[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15 AND 193-208. DOI=10.1074/jbc.273.10.5752; PubMed=9488708 [NCBI, ExPASy, EBI, Israel, Japan] delCardayre S.B., Davies J.E.; "Staphylococcus aureus coenzyme A disulfide reductase, a new subfamily of pyridine nucleotide-disulfide oxidoreductase. Sequence, expression, and analysis of cdr."; J. Biol. Chem. 273:5752-5757(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.; "The Staphylococcus aureus NCTC8325 genome."; Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[3]	CHARACTERIZATION. DOI=10.1074/jbc.273.10.5744; PubMed=9488707 [NCBI, ExPASy, EBI, Israel, Japan] delCardayre S.B., Stock K.P., Newton G.L., Fahey R.C., Davies J.E.; "Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus. Purification and characterization of the native enzyme."; J. Biol. Chem. 273:5744-5751(1998).
[4]	CHARACTERIZATION, ACTIVE SITE, MUTAGENESIS OF CYS-43, AND MASS SPECTROMETRY. DOI=10.1021/bi9825899; PubMed=10052943 [NCBI, ExPASy, EBI, Israel, Japan] Luba J., Charrier V., Claiborne A.; "Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction with pyridine nucleotides."; Biochemistry 38:2725-2737(1999).
[5]	X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH FAD AND SUBSTRATE, MUTAGENESIS OF TYR-361 AND TYR-419, AND SUBUNIT. DOI=10.1021/bi061139a; PubMed=16981688 [NCBI, ExPASy, EBI, Israel, Japan] Mallett T.C., Wallen J.R., Karplus P.A., Sakai H., Tsukihara T., Claiborne A.; "Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution."; Biochemistry 45:11278-11289(2006).

Comments

FUNCTION: Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide. Is also active with other disulfide substrates containing at least one 4'-phosphopantethienyl moiety such as 4,4'-diphosphopantethine, but is not able to reduce oxidized glutathione, cystine, pantethine, or H(2)O(2).
CATALYTIC ACTIVITY: 2 CoA + NAD(P)⁺ = CoA-disulfide + NAD(P)H.
COFACTOR: Binds 1 FAD per subunit.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=2 µM for NADPH;
	K_M=11 µM for CoA disulfide;
	K_M=140 µM for 3'-dephospho-CoA disulfide;
	K_M=80 µM for 4,4'-diphosphopantethine;
	K_M=1100 µM for CoA glutathione mixed disulfide;
pH dependence:	Optimum pH is 7.0-8.0;

SUBUNIT: Homodimer.
DOMAIN: Contains 2 FAD binding domains and a single NADPH binding domain.
MASS SPECTROMETRY: Mass=49153; Method=Electrospray; Range=2-438; Source=PubMed:10052943;.
MISCELLANEOUS: Reduction of disulfides occurs by a thiol-disulfide exchange reaction, but involves only a single catalytic cysteine residue that forms a stable mixed disulfide with CoA during catalysis.
SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family.

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

AF041467; AAB97073.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000253; ABD30033.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_499461.1; -.

3D structure databases

PDB

1YQZ; X-ray; 1.54 A; A/B=1-438.

[ExPASy / RCSB / EBI]

PDBsum

1YQZ; -.

ModBase

O52582.

Enzyme and pathway databases

BioCyc

SAUR93061:SAOUHSC_00908-MON; -.

Ontologies

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

3920795; -.

GenomeReviews

CP000253_GR; SAOUHSC_00908.

KEGG

sao:SAOUHSC_00908; -.

Phylogenomic databases

HOGENOM

O52582; -.

Genome annotation databases

CMR

O52582; SAOUHSC_00908.

