Reviewed, UniProtKB/Swiss-Prot A8Z076 (CDR_STAAT)

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:	USA300HOU_0929

Organism

Staphylococcus aureus (strain USA300 / TCH1516) [Complete proteome] [HAMAP]

Taxonomic identifier

451516 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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. HAMAP MF_01608
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	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.
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 electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 438	438	Coenzyme A disulfide reductase HAMAP MF_01608		PRO_1000088037
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)
	A8Z076-1 [UniParc]. Last modified January 15, 2008. Version 1. Checksum: 648B6AFDEFD440F8	FASTA	438	49,290
	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 LEVLENLYER 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

References

[1]

"Subtle genetic changes enhance virulence of methicillin resistant and sensitive Staphylococcus aureus." Highlander S.K., Hulten K.G., Qin X., Jiang H., Yerrapragada S., Mason E.O. Jr., Shang Y., Williams T.M., Fortunov R.M., Liu Y., Igboeli O., Petrosino J., Tirumalai M., Uzman A., Fox G.E., Cardenas A.M., Muzny D.M., Hemphill L. , Ding Y., Dugan S., Blyth P.R., Buhay C.J., Dinh H.H., Hawes A.C., Holder M., Kovar C.L., Lee S.L., Liu W., Nazareth L.V., Wang Q., Zhou J., Kaplan S.L., Weinstock G.M. BMC Microbiol. 7:99-99(2007) [PubMed: 17986343] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000730 Genomic DNA. Translation: ABX28950.1.
RefSeq	YP_001574829.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5775907.
GenomeReviews	Gene locus USA300HOU_0929 in contig CP000730_GR.
KEGG	sax:USA300HOU_0929.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	IVTEYNF.
Family and domain databases
HAMAP	MF_01608. [Tree]
InterPro	IPR017758. CoA_disulphide_reductase. 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.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03385. CoA_CoA_reduc. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CDR_STAAT

Accession

Primary (citable) accession number: A8Z076

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	January 15, 2008
Last modified:	November 3, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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