Reviewed, UniProtKB/Swiss-Prot Q5HQI9 (CDR_STAEQ)

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:	SERP0560

Organism

Staphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]

Taxonomic identifier

176279 [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_0000184696
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)
	Q5HQI9-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 5B27C5462208D91A	FASTA	438	49,366
	10 20 30 40 50 60 MNKIIIVGAV AGGATCASQI RRLDKESEII VFEKDRDMSF ANCALPYYIG NVIEDRRKVL 70 80 90 100 110 120 AYTPNQFYDK KQITVKTYHE VIQINDERQT VTVLNHQTNQ TFEESYDTLI LSPGASANRL 130 140 150 160 170 180 NTHSDISFTV RNLEDTETID TFITNTKAQR ALVVGAGYIS LEVLENLHHR GLDVTWIHRS 190 200 210 220 230 240 TNINKLMDQD MNQPIIDEIE KRNITYRFNE EISHVNGHEV TFTSGKVENF DLIIEGVGTH 250 260 270 280 290 300 PNSQFIKSSN VILNDKGYIP VNHNFQTNIP NIYALGDVIT SHYRHVNLPA QVPLAWGAHR 310 320 330 340 350 360 GASIIAEQLS GNSSIHFKGY LGNNIVKFFD YTLASVGIKP NELKNFDYDM VEVKQGAHAG 370 380 390 400 410 420 YYPGNSPLHL RVYFEKDSRK LIRAAAVGKQ GADKRIDVLS MAMMNNATVD DLTEFEVAYA 430 PPYSHPKDLI NLIGYKAQ

References

[1]

"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain." Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M. J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000029 Genomic DNA. Translation: AAW53947.1.
RefSeq	YP_188151.1.
3D structure databases
SMR	Q5HQI9. Positions 3-438.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5HQI9.
Genome annotation databases
GeneID	3241478.
GenomeReviews	Gene locus SERP0560 in contig CP000029_GR.
KEGG	ser:SERP0560.
TIGR	SERP0560.
Phylogenomic databases
HOGENOM	Q5HQI9.
OMA	IVTEYNF.
Enzyme and pathway databases
BioCyc	SEPI176279:SERP0560-MON.
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_STAEQ

Accession

Primary (citable) accession number: Q5HQI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2005
Last sequence update:	February 15, 2005
Last modified:	November 3, 2009
This is version 37 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)