CDR_STAA8
ID CDR_STAA8 Reviewed; 438 AA.
AC O52582; Q2FZT2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Coenzyme A disulfide reductase;
DE Short=CoA-disulfide reductase;
DE Short=CoADR;
DE EC=1.8.1.14;
GN Name=cdr; OrderedLocusNames=SAOUHSC_00908;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15 AND
RP 193-208.
RX PubMed=9488708; DOI=10.1074/jbc.273.10.5752;
RA delCardayre S.B., Davies J.E.;
RT "Staphylococcus aureus coenzyme A disulfide reductase, a new subfamily of
RT pyridine nucleotide-disulfide oxidoreductase. Sequence, expression, and
RT analysis of cdr.";
RL J. Biol. Chem. 273:5752-5757(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9488707; DOI=10.1074/jbc.273.10.5744;
RA delCardayre S.B., Stock K.P., Newton G.L., Fahey R.C., Davies J.E.;
RT "Coenzyme A disulfide reductase, the primary low molecular weight disulfide
RT reductase from Staphylococcus aureus. Purification and characterization of
RT the native enzyme.";
RL J. Biol. Chem. 273:5744-5751(1998).
RN [4]
RP CHARACTERIZATION, ACTIVE SITE, MUTAGENESIS OF CYS-43, AND MASS
RP SPECTROMETRY.
RX PubMed=10052943; DOI=10.1021/bi9825899;
RA Luba J., Charrier V., Claiborne A.;
RT "Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for
RT asymmetric behavior on interaction with pyridine nucleotides.";
RL Biochemistry 38:2725-2737(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH FAD AND SUBSTRATE,
RP COFACTOR, SUBUNIT, AND MUTAGENESIS OF TYR-361 AND TYR-419.
RX PubMed=16981688; DOI=10.1021/bi061139a;
RA Mallett T.C., Wallen J.R., Karplus P.A., Sakai H., Tsukihara T.,
RA Claiborne A.;
RT "Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at
RT 1.54 A resolution.";
RL Biochemistry 45:11278-11289(2006).
CC -!- FUNCTION: Catalyzes specifically the NADPH-dependent reduction of
CC coenzyme A disulfide. Is also active with other disulfide substrates
CC containing at least one 4'-phosphopantethienyl moiety such as 4,4'-
CC diphosphopantethine, but is not able to reduce oxidized glutathione,
CC cystine, pantethine, or H(2)O(2).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 CoA + NADP(+) = CoA-disulfide + H(+) + NADPH;
CC Xref=Rhea:RHEA:14705, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62209; EC=1.8.1.14;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:16981688};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:16981688};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 uM for NADPH;
CC KM=11 uM for CoA disulfide;
CC KM=140 uM for 3'-dephospho-CoA disulfide;
CC KM=80 uM for 4,4'-diphosphopantethine;
CC KM=1100 uM for CoA glutathione mixed disulfide;
CC pH dependence:
CC Optimum pH is 7.0-8.0.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16981688}.
CC -!- DOMAIN: Contains 2 FAD binding domains and a single NADPH binding
CC domain.
CC -!- MASS SPECTROMETRY: Mass=49153; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10052943};
CC -!- MISCELLANEOUS: Reduction of disulfides occurs by a thiol-disulfide
CC exchange reaction, but involves only a single catalytic cysteine
CC residue that forms a stable mixed disulfide with CoA during catalysis.
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AF041467; AAB97073.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30033.1; -; Genomic_DNA.
DR RefSeq; YP_499461.1; NC_007795.1.
DR PDB; 1YQZ; X-ray; 1.54 A; A/B=1-438.
DR PDBsum; 1YQZ; -.
DR AlphaFoldDB; O52582; -.
DR SMR; O52582; -.
DR STRING; 1280.SAXN108_0965; -.
DR EnsemblBacteria; ABD30033; ABD30033; SAOUHSC_00908.
DR GeneID; 3920795; -.
DR KEGG; sao:SAOUHSC_00908; -.
DR PATRIC; fig|93061.5.peg.829; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_3_9; -.
DR BRENDA; 1.8.1.14; 3352.
DR SABIO-RK; O52582; -.
DR EvolutionaryTrace; O52582; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0050451; F:CoA-disulfide reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR HAMAP; MF_01608; CoA_diS_reduct; 1.
DR InterPro; IPR017758; CoA_disulphide_reductase.
DR InterPro; IPR023536; CoA_disulphide_reductase_staph.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR03385; CoA_CoA_reduc; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; FAD; Flavoprotein; NADP;
KW Oxidoreductase; Redox-active center; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9488708"
FT CHAIN 2..438
FT /note="Coenzyme A disulfide reductase"
FT /id="PRO_0000184688"
FT ACT_SITE 43
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:10052943"
FT ACT_SITE 43
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:10052943"
FT BINDING 8..33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16981688"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16981688"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16981688"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16981688"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16981688"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16981688"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16981688"
FT BINDING 151..166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 267..277
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16981688"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16981688"
FT BINDING 419
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16981688"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16981688"
FT MUTAGEN 43
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10052943"
FT MUTAGEN 361
FT /note="Y->F: Reduces activity by 92%. Loss of activity;
FT when associated with F-419."
FT /evidence="ECO:0000269|PubMed:16981688"
FT MUTAGEN 419
FT /note="Y->F: Reduces activity by 80%. Loss of activity;
FT when associated with F-361."
FT /evidence="ECO:0000269|PubMed:16981688"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1YQZ"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1YQZ"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 279..290
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 295..310
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 340..345
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 348..358
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 367..375
FT /evidence="ECO:0007829|PDB:1YQZ"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:1YQZ"
FT STRAND 380..391
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 392..404
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 410..414
FT /evidence="ECO:0007829|PDB:1YQZ"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:1YQZ"
FT HELIX 429..435
FT /evidence="ECO:0007829|PDB:1YQZ"
SQ SEQUENCE 438 AA; 49241 MW; 3A9B643BD8D44402 CRC64;
MPKIVVVGAV AGGATCASQI RRLDKESDII IFEKDRDMSF ANCALPYVIG EVVEDRRYAL
AYTPEKFYDR KQITVKTYHE VIAINDERQT VSVLNRKTNE QFEESYDKLI LSPGASANSL
GFESDITFTL RNLEDTDAID QFIKANQVDK VLVVGAGYVS LEVLENLNER GLHPTLIHRS
DKINKLMDAD MNQPILDELD KREIPYRLNE EINAINGNEI TFKSGKVEHY DMIIEGVGTH
PNSKFIESSN IKLDRKGFIP VNDKFETNVP NIYAIGDIAT SHYRHVDLPA SVPLAWGAHR
AASIVAEQIA GNDTIEFKGF LGNNIVKFFD YTFASVGVKP NELKQFDYKM VEVTQGAHAN
YYPGNSPLHL RVYYDTSNRQ ILRAAAVGKE GADKRIDVLS MAMMNQLTVD ELTEFEVAYA
PPYSHPKDLI NMIGYKAK
