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Reviewed, UniProtKB/Swiss-Prot O27906 (HDRC_METTH)

Last modified September 22, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    CoB--CoM heterodisulfide reductase iron-sulfur subunit C
    EC=1.8.98.1
Gene names
Name: hdrC
Ordered Locus Names: MTH_1878
OrganismMethanobacterium thermoautotrophicum [Complete proteome] [HAMAP]
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B). HdrC may carry electrons from hydrogenase to hdrA By similarity.

Catalytic activity

Coenzyme B + coenzyme M + methanophenazine = N-(7-((2-sulfoethyl)dithio)heptanoyl)-O(3)-phospho-L-threonine + dihydromethanophenazine.

Cofactor

Binds 2 4Fe-4S clusters per subunit By similarity.

Pathway

Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B heterodisulfide: step 1/1.

Subunit structure

The heterodisulfide reductase is composed of three subunits; hdrA, hdrB and hdrC. It forms a complex with the F420-non-reducing hydrogenase (Mvh), which provides the reducing equivalents to the heterodisulfide reductase By similarity.

Sequence similarities

Belongs to the hdrC family.

Contains 2 4Fe-4S ferredoxin-type domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 185185CoB--CoM heterodisulfide reductase iron-sulfur subunit C
PRO_0000150077

Regions

Domain25 – 55314Fe-4S ferredoxin-type 1
Domain68 – 99324Fe-4S ferredoxin-type 2

Sites

Metal binding351Iron-sulfur 1 (4Fe-4S) Potential
Metal binding381Iron-sulfur 1 (4Fe-4S) Potential
Metal binding411Iron-sulfur 1 (4Fe-4S) Potential
Metal binding451Iron-sulfur 2 (4Fe-4S) Potential
Metal binding791Iron-sulfur 2 (4Fe-4S) Potential
Metal binding821Iron-sulfur 2 (4Fe-4S) Potential
Metal binding851Iron-sulfur 2 (4Fe-4S) Potential
Metal binding891Iron-sulfur 1 (4Fe-4S) Potential

Sequences

Sequence LengthMass (Da)Tools
O27906-1 [UniParc].

Last modified January 16, 2004. Version 2.
Checksum: 7DD936AFBDF9D499

FASTA18520,490
        10         20         30         40         50         60 
MTLLQREENI IRKGNIDKEF SEKIKAAGGD SLEYCFQCGT CTGSCPSGRR TPYRVRQIIR 

        70         80         90        100        110        120 
KANVGLKDEI ISDPALWMCT TCYSCQERCP RKVKIVDVVK LARNEAAKAG FMAPAHKAVG 

       130        140        150        160        170        180 
SFVIKTGHGV PINDATMELR KAVGLGELPP TTHQFPEALE EVQKIIKATG FDQLIGYNWE 


TGELE 

« Hide

References

[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Delta H.

Cross-references

Sequence databases

AE000666 Genomic DNA. Translation: AAB86344.1. Different initiation.
PIRC69118.
RefSeqNP_276984.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO27906.

Genome annotation databases

GeneID1470963.
GenomeReviewsGene locus MTH_1878 in contig AE000666_GR.
KEGGmth:MTH1878.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO27906.

Enzyme and pathway databases

BioCycMTHE187420:MTH1878-MON.
BRENDA1.8.98.1. 270.

Family and domain databases

InterProIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR017680. CoB/CoM_hetero-S_Rdtase_csu.
IPR012285. Fum_reductase_C.
[Graphical view]
Gene3DG3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
TIGRFAMsTIGR03290. CoB_CoM_SS_C. 1 hit.
PROSITEPS00198. 4FE4S_FER_1. 2 hits.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHDRC_METTH
AccessionPrimary (citable) accession number: O27906
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: September 22, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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