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UniProtKB/Swiss-Prot entry O58308

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

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Entry information
Entry name CDR_PYRHO
Primary accession number O58308
Secondary accession numbers None
Integrated into Swiss-Prot on September 27, 2005
Sequence was last modified on August 1, 1998 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 52)
Name and origin of the protein
Protein name Coenzyme A disulfide reductase
Synonyms CoA-disulfide reductase
CoADR
EC 1.8.1.14
Gene name
OrderedLocusNames: PH0572
From
Pyrococcus horikoshii [TaxID: 53953] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; Pyrococcus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OT3;
DOI=10.1093/dnares/5.2.55; PubMed=9679194 [NCBI, ExPASy, EBI, Israel, Japan]
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
DNA Res. 5:55-76(1998).
[2]
 CHARACTERIZATION.
DOI=10.1111/j.1742-4658.2005.04555.x; PubMed=15720393 [NCBI, ExPASy, EBI, Israel, Japan]
Harris D.R., Ward D.E., Feasel J.M., Lancaster K.M., Murphy R.D., Mallet T.C., Crane E.J. III;
"Discovery and characterization of a coenzyme A disulfide reductase from Pyrococcus horikoshii. Implications for this disulfide metabolism of anaerobic hyperthermophiles.";
FEBS J. 272:1189-1200(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
BA000001; BAA29661.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H71171; H71171.
RefSeq NP_142538.1; -.
3D structure databases
HSSP P37062; 1NHP. [HSSP ENTRY / PDB]
ModBase O58308.
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 EC).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
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).
QuickGo view.
Family and domain databases
InterPro IPR000759; Adrndx_reductase.
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; 2.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.
PRINTS PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00411; PNDRDTASEI.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
Genome annotation databases
GeneID 1442906; -.
GenomeReviews BA000001_GR; PH0572.
KEGG pho:PH0572; -.
NMPDR fig|70601.1.peg.559; -.
Phylogenomic databases
HOGENOM O58308; -.
Genome annotation databases
CMR O58308; PH0572.
Other
ProtoNet O58308.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Flavoprotein; NAD; Oxidoreductase; Redox-active center.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   445  445     Coenzyme A disulfide reductase. PRO_0000184699
NP_BIND   13    38  26     FAD (By similarity). 
NP_BIND   154   169  16     NADP (By similarity). 
NP_BIND   273   283  11     FAD (By similarity). 
ACT_SITE   48    48        Nucleophile (By similarity). 
ACT_SITE   48    48        Redox-active (By similarity). 
BINDING   20    20        Substrate (By similarity). 
BINDING   24    24        Substrate (By similarity). 
BINDING   27    27        Substrate (By similarity). 
BINDING   44    44        Substrate (By similarity). 
BINDING   75    75        Substrate (By similarity). 
BINDING   425   425        FAD; via carbonyl oxygen (By similarity). 
Sequence information
Length: 445 AA [This is the length of the unprocessed precursor] Molecular weight: 48977 Da [This is the MW of the unprocessed precursor] CRC64: 896A034000A0B233 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MGENMKKKVV IIGGGAAGMS AASRVKRLKP EWDVKVFEAT EWVSHAPCGI PYVVEGLSTP 

        70         80         90        100        110        120 
DKLMYYPPEV FIKKRGIDLH LNAEVIEVDT GYVRVRENGG EKSYEWDYLV FANGASPQVP 

       130        140        150        160        170        180 
AIEGVNLKGV FTADLPPDAL AIREYMEKYK VENVVIIGGG YIGIEMAEAF AAQGKNVTMI 

       190        200        210        220        230        240 
VRGERVLRRS FDKEVTDILE EKLKKHVNLR LQEITMKIEG EERVEKVVTD AGEYKAELVI 

       250        260        270        280        290        300 
LATGIKPNIE LAKQLGVRIG ETGAIWTNEK MQTSVENVYA AGDVAETRHV ITGRRVWVPL 

       310        320        330        340        350        360 
APAGNKMGYV AGSNIAGKEL HFPGVLGTAV TKFMDVEIGK TGLTEMEALK EGYDVRTAFI 

       370        380        390        400        410        420 
KASTRPHYYP GGREIWLKGV VDNETNRLLG VQVVGSDILP RIDTAAAMLM AGFTTKDAFF 

       430        440 
TDLAYAPPFA PVWDPLIVLA RVLKF
O58308 in FASTA format

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