Reviewed, UniProtKB/Swiss-Prot Q7A6H1 (CDR_STAAN)

Names and origin

Protein names

Recommended name:
    Coenzyme A disulfide reductase
      Short name=CoA-disulfide reductase
      Short name=CoADR
    EC=1.8.1.14

Gene names

Name:	cdr
Ordered Locus Names:	SA0831

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide By similarity. HAMAP MF_01608
Catalytic activity	2 CoA + NAD(P)+ = CoA-disulfide + NAD(P)H. HAMAP MF_01608
Cofactor	Binds 1 FAD per subunit By similarity. HAMAP MF_01608
Subunit structure	Homodimer By similarity. HAMAP MF_01608
Domain	Contains 2 FAD binding domains and a single NADPH binding domain By similarity. HAMAP MF_01608
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. HAMAP MF_01608
Sequence similarities	Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein thiol-disulfide exchange Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	CoA-disulfide reductase activity Inferred from electronic annotation. Source: HAMAP FAD binding Inferred from electronic annotation. Source: HAMAP NADP or NADPH binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 438	437	Coenzyme A disulfide reductase HAMAP MF_01608		PRO_0000184691
Regions
	Nucleotide binding	8 – 33	26	FAD By similarity
	Nucleotide binding	151 – 166	16	NADP By similarity
	Nucleotide binding	267 – 277	11	FAD By similarity
Sites
	Active site	43	1	Nucleophile By similarity
	Active site	43	1	Redox-active By similarity
	Binding site	15	1	Substrate By similarity
	Binding site	19	1	Substrate By similarity
	Binding site	22	1	Substrate By similarity
	Binding site	39	1	Substrate By similarity
	Binding site	42	1	Substrate By similarity
	Binding site	71	1	Substrate By similarity
	Binding site	299	1	Substrate By similarity
	Binding site	419	1	FAD; via carbonyl oxygen By similarity
	Binding site	427	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7A6H1-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 3970317541CFF013	FASTA	438	49,291
	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 VLVIGAGYVS 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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth." Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J. J. Microbiol. Methods 60:247-257(2005) [PubMed: 15590099] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[3]	"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000018 Genomic DNA. Translation: BAB42070.1.
PIR	C89864.
RefSeq	NP_374092.1.
3D structure databases
SMR	Q7A6H1. Positions 2-438.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7A6H1.
2-D gel databases
SWISS-2DPAGE	Q7A6H1.
Genome annotation databases
GeneID	1123646.
GenomeReviews	Gene locus SA0831 in contig BA000018_GR.
KEGG	sau:SA0831.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0446.
HOGENOM	HBG535576.
OMA	IVTEYNF.
Enzyme and pathway databases
BioCyc	SAUR158879:SA0831-MONOMER.
Family and domain databases
HAMAP	MF_01608. CoA-diS-reduct. [Tree]
InterPro	IPR017758. CoA_disulphide_reductase. IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
TIGRFAMs	TIGR03385. CoA_CoA_reduc. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CDR_STAAN

Accession

Primary (citable) accession number: Q7A6H1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 49 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)