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UniProtKB/Swiss-Prot entry Q6GIB7

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CDR_STAAR
Primary accession number Q6GIB7
Secondary accession numbers None
Integrated into Swiss-Prot on March 15, 2005
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 31)
Name and origin of the protein
Protein name Coenzyme A disulfide reductase
Synonyms CoA-disulfide reductase
CoADR
EC 1.8.1.14
Gene name
Name: cdr
OrderedLocusNames: SAR0933
From
Staphylococcus aureus (strain MRSA252) [TaxID: 282458] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Staphylococcus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0402521101; PubMed=15213324 [NCBI, ExPASy, EBI, Israel, Japan]
Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance.";
Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
BX571856; CAG39939.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_040355.1; -.
3D structure databases
SMR Q6GIB7; 1-437, 2-438.
ModBase Q6GIB7.
Enzyme and pathway databases
BioCyc SAUR282458:SAR0933-MON; -.
Ontologies
GO
GO:0050451; Molecular function: CoA-disulfide reductase activity (inferred from electronic annotation from HAMAP).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from HAMAP).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006467; Biological process: protein thiol-disulfide exchange (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01608; -; 1.
PBIL [Tree]
InterPro IPR017758; CoA_disulphide_reductase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.30.390.30; Pyr_redox_dim; 1.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00411; PNDRDTASEI.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS Q6GIB7.
ProtoNet Q6GIB7.
Genome annotation databases
GeneID 2861721; -.
GenomeReviews BX571856_GR; SAR0933.
KEGG sar:SAR0933; -.
Phylogenomic databases
HOGENOM Q6GIB7; -.
Genome annotation databases
CMR Q6GIB7; SAR0933.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   438  437     Coenzyme A disulfide reductase. PRO_0000184692
NP_BIND   8    33  26     FAD (By similarity). 
NP_BIND   151   166  16     NADP (By similarity). 
NP_BIND   267   277  11     FAD (By similarity). 
ACT_SITE   43    43        Nucleophile (By similarity). 
ACT_SITE   43    43        Redox-active (By similarity). 
BINDING   15    15        Substrate (By similarity). 
BINDING   19    19        Substrate (By similarity). 
BINDING   22    22        Substrate (By similarity). 
BINDING   39    39        Substrate (By similarity). 
BINDING   42    42        Substrate (By similarity). 
BINDING   71    71        Substrate (By similarity). 
BINDING   299   299        Substrate (By similarity). 
BINDING   419   419        FAD; via carbonyl oxygen (By similarity). 
BINDING   427   427        Substrate (By similarity). 
Sequence information
Length: 438 AA [This is the length of the unprocessed precursor] Molecular weight: 49291 Da [This is the MW of the unprocessed precursor] CRC64: 1079746A4ED26803 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MPKIVVVGAV AGGATCASQI RRLDKESDII IFEKDRDMSF ANCALPYVIG EVVEDRKYAL 

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

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

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

       250        260        270        280        290        300 
PNSKFIESSN IKLDRKGFIP VNDKFETNVP NIYVIGDIAT 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
Q6GIB7 in FASTA format

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