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Reviewed, UniProtKB/Swiss-Prot Q4L4Y7 (CDR_STAHJ)

Last modified June 16, 2009. Version 37. 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: SH1979
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

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Protein attributes

Sequence length440 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 – 440440Coenzyme A disulfide reductase HAMAP MF_01608
PRO_0000289962

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
Q4L4Y7-1 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: B709D2AB14B9EC0C

FASTA44049,334
        10         20         30         40         50         60 
MRKIIVVGAV AGGATCASQI RRLDKDSEIT IFEKDRDMSF ANCGLPYFIG NIVNERKDVL 

        70         80         90        100        110        120 
PITPDVFKEK KDITVKTYHE VIAINDKDQT VTVVNRQTNE KFEASYDKLI LSPGAGANSL 

       130        140        150        160        170        180 
GFDSDYIFTL RNMEDTDAID QFIDQHQAKK ALVVGAGYIS LEVLENLYAR GLDVTLIHRS 

       190        200        210        220        230        240 
EKVNKLMDQD MNQVIFDELD SRHIPYRLNE EIVSVKDHLV TFKSGIQEDF DIIIEGVGTH 

       250        260        270        280        290        300 
PHSKFIESSN VALDDKGFVK VNDKFETNIP NIYALGDVIT STYRHVNLPA QVPLAWGAHR 

       310        320        330        340        350        360 
GASVIAEQLA GNKNIIFKGF LGTNIVKFFD YTLASVGIKV EELTHFDYQM VELNSGTHAG 

       370        380        390        400        410        420 
YYPGNTNVHL RVYFDTNNRH LLRAAAVGKT GVDKRIDVLS MAMMSELTID ELTEFEVAYA 

       430        440 
PPYSHPKDLV NMIGYKARDL

« Hide

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References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed: 16237012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

AP006716 Genomic DNA. Translation: BAE05288.1.
RefSeqYP_253894.1.

3D structure databases

SMRQ4L4Y7. Positions 3-438.
ModBaseSearch...

Genome annotation databases

GeneID3482335.
GenomeReviewsGene locus SH1979 in contig AP006716_GR.
KEGGsha:SH1979.
NMPDRfig|279808.3.peg.2268.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ4L4Y7.
OMAQ4L4Y7. LNENASI.

Enzyme and pathway databases

BioCycSHAE279808:SH1979-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_STAHJ
AccessionPrimary (citable) accession number: Q4L4Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: August 2, 2005
Last modified: June 16, 2009
This is version 37 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