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Reviewed, UniProtKB/Swiss-Prot A7X0I7 (CDR_STAA1)

Last modified June 16, 2009. Version 17. 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: SAHV_0965
OrganismStaphylococcus aureus (strain Mu3 / ATCC 700698) [Complete proteome] [HAMAP]
Taxonomic identifier418127 [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_1000069425

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
A7X0I7-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 3970317541CFF013

FASTA43849,291
        10         20         30         40         50         60 
MPKIVVVGAV AGGATCASQI RRLDKESDII IFEKDRDMSF ANCALPYVIG EVVEDRKYAL 

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

       130        140        150        160        170        180 
GFESDITFTL RNLEDTDAID QFIKANQVDK VLVIGAGYVS LEVLENLYER GLHPTLIHRS 

       190        200        210        220        230        240 
DKINKLMDAD MNQPILDELD KREIPYRLNE EIDAINGNEI TFKSGKVEHY DMIIEGVGTH 

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

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

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

       430 
PPYSHPKDLI NMIGYKAK

« Hide

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References

[1]"Mutated response regulator graR is responsible for phenotypic conversion of Staphylococcus aureus from heterogeneous vancomycin-intermediate resistance to vancomycin-intermediate resistance."
Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.
Antimicrob. Agents Chemother. 52:45-53(2008) [PubMed: 17954695] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

AP009324 Genomic DNA. Translation: BAF77848.1.
RefSeqYP_001441555.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5561676.
GenomeReviewsGene locus SAHV_0965 in contig AP009324_GR.
KEGGsaw:SAHV_0965.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA7X0I7. IVTEYNF.

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_STAA1
AccessionPrimary (citable) accession number: A7X0I7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: June 16, 2009
This is version 17 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