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Reviewed, UniProtKB/Swiss-Prot P96796 (HDRE_METBF)

Last modified January 19, 2010. 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 subunit E
    EC=1.8.98.1
Gene names
Name: hdrE
Ordered Locus Names: Mbar_A1598
OrganismMethanosarcina barkeri (strain Fusaro / DSM 804) [Complete proteome] [HAMAP]
Taxonomic identifier269797 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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.3

Catalytic activity

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

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 two subunits; hdrD and hdrE. Ref.3

Subcellular location

Cell membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the hdrE family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 263263CoB--CoM heterodisulfide reductase subunit E
PRO_0000150083

Regions

Transmembrane18 – 3821 Potential
Transmembrane108 – 12821 Potential
Transmembrane150 – 17021 Potential
Transmembrane184 – 20421 Potential
Transmembrane221 – 24121 Potential

Experimental info

Sequence conflict1 – 22MS → K AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P96796-1 [UniParc].

Last modified January 1, 1998. Version 2.
Checksum: 8202887145462E08

FASTA26329,734
        10         20         30         40         50         60 
MSEEMLYFSG LSDVLRMTFV QIMIFSTIAI VIFLYGLISN FQKWGTGVTG YALEPQEGKK 

        70         80         90        100        110        120 
GSAITFLKTW WSQVTAESHH RGESILEILI LDILFQRRIL KRSPFRWVMH LFIFGGWMTL 

       130        140        150        160        170        180 
FALSGMMFAV EMTEKIGIAL PFTPAEFRDF LSIPNYIFGY ILLIGVLVAL VRRLFVSEVR 

       190        200        210        220        230        240 
EASIMYDWVL IGIVFLVTIS GFIADGIRTG FIWSFGLDPS VAPPAALFHS IFSLLFCIAF 

       250        260 
IPYSKYIHII AIPLALLANK GGE 

« Hide

References

« Hide 'large scale' references
[1]"Heterodisulfide reductase from methanol-grown cells of Methanosarcina barkeri is not a flavoenzyme."
Kuenkel A., Vaupel M., Heim S., Thauer R.K., Hedderich R.
Eur. J. Biochem. 244:226-234(1997) [PubMed: 9063468] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-24.
[2]"The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes."
Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.
J. Bacteriol. 188:7922-7931(2006) [PubMed: 16980466] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Purification of a two-subunit cytochrome-b-containing heterodisulfide reductase from methanol-grown Methanosarcina barkeri."
Heiden S., Hedderich R., Setzke E., Thauer R.K.
Eur. J. Biochem. 221:855-861(1994) [PubMed: 8174566] [Abstract]
Cited for: FUNCTION, SUBUNIT, PROTEIN SEQUENCE OF 1-24.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y09870 Genomic DNA. Translation: CAA70996.1.
CP000099 Genomic DNA. Translation: AAZ70544.1. Different initiation.
PIRS43469.
RefSeqYP_305124.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP96796.

Protein family/group databases

TCDB3.D.7.1.1. H2:heterodisulfide oxidoreductase (HHO) family.

Genome annotation databases