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Reviewed, UniProtKB/Swiss-Prot Q8CPT6 (CDR_STAES)

Last modified June 16, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Coenzyme A disulfide reductase
      Short name=CoA-disulfide reductase
      Short name=CoADR
    EC=1.8.1.14
Gene names
Name: cdr
Ordered Locus Names: SE_0669
OrganismStaphylococcus epidermidis (strain ATCC 12228) [Complete proteome] [HAMAP]
Taxonomic identifier176280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide By similarity.

Catalytic activity

2 CoA + NAD(P)+ = CoA-disulfide + NAD(P)H. HAMAP MF_01608

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer By similarity.

Domain

Contains 2 FAD binding domains and a single NADPH binding domain By similarity.

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 By similarity.

Sequence similarities

Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Coenzyme A disulfide reductase HAMAP MF_01608
PRO_0000184695

Regions

Nucleotide binding8 – 3326FAD By similarity
Nucleotide binding151 – 16616NADP By similarity
Nucleotide binding267 – 27711FAD By similarity

Sites

Active site431Nucleophile By similarity
Active site431Redox-active By similarity
Binding site151Substrate By similarity
Binding site191Substrate By similarity
Binding site221Substrate By similarity
Binding site391Substrate By similarity
Binding site421Substrate By similarity
Binding site711Substrate By similarity
Binding site2991Substrate By similarity
Binding site4191FAD; via carbonyl oxygen By similarity
Binding site4271Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8CPT6-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 5B27C5462208D91A

FASTA43849,366
        10         20         30         40         50         60 
MNKIIIVGAV AGGATCASQI RRLDKESEII VFEKDRDMSF ANCALPYYIG NVIEDRRKVL 

        70         80         90        100        110        120 
AYTPNQFYDK KQITVKTYHE VIQINDERQT VTVLNHQTNQ TFEESYDTLI LSPGASANRL 

       130        140        150        160        170        180 
NTHSDISFTV RNLEDTETID TFITNTKAQR ALVVGAGYIS LEVLENLHHR GLDVTWIHRS 

       190        200        210        220        230        240 
TNINKLMDQD MNQPIIDEIE KRNITYRFNE EISHVNGHEV TFTSGKVENF DLIIEGVGTH 

       250        260        270        280        290        300 
PNSQFIKSSN VILNDKGYIP VNHNFQTNIP NIYALGDVIT SHYRHVNLPA QVPLAWGAHR 

       310        320        330        340        350        360 
GASIIAEQLS GNSSIHFKGY LGNNIVKFFD YTLASVGIKP NELKNFDYDM VEVKQGAHAG 

       370        380        390        400        410        420 
YYPGNSPLHL RVYFEKDSRK LIRAAAVGKQ GADKRIDVLS MAMMNNATVD DLTEFEVAYA 

       430 
PPYSHPKDLI NLIGYKAQ 

« Hide

References

[1]"Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228)."
Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.
Mol. Microbiol. 49:1577-1593(2003) [PubMed: 12950922] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE015929 Genomic DNA. Translation: AAO04266.1.
RefSeqNP_764224.1.

3D structure databases

SMRQ8CPT6. Positions 3-438.
ModBaseSearch...

Genome annotation databases

GeneID1057913.
GenomeReviewsGene locus SE_0669 in contig AE015929_GR.
KEGGsep:SE0669.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8CPT6.
OMAQ8CPT6. IVTEYNF.

Enzyme and pathway databases

BioCycSEPI176280:SE_0669-MON.

Family and domain databases

HAMAPMF_01608.
[Tree]
InterProIPR017758. CoA_disulphide_reductase.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR03385. CoA_CoA_reduc. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCDR_STAES
AccessionPrimary (citable) accession number: Q8CPT6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 1, 2003
Last modified: June 16, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents