ID   CDR_PYRHO               Reviewed;         445 AA.
AC   O58308;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Coenzyme A disulfide reductase;
DE            Short=CoA-disulfide reductase;
DE            Short=CoADR;
DE            EC=1.8.1.14;
GN   OrderedLocusNames=PH0572;
OS   Pyrococcus horikoshii.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=53953;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT3;
RX   MEDLINE=98344137; PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y.,
RA   Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y.,
RA   Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K.,
RA   Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=15720393; DOI=10.1111/j.1742-4658.2005.04555.x;
RA   Harris D.R., Ward D.E., Feasel J.M., Lancaster K.M., Murphy R.D.,
RA   Mallet T.C., Crane E.J. III;
RT   "Discovery and characterization of a coenzyme A disulfide reductase
RT   from Pyrococcus horikoshii. Implications for this disulfide metabolism
RT   of anaerobic hyperthermophiles.";
RL   FEBS J. 272:1189-1200(2005).
CC   -!- FUNCTION: Acts as a coenzyme A disulfide reductase. Specific for
CC       CoA disulfide. Shows a slow NAD(P)H oxidase activity in the
CC       presence of high concentrations of substrate-level FAD. This
CC       demonstrates that it is not likely to act as an NADH oxidase in
CC       vivo.
CC   -!- CATALYTIC ACTIVITY: 2 CoA + NAD(P)(+) = CoA-disulfide + NAD(P)H.
CC   -!- COFACTOR: Binds 1 FAD per subunit.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=73 uM for NADH;
CC         Note=KM value for NADH is lower than 9uM;
CC       Temperature dependence:
CC         Optimum temperature is 85 degrees Celsius. Thermostable;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BA000001; BAA29661.1; -; Genomic_DNA.
DR   PIR; H71171; H71171.
DR   RefSeq; NP_142538.1; -.
DR   HSSP; P37062; 1NHP.
DR   GeneID; 1442906; -.
DR   GenomeReviews; BA000001_GR; PH0572.
DR   KEGG; pho:PH0572; -.
DR   NMPDR; fig|70601.1.peg.559; -.
DR   HOGENOM; O58308; -.
DR   OMA; O58308; KSHEDLM.
DR   BRENDA; 1.8.1.14; 74679.
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; 2.
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   1: Evidence at protein level;
KW   Complete proteome; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN         1    445       Coenzyme A disulfide reductase.
FT                                /FTId=PRO_0000184699.
FT   NP_BIND      13     38       FAD (By similarity).
FT   NP_BIND     154    169       NADP (By similarity).
FT   NP_BIND     273    283       FAD (By similarity).
FT   ACT_SITE     48     48       Nucleophile (By similarity).
FT   ACT_SITE     48     48       Redox-active (By similarity).
FT   BINDING      20     20       Substrate (By similarity).
FT   BINDING      24     24       Substrate (By similarity).
FT   BINDING      27     27       Substrate (By similarity).
FT   BINDING      44     44       Substrate (By similarity).
FT   BINDING      75     75       Substrate (By similarity).
FT   BINDING     425    425       FAD; via carbonyl oxygen (By similarity).
SQ   SEQUENCE   445 AA;  48977 MW;  896A034000A0B233 CRC64;
     MGENMKKKVV IIGGGAAGMS AASRVKRLKP EWDVKVFEAT EWVSHAPCGI PYVVEGLSTP
     DKLMYYPPEV FIKKRGIDLH LNAEVIEVDT GYVRVRENGG EKSYEWDYLV FANGASPQVP
     AIEGVNLKGV FTADLPPDAL AIREYMEKYK VENVVIIGGG YIGIEMAEAF AAQGKNVTMI
     VRGERVLRRS FDKEVTDILE EKLKKHVNLR LQEITMKIEG EERVEKVVTD AGEYKAELVI
     LATGIKPNIE LAKQLGVRIG ETGAIWTNEK MQTSVENVYA AGDVAETRHV ITGRRVWVPL
     APAGNKMGYV AGSNIAGKEL HFPGVLGTAV TKFMDVEIGK TGLTEMEALK EGYDVRTAFI
     KASTRPHYYP GGREIWLKGV VDNETNRLLG VQVVGSDILP RIDTAAAMLM AGFTTKDAFF
     TDLAYAPPFA PVWDPLIVLA RVLKF
//