NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/S0140-6736(02)08713-5; PubMed=12044378 [NCBI, ExPASy, EBI, Israel, Japan]
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
"Genome and virulence determinants of high virulence community-acquired MRSA.";
Lancet 359:1819-1827(2002).

Comments

FUNCTION: Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide (By similarity).
CATALYTIC ACTIVITY: 2 CoA + NAD(P)⁺ = CoA-disulfide + NAD(P)H.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBUNIT: Homodimer (By similarity).
DOMAIN: Contains 2 FAD binding domains and a single NADPH binding domain (By similarity).
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 (By similarity).
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

BA000033; BAB94717.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_645669.1; -.

3D structure databases

SMR

Q8NXE8; 1-437, 2-438.

ModBase

Q8NXE8.

Enzyme and pathway databases

BioCyc

SAUR196620:MW0852-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

1002964; -.

GenomeReviews

BA000033_GR; MW0852.

KEGG

sam:MW0852; -.

Phylogenomic databases

HOGENOM

Q8NXE8; -.

Genome annotation databases

CMR

Q8NXE8; MW0852.

Other

ProtoNet

Q8NXE8.

UniRef

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

Keywords

Complete proteome; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 438`	`437`	`Coenzyme A disulfide reductase.`	`PRO_0000184694`
`NP_BIND`	`8 33`	`26`	`FAD (By similarity).`
`NP_BIND`	`151 166`	`16`	`NADP (By similarity).`
`NP_BIND`	`267 277`	`11`	`FAD (By similarity).`
`ACT_SITE`	`43 43`		`Nucleophile (By similarity).`
`ACT_SITE`	`43 43`		`Redox-active (By similarity).`
`BINDING`	`15 15`		`Substrate (By similarity).`
`BINDING`	`19 19`		`Substrate (By similarity).`
`BINDING`	`22 22`		`Substrate (By similarity).`
`BINDING`	`39 39`		`Substrate (By similarity).`
`BINDING`	`42 42`		`Substrate (By similarity).`
`BINDING`	`71 71`		`Substrate (By similarity).`
`BINDING`	`299 299`		`Substrate (By similarity).`
`BINDING`	`419 419`		`FAD; via carbonyl oxygen (By similarity).`
`BINDING`	`427 427`		`Substrate (By similarity).`

Sequence information

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

Molecular weight: 49277 Da [This is the MW of the unprocessed precursor]

CRC64: 33E0A8764616BD80 [This is a checksum on the sequence]

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

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

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

       190        200        210        220        230        240 
DKINKLMDAD MNQPILDELD KREIPYRLNE EIDAINGNEI 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

Q8NXE8 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