphide_reductase_staph.
    IPR023753. FAD/NAD-binding_dom.
    IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    [Graphical view]
    PfamiPF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 1 hit.
    SSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR03385. CoA_CoA_reduc. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCDR_STAA8
    AccessioniPrimary (citable) accession number: O52582
    Secondary accession number(s): Q2FZT2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: January 23, 2007
    Last modified: September 7, 2016
    This is version 105 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Reduction of disulfides occurs by a thiol-disulfide exchange reaction, but involves only a single catalytic cysteine residue that forms a stable mixed disulfide with CoA during catalysis.

    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.