A6QFI1 (CDR_STAAE) Reviewed, UniProtKB/Swiss-Prot

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:	NWMN_0841

Organism

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

Taxonomic identifier

426430 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 protein thiol-disulfide exchange Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	CoA-disulfide reductase activity Inferred from electronic annotation. Source: EC NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding 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_1000073626
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)
	A6QFI1 [UniParc]. Last modified August 21, 2007. 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]

"Genome sequence of Staphylococcus aureus strain Newman and comparative analysis of staphylococcal genomes: polymorphism and evolution of two major pathogenicity islands." Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K. J. Bacteriol. 190:300-310(2008) [PubMed: 17951380] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Newman.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP009351 Genomic DNA. Translation: BAF67113.1.
RefSeq	YP_001331875.1. NC_009641.1.
3D structure databases
ProteinModelPortal	A6QFI1.
SMR	A6QFI1. Positions 2-438.
ModBase	Search...
Protein-protein interaction databases
STRING	A6QFI1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000031160; EBSTAP00000030030; EBSTAG00000031158.
GeneID	5330492.
GenomeReviews	Gene locus NWMN_0841 in contig AP009351_GR.
KEGG	sae:NWMN_0841.
PATRIC	19585171. VBIStaAur133992_0914.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0446.
GeneTree	EBGT00050000023767.
HOGENOM	HBG535576.
OMA	RNVMDIQ.
ProtClustDB	PRK13512.
Enzyme and pathway databases
BioCyc	SAUR426430:NWMN_0841-MONOMER.
Family and domain databases
HAMAP	MF_01608. CoA-diS-reduct. [Tree]
InterPro	IPR017758. CoA_disulphide_reductase. IPR023536. CoA_disulphide_reductase_staph. IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR001327. Pyr_OxRdtase_NAD-bd_dom. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
KO	K08255.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMs	TIGR03385. CoA_CoA_reduc. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CDR_STAAE

Accession

Primary (citable) accession number: A6QFI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	August 21, 2007
Last modified:	December 14, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program