Other

ProtoNet

O52582.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Direct protein sequencing; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 438`	`437`	`Coenzyme A disulfide reductase.`	`PRO_0000184688`
`NP_BIND`	`8 33`	`26`	`FAD.`
`NP_BIND`	`151 166`	`16`	`NADP (By similarity).`
`NP_BIND`	`267 277`	`11`	`FAD.`
`ACT_SITE`	`43 43`		`Nucleophile.`
`ACT_SITE`	`43 43`		`Redox-active.`
`BINDING`	`15 15`		`Substrate.`
`BINDING`	`19 19`		`Substrate.`
`BINDING`	`22 22`		`Substrate.`
`BINDING`	`39 39`		`Substrate.`
`BINDING`	`42 42`		`Substrate.`
`BINDING`	`71 71`		`Substrate.`
`BINDING`	`299 299`		`Substrate.`
`BINDING`	`419 419`		`FAD; via carbonyl oxygen.`
`BINDING`	`427 427`		`Substrate.`
`MUTAGEN`	`43 43`		`C->S: Loss of activity.`
`MUTAGEN`	`361 361`		`Y->F: Reduces activity by 92%. Loss of activity; when associated with F-419.`
`MUTAGEN`	`419 419`		`Y->F: Reduces activity by 80%. Loss of activity; when associated with F-361.`
`STRAND`	`4 7`	`4`
`HELIX`	`13 23`	`11`
`STRAND`	`25 27`	`3`
`STRAND`	`29 36`	`8`
`STRAND`	`38 40`	`3`
`HELIX`	`42 44`	`3`
`HELIX`	`45 49`	`5`
`HELIX`	`56 59`	`4`
`HELIX`	`64 71`	`8`
`STRAND`	`74 77`	`4`
`STRAND`	`79 85`	`7`
`TURN`	`86 89`	`4`
`STRAND`	`90 95`	`6`
`TURN`	`96 99`	`4`
`STRAND`	`100 105`	`6`
`STRAND`	`107 111`	`5`
`STRAND`	`115 117`	`3`
`HELIX`	`133 146`	`14`
`STRAND`	`150 154`	`5`
`HELIX`	`158 170`	`13`
`STRAND`	`173 181`	`9`
`HELIX`	`189 192`	`4`
`HELIX`	`193 201`	`9`
`STRAND`	`206 209`	`4`
`STRAND`	`212 216`	`5`
`STRAND`	`219 222`	`4`
`STRAND`	`227 229`	`3`
`STRAND`	`231 235`	`5`
`STRAND`	`239 242`	`4`
`HELIX`	`244 246`	`3`
`STRAND`	`272 274`	`3`
`HELIX`	`276 278`	`3`
`STRAND`	`279 290`	`12`
`HELIX`	`295 310`	`16`
`STRAND`	`324 328`	`5`
`STRAND`	`331 338`	`8`
`HELIX`	`340 345`	`6`
`STRAND`	`348 358`	`11`
`STRAND`	`362 364`	`3`
`STRAND`	`367 375`	`9`
`TURN`	`376 378`	`3`
`STRAND`	`380 391`	`12`
`HELIX`	`392 404`	`13`
`HELIX`	`410 414`	`5`
`TURN`	`421 423`	`3`
`HELIX`	`429 435`	`7`

Sequence information

Length: 438 AA [This is the length of the unprocessed precursor]

Molecular weight: 49241 Da [This is the MW of the unprocessed precursor]

CRC64: 3A9B643BD8D44402 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPKIVVVGAV AGGATCASQI RRLDKESDII IFEKDRDMSF ANCALPYVIG EVVEDRRYAL 

        70         80         90        100        110        120 
AYTPEKFYDR KQITVKTYHE VIAINDERQT VSVLNRKTNE QFEESYDKLI LSPGASANSL 

       130        140        150        160        170        180 
GFESDITFTL RNLEDTDAID QFIKANQVDK VLVVGAGYVS LEVLENLNER GLHPTLIHRS 

       190        200        210        220        230        240 
DKINKLMDAD MNQPILDELD KREIPYRLNE EINAINGNEI TFKSGKVEHY DMIIEGVGTH 

       250        260        270        280        290        300 
PNSKFIESSN IKLDRKGFIP VNDKFETNVP NIYAIGDIAT SHYRHVDLPA SVPLAWGAHR 

       310        320        330        340        350        360 
AASIVAEQIA GNDTIEFKGF LGNNIVKFFD YTFASVGVKP NELKQFDYKM VEVTQGAHAN 

       370        380        390        400        410        420 
YYPGNSPLHL RVYYDTSNRQ ILRAAAVGKE GADKRIDVLS MAMMNQLTVD ELTEFEVAYA 

       430 
PPYSHPKDLI NMIGYKAK

O52582 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools