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UniProtKB/Swiss-Prot entry Q5HQI9

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

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Entry information
Entry name CDR_STAEQ
Primary accession number Q5HQI9
Secondary accession numbers None
Integrated into Swiss-Prot on September 27, 2005
Sequence was last modified on February 15, 2005 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 29)
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: SERP0560
From
Staphylococcus epidermidis (strain ATCC 35984 / RP62A) [TaxID: 176279] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Staphylococcus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.187.7.2426-2438.2005; PubMed=15774886 [NCBI, ExPASy, EBI, Israel, Japan]
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.;
"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain.";
J. Bacteriol. 187:2426-2438(2005).
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
CP000029; AAW53947.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_188151.1; -.
3D structure databases
SMR Q5HQI9; 3-438.
ModBase Q5HQI9.
Enzyme and pathway databases
BioCyc SEPI176279:SERP0560-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0050451; Molecular function: CoA-disulfide reductase activity (inferred from electronic annotation from HAMAP).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
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:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
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]
ProtoNet Q5HQI9.
Genome annotation databases
GeneID 3241478; -.
GenomeReviews CP000029_GR; SERP0560.
KEGG ser:SERP0560; -.
TIGR SERP0560; -.
Phylogenomic databases
HOGENOM Q5HQI9; -.
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
CHAIN   1   438  438     Coenzyme A disulfide reductase. PRO_0000184696
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: 49366 Da [This is the MW of the unprocessed precursor] CRC64: 5B27C5462208D91A [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNKIIIVGAV AGGATCASQI RRLDKESEII VFEKDRDMSF ANCALPYYIG NVIEDRRKVL 

        70         80         90        100        110        120 
AYTPNQFYDK KQITVKTYHE VIQINDERQT VTVLNHQTNQ TFEESYDTLI LSPGASANRL 

       130        140        150        160        170        180 
NTHSDISFTV RNLEDTETID TFITNTKAQR ALVVGAGYIS LEVLENLHHR GLDVTWIHRS 

       190        200        210        220        230        240 
TNINKLMDQD MNQPIIDEIE KRNITYRFNE EISHVNGHEV TFTSGKVENF DLIIEGVGTH 

       250        260        270        280        290        300 
PNSQFIKSSN VILNDKGYIP VNHNFQTNIP NIYALGDVIT SHYRHVNLPA QVPLAWGAHR 

       310        320        330        340        350        360 
GASIIAEQLS GNSSIHFKGY LGNNIVKFFD YTLASVGIKP NELKNFDYDM VEVKQGAHAG 

       370        380        390        400        410        420 
YYPGNSPLHL RVYFEKDSRK LIRAAAVGKQ GADKRIDVLS MAMMNNATVD DLTEFEVAYA 

       430 
PPYSHPKDLI NLIGYKAQ
Q5HQI9 in FASTA format

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