ID   CDR_PYRAB               Reviewed;         446 AA.
AC   Q9UYU5;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-JUN-2009, entry version 47.
DE   RecName: Full=Coenzyme A disulfide reductase;
DE            Short=CoA-disulfide reductase;
DE            Short=CoADR;
DE            EC=1.8.1.14;
GN   OrderedLocusNames=PYRAB14120; ORFNames=PAB0936;
OS   Pyrococcus abyssi.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=29292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   MEDLINE=22511545; PubMed=12622808;
RX   DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C.,
RA   Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic
RT   archaeon Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
CC   -!- CATALYTIC ACTIVITY: 2 CoA + NAD(P)(+) = CoA-disulfide + NAD(P)H.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; AJ248287; CAB50317.1; -; Genomic_DNA.
DR   PIR; H75052; H75052.
DR   RefSeq; NP_127087.1; -.
DR   HSSP; P37062; 1NHP.
DR   GeneID; 1496802; -.
DR   GenomeReviews; AL096836_GR; PYRAB14120.
DR   KEGG; pab:PAB0936; -.
DR   NMPDR; fig|272844.1.peg.1495; -.
DR   HOGENOM; Q9UYU5; -.
DR   OMA; Q9UYU5; DVAETKH.
DR   BioCyc; PABY272844:PAB0936-MON; -.
DR   BRENDA; 1.8.1.14; 262861.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0050451; F:CoA-disulfide reductase activity; IEA:EC.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006467; P:protein thiol-disulfide exchange; IEA:InterPro.
DR   InterPro; IPR017758; CoA_disulphide_reductase.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR03385; CoA_CoA_reduc; 1.
PE   3: Inferred from homology;
KW   Complete proteome; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN         1    446       Coenzyme A disulfide reductase.
FT                                /FTId=PRO_0000184697.
FT   NP_BIND      14     39       FAD (By similarity).
FT   NP_BIND     155    170       NADP (By similarity).
FT   NP_BIND     274    284       FAD (By similarity).
FT   ACT_SITE     49     49       Nucleophile (By similarity).
FT   ACT_SITE     49     49       Redox-active (By similarity).
FT   BINDING      21     21       Substrate.
FT   BINDING      25     25       Substrate.
FT   BINDING      28     28       Substrate (By similarity).
FT   BINDING      45     45       Substrate (By similarity).
FT   BINDING      76     76       Substrate.
FT   BINDING     426    426       FAD; via carbonyl oxygen (By similarity).
SQ   SEQUENCE   446 AA;  49181 MW;  0B7048662F50BD72 CRC64;
     MRVVKVKKTV VIIGGGAAGM SAASRVKRLK PEWDVKVFEA TEWVSHAPCG IPYVVEGISP
     TEKLMHYPPE VFIKKRGIDL HLNAEVIEVD TGYVRVREKD GEKSYEWDYL VFANGASPQV
     PAIEGVDLKG VFTADLPPDA VAIREYMEKN RVEDVVIVGG GYIGLEMAEA FVAQGKRVTM
     IVRGERILRR SFDKEVTDII EEKLKQHVNL RLQEIVLRIE GKDRVEKVVT DAGEYRADLV
     ILATGIKPNI ELARQLGVRI GETGAIWTNE KMQTSVENVY AAGDVAETKH VITGRRVWVP
     LAPPGNKMGY VAGSNIAGKE IHFPGVLGTT VTKFLDVEIG KTGLTETEAL KEGYDIRTAF
     IKASTRPHYY PGGKEIWLKG VVDNETNRLL GVQAVGAEIL PRIDAAAAML MANFTTKDAF
     FTDLAYAPPF APVWDPLVVL ARVLKF
//