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UniProtKB/Swiss-Prot entry Q49WB0

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

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Entry information
Entry name CDR_STAS1
Primary accession number Q49WB0
Secondary accession numbers None
Integrated into Swiss-Prot on May 29, 2007
Sequence was last modified on September 13, 2005 (Sequence version 1)
Annotations were last modified on    December 16, 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: SSP1804
From
Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) [TaxID: 342451] [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.0502950102; PubMed=16135568 [NCBI, ExPASy, EBI, Israel, Japan]
Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
"Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection.";
Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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
AP008934; BAE18949.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_301894.1; -.
3D structure databases
SMR Q49WB0; 3-438.
ModBase Q49WB0.
Enzyme and pathway databases
BioCyc SSAP342451:SSP1804-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: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]
Genome annotation databases
GeneID 3616459; -.
GenomeReviews AP008934_GR; SSP1804.
KEGG ssp:SSP1804; -.
NMPDR fig|342451.4.peg.1876; -.
Phylogenomic databases
HOGENOM Q49WB0; -.
Genome annotation databases
CMR Q49WB0; SSP1804.
Other
ProtoNet Q49WB0.
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   440  440     Coenzyme A disulfide reductase. PRO_0000289963
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: 440 AA [This is the length of the unprocessed precursor] Molecular weight: 49473 Da [This is the MW of the unprocessed precursor] CRC64: 86317B7DB21F669D [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MNKIVVVGAV AGGATVASQI RRLDQESEIV VFEKDRDMSF ANCALPYYLG NVVDSRNKVL 

        70         80         90        100        110        120 
EATPESFYEA KNIVVKPCHK VTSINDTENT ITVYDRIQDT YFETHYDTLI LSPGCSANSL 

       130        140        150        160        170        180 
NLDSPIAFTL RNMEDTDAIE TFIKENQVKN ALVVGTGYIG LEILDNLYER GISPTLIHRS 

       190        200        210        220        230        240 
THINKLMDQD MNQAILDEMD KRDIHYRFNE EISKVVGNAV HFESGKVENY DLIIEGVGVK 

       250        260        270        280        290        300 
PNSEFIKNSN VTLDDKGYIP VNDQFQTNIP NIYALGDIIT SHYRHVDLNA HVPLAWGAHR 

       310        320        330        340        350        360 
GASVIAEQLA GDHKIHFKGY LGSNIVKFFD YTFASVGVSP KELSNFDYAM VEANQGEHAG 

       370        380        390        400        410        420 
YYPGNTKLHL RVYFDKTNRR IIRAAAVGMK GVDKRIDVLS MAMMHKLTID ELVEFEVAYA 

       430        440 
PPYSRPKDII NMIGYKARNK
Q49WB0 in FASTA format

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