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Reviewed, UniProtKB/Swiss-Prot Q2YWW1 (CDR_STAAB)

Last modified June 16, 2009. Version 35. 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

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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: SAB0839c
OrganismStaphylococcus aureus (strain bovine RF122 / ET3-1) [Complete proteome] [HAMAP]
Taxonomic identifier273036 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

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Protein attributes

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

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Coenzyme A disulfide reductase HAMAP MF_01608
PRO_0000289960

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

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Sequences

Sequence LengthMass (Da)Tools
Q2YWW1-1 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: D553C2CC6EF433A2

FASTA43849,282
        10         20         30         40         50         60 
MPKIVVVGAV AGGATCASQI RRLDKESDII IFEKDRDMSF ANCALPYVIG EVVEDRKYAL 

        70         80         90        100        110        120 
AYTPEKFYDR KQITVKTYHE VIAINDERQT VSVLNRKTNE QFEESYDKLI LSPGASANSL 

       130        140        150        160        170        180 
GFESDITFTL RNLEDTDAIE QFIKANQVDK VLVVGAGYVS LEVLENLYKR GLHPTLIHRS 

       190        200        210        220        230        240 
DKINKLMDAD MNQPILDELD KREIPYRLNE EIVAINGNEI TFKSGRVEHY DMIIEGVGTH 

       250        260        270        280        290        300 
PNSKFIESSN IKLDRKGFIP VNDKLETNVP NIYAIGDIAT SHYRHVDLPA SVPLAWGAHR 

       310        320        330        340        350        360 
AASIVAEQIA GNDTIEFKGF LGNNIVKFFD YTFASVGVKP NELKQFDYKM VEVTQGAHAN 

       370        380        390        400        410        420 
YYPGNSPLHL RVYYDTSNRQ ILRAAAVGKE GVDKRIDVLS MAMMNQLTVD ELTEFEVAYA 

       430 
PPYSHPKDLI NMIGYKAK

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References

[1]"Molecular correlates of host specialization in Staphylococcus aureus."
Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.
PLoS ONE 2:E1120-E1120(2007) [PubMed: 17971880] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

AJ938182 Genomic DNA. Translation: CAI80527.1.
RefSeqYP_416328.1.

3D structure databases

SMRQ2YWW1. Positions 2-438.
ModBaseSearch...

Genome annotation databases

GeneID3793490.
GenomeReviewsGene locus SAB0839c in contig AJ938182_GR.
KEGGsab:SAB0839c.
NMPDRfig|273036.3.peg.938.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2YWW1.
OMAQ2YWW1. IVTEYNF.

Enzyme and pathway databases

BioCycSAUR273036:SAB0839C-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...

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Entry information

Entry nameCDR_STAAB
AccessionPrimary (citable) accession number: Q2YWW1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: December 20, 2005
Last modified: June 16, 2009
This is version 35 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)

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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