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Q7A6H1 (CDR_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:SA0831
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide By similarity. HAMAP MF_01608

Catalytic activity

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

Cofactor

Binds 1 FAD per subunit By similarity. HAMAP MF_01608

Subunit structure

Homodimer By similarity. HAMAP MF_01608

Domain

Contains 2 FAD binding domains and a single NADPH binding domain By similarity. HAMAP MF_01608

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. HAMAP MF_01608

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 438437Coenzyme A disulfide reductase HAMAP MF_01608
PRO_0000184691

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
Q7A6H1 [UniParc].

Last modified January 23, 2007. Version 3.
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

References

« Hide 'large scale' references
[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: N315.
[2]"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth."
Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.
J. Microbiol. Methods 60:247-257(2005) [PubMed: 15590099] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
Strain: N315.
[3]"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
Submitted (OCT-2007) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: N315.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000018 Genomic DNA. Translation: BAB42070.1.
PIRC89864.
RefSeqNP_374092.1. NC_002745.2.

3D structure databases

ProteinModelPortalQ7A6H1.
SMRQ7A6H1. Positions 2-438.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7A6H1.

2D gel databases

SWISS-2DPAGEQ7A6H1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000001885; EBSTAP00000001885; EBSTAG00000001885.
GeneID1123646.
GenomeReviewsGene locus SA0831 in contig BA000018_GR.
KEGGsau:SA0831.
PATRIC19573826. VBIStaAur116463_0885.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0446.
GeneTreeEBGT00050000023767.
HOGENOMHBG535576.
OMARNVMDIQ.
ProtClustDBPRK13512.

Enzyme and pathway databases

BioCycSAUR158879:SA0831-MONOMER.

Family and domain databases

HAMAPMF_01608. CoA-diS-reduct.
[Tree]
InterProIPR017758. CoA_disulphide_reductase.
IPR023536. CoA_disulphide_reductase_staph.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
KOK08255.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMsTIGR03385. CoA_CoA_reduc. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCDR_STAAN
AccessionPrimary (citable) accession number: Q7A6H1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 64 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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