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Reviewed, UniProtKB/Swiss-Prot Q8PVW4 (HDRE_METMA)

Last modified June 16, 2009. Version 40. 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 2 subunit E
    EC=1.8.98.1
Gene names
Name: hdrE
Ordered Locus Names: MM_1843
OrganismMethanosarcina mazei (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier2209 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length259 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). HdrE may be responsible for anchoring the complex to the membrane. Ref.2

Catalytic activity

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

Pathway

Cofactor metabolism; coenzyme B/coenzyme M regeneration; coenzyme B and coenzyme M from CoB-CoM heterodisulfide: step 1/1.

Subunit structure

The heterodisulfide reductase 2 is composed of two subunits; hdrD and hdrE By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein Potential.

Miscellaneous

Methanophenazine seems to mediate electron transfer from a F420-non-reducing hydrogenase to the heterodisulfide reductase 2.

Sequence similarities

Belongs to the hdrE family.

Ontologies

Keywords
   Biological processMethanogenesis
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processmethanogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionCoB--CoM heterodisulfide reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 259259CoB--CoM heterodisulfide reductase 2 subunit E
PRO_0000150084

Regions

Transmembrane15 – 3521 Potential
Transmembrane104 – 12421 Potential
Transmembrane147 – 16721 Potential
Transmembrane180 – 20021 Potential
Transmembrane218 – 23821 Potential

Sequences

Sequence LengthMass (Da)Tools
Q8PVW4-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: A328ADE9E99406F9

FASTA25928,989
        10         20         30         40         50         60 
MAYFSGLSDA LRLTFVQIMI LSAIAVVIFL YGMIGNFQKW GAGVTGYALE PPTGKKGSAI 

        70         80         90        100        110        120 
RFLKTWWAQV RAESHHHGKP ILEVLILDIF FQRRILKRSP IRWFMHFTIF AGWMSLFALS 

       130        140        150        160        170        180 
GLMFAVEMTE KIGIELPFTP AEFREMLSLP NYIFGYILLI GVMIAVVRRL FVSEVREASI 

       190        200        210        220        230        240 
MYDWVLLGGV FIVTISGFIA DGIRTGIIWG FGLDPVTAPP AALFHSVISL LFCIAYIPYS 

       250 
KYIHVIATPL AILANKGGE 

« Hide

References

« Hide 'large scale' references
[1]"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88.
[2]"The F420H2:heterodisulfide oxidoreductase system from Methanosarcina species. 2-Hydroxyphenazine mediates electron transfer from F420H2 dehydrogenase to heterodisulfide reductase."
Baeumer S., Murakami E., Brodersen J., Gottschalk G., Ragsdale S.W., Deppenmeier U.
FEBS Lett. 428:295-298(1998) [PubMed: 9654152] [Abstract]
Cited for: FUNCTION, SOURCE OF ELECTRONS.
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88.

Cross-references

Sequence databases

AE008384 Genomic DNA. Translation: AAM31539.1.
RefSeqNP_633867.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1480185.
GenomeReviewsGene locus MM_1843 in contig AE008384_GR.
KEGGmma:MM_1843.
NMPDRfig|192952.1.peg.1843.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8PVW4.
OMAQ8PVW4. REASIMY.

Enzyme and pathway databases

BioCycMMAZ192952:MM1843-MON.
BRENDA1.8.98.1. 261165.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameHDRE_METMA
AccessionPrimary (citable) accession number: Q8PVW4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 40 of the entry and version 1 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