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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei15 – 151SubstrateUniRule annotation
Binding sitei19 – 191SubstrateUniRule annotation
Binding sitei22 – 221SubstrateUniRule annotation
Binding sitei39 – 391SubstrateUniRule annotation
Binding sitei42 – 421SubstrateUniRule annotation
Active sitei43 – 431NucleophileUniRule annotation
Active sitei43 – 431Redox-activeUniRule annotation
Binding sitei71 – 711SubstrateUniRule annotation
Binding sitei299 – 2991SubstrateUniRule annotation
Binding sitei419 – 4191FAD; via carbonyl oxygenUniRule annotation
Binding sitei427 – 4271SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 3326FADUniRule annotationAdd
BLAST
Nucleotide bindingi151 – 16616NADPUniRule annotationAdd
BLAST
Nucleotide bindingi267 – 27711FADUniRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciSAUR282458:GJA5-934-MONOMER.

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 438437Coenzyme A disulfide reductasePRO_0000184692Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ6GIB7.
SMRiQ6GIB7. Positions 2-438.
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.
OrthoDBiEOG6QCD6D.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
HAMAPiMF_01608. CoA_diS_reduct.
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.
SMRiQ6GIB7. Positions 2-438.
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.
OrthoDBiEOG6QCD6D.

Enzyme and pathway databases

BioCyciSAUR282458:GJA5-934-MONOMER.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
HAMAPiMF_01608. CoA_diS_reduct.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MRSA252.

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: March 16, 2016
This is version 86 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.