Coenzyme A disulfide reductase - Pyrococcus horikoshii

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Reviewed, UniProtKB/Swiss-Prot O58308 (CDR_PYRHO)

Last modified June 16, 2009. Version 57. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

Ordered Locus Names:

PH0572

Organism

Pyrococcus horikoshii [Complete proteome] [HAMAP]

Taxonomic identifier

53953 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

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Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Acts as a coenzyme A disulfide reductase. Specific for CoA disulfide. Shows a slow NAD(P)H oxidase activity in the presence of high concentrations of substrate-level FAD. This demonstrates that it is not likely to act as an NADH oxidase in vivo.
Catalytic activity	2 CoA + NAD(P)⁺ = CoA-disulfide + NAD(P)H.
Cofactor	Binds 1 FAD per subunit.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family.
Biophysicochemical properties	Kinetic parameters: KM value for NADH is lower than 9uM. K_M=73 µM for NADH Temperature dependence: Optimum temperature is 85 degrees Celsius. Thermostable.

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Ontologies

Keywords
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD
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: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	CoA-disulfide reductase activity Inferred from electronic annotation. Source: EC FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 445

445

Coenzyme A disulfide reductase

PRO_0000184699

Regions

Nucleotide binding

13 – 38

FAD By similarity

Nucleotide binding

154 – 169

NADP By similarity

Nucleotide binding

273 – 283

FAD By similarity

Sites

Active site

Nucleophile By similarity

Active site

Redox-active By similarity

Binding site

Substrate By similarity

Binding site

Substrate By similarity

Binding site

Substrate By similarity

Binding site

Substrate By similarity

Binding site

Substrate By similarity

Binding site

425

FAD; via carbonyl oxygen By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

O58308-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 896A034000A0B233
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FASTA

445

48,977

        10         20         30         40         50         60 
MGENMKKKVV IIGGGAAGMS AASRVKRLKP EWDVKVFEAT EWVSHAPCGI PYVVEGLSTP 

        70         80         90        100        110        120 
DKLMYYPPEV FIKKRGIDLH LNAEVIEVDT GYVRVRENGG EKSYEWDYLV FANGASPQVP 

       130        140        150        160        170        180 
AIEGVNLKGV FTADLPPDAL AIREYMEKYK VENVVIIGGG YIGIEMAEAF AAQGKNVTMI 

       190        200        210        220        230        240 
VRGERVLRRS FDKEVTDILE EKLKKHVNLR LQEITMKIEG EERVEKVVTD AGEYKAELVI 

       250        260        270        280        290        300 
LATGIKPNIE LAKQLGVRIG ETGAIWTNEK MQTSVENVYA AGDVAETRHV ITGRRVWVPL 

       310        320        330        340        350        360 
APAGNKMGYV AGSNIAGKEL HFPGVLGTAV TKFMDVEIGK TGLTEMEALK EGYDVRTAFI 

       370        380        390        400        410        420 
KASTRPHYYP GGREIWLKGV VDNETNRLLG VQVVGSDILP RIDTAAAMLM AGFTTKDAFF 

       430        440 
TDLAYAPPFA PVWDPLIVLA RVLKF

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: OT3.
[2]	"Discovery and characterization of a coenzyme A disulfide reductase from Pyrococcus horikoshii. Implications for this disulfide metabolism of anaerobic hyperthermophiles." Harris D.R., Ward D.E., Feasel J.M., Lancaster K.M., Murphy R.D., Mallet T.C., Crane E.J. III FEBS J. 272:1189-1200(2005) [PubMed: 15720393] [Abstract] Cited for: CHARACTERIZATION.

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Cross-references

Sequence databases
	BA000001 Genomic DNA. Translation: BAA29661.1.
PIR	H71171.
RefSeq	NP_142538.1.
3D structure databases
HSSP	HSSP built from PDB template 1NHP based on UniProtKB P37062.
ModBase	Search...
Genome annotation databases
GeneID	1442906.
GenomeReviews	Gene locus PH0572 in contig BA000001_GR.
KEGG	pho:PH0572.
NMPDR	fig\|70601.1.peg.559.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O58308.
OMA	O58308. KSHEDLM.
Enzyme and pathway databases
BRENDA	1.8.1.14. 74679.
Family and domain databases
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. 2 hits. 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...

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Entry information

Entry name

CDR_PYRHO

Accession

Primary (citable) accession number: O58308

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2005
Last sequence update:	August 1, 1998
Last modified:	June 16, 2009
This is version 57 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)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents