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Protein

Coenzyme A disulfide reductase

Gene

cdr

Organism
Staphylococcus aureus (strain MRSA252)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide.UniRule annotation

Catalytic activityi

2 CoA + NADP+ = CoA-disulfide + NADPH.UniRule annotation

Cofactori

FADUniRule annotationNote: Binds 1 FAD per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei15SubstrateUniRule annotation1
Binding sitei19SubstrateUniRule annotation1
Binding sitei22SubstrateUniRule annotation1
Binding sitei39SubstrateUniRule annotation1
Binding sitei42SubstrateUniRule annotation1
Active sitei43NucleophileUniRule annotation1
Active sitei43Redox-activeUniRule annotation1
Binding sitei71SubstrateUniRule annotation1
Binding sitei299SubstrateUniRule annotation1
Binding sitei419FAD; via carbonyl oxygenUniRule annotation1
Binding sitei427SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi8 – 33FADUniRule annotationAdd BLAST26
Nucleotide bindingi151 – 166NADPUniRule annotationAdd BLAST16
Nucleotide bindingi267 – 277FADUniRule annotationAdd BLAST11

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Coenzyme A disulfide reductaseUniRule annotation (EC:1.8.1.14UniRule annotation)
Short name:
CoA-disulfide reductaseUniRule annotation
Short name:
CoADRUniRule annotation
Gene namesi
Name:cdrUniRule annotation
Ordered Locus Names:SAR0933
OrganismiStaphylococcus aureus (strain MRSA252)
Taxonomic identifieri282458 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001846922 – 438Coenzyme A disulfide reductaseAdd BLAST437

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ6GIB7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Contains 2 FAD binding domains and a single NADPH binding domain.UniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center

Phylogenomic databases

HOGENOMiHOG000276710.
KOiK08255.
OMAiGIPYWVG.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
HAMAPiMF_01608. CoA_diS_reduct. 1 hit.
InterProiIPR017758. CoA_disulphide_reductase.
IPR023536. CoA_disulphide_reductase_staph.
IPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR03385. CoA_CoA_reduc. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6GIB7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKIVVVGAV AGGATCASQI RRLDKESDII IFEKDRDMSF ANCALPYVIG
60 70 80 90 100
EVVEDRKYAL AYTPEKFYDR KQITVKTYHE VIAINDERQT VSVLNRKTNE
110 120 130 140 150
QFEESYDKLI LSPGASANSL GFESDITFTL RNLEDTDAID QFIKANQVDK
160 170 180 190 200
VLVVGAGYVS LEVLENLYER GLHPTLIHRS DKINKLMDAD MNQPILDELD
210 220 230 240 250
KREIPYRLNE EIDAINGNEI TFKSGKVEHY DMIIEGVGTH PNSKFIESSN
260 270 280 290 300
IKLDRKGFIP VNDKFETNVP NIYVIGDIAT SHYRHVDLPA SVPLAWGAHR
310 320 330 340 350
AASIVAEQIA GNDTIEFKGF LGNNIVKFFD YTFASVGVKP NELKQFDYKM
360 370 380 390 400
VEVTQGAHAN YYPGNSPLHL RVYYDTSNRQ ILRAAAVGKE GADKRIDVLS
410 420 430
MAMMNQLTVD ELTEFEVAYA PPYSHPKDLI NMIGYKAK
Length:438
Mass (Da):49,291
Last modified:January 23, 2007 - v3
Checksum:i1079746A4ED26803
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG39939.1.
RefSeqiWP_001124494.1. NC_002952.2.

Genome annotation databases

EnsemblBacteriaiCAG39939; CAG39939; SAR0933.
KEGGisar:SAR0933.
PATRICi19545399. VBIStaAur71814_0932.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571856 Genomic DNA. Translation: CAG39939.1.
RefSeqiWP_001124494.1. NC_002952.2.

3D structure databases

ProteinModelPortaliQ6GIB7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG39939; CAG39939; SAR0933.
KEGGisar:SAR0933.
PATRICi19545399. VBIStaAur71814_0932.

Phylogenomic databases

HOGENOMiHOG000276710.
KOiK08255.
OMAiGIPYWVG.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
HAMAPiMF_01608. CoA_diS_reduct. 1 hit.
InterProiIPR017758. CoA_disulphide_reductase.
IPR023536. CoA_disulphide_reductase_staph.
IPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR03385. CoA_CoA_reduc. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCDR_STAAR
AccessioniPrimary (citable) accession number: Q6GIB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.UniRule annotation

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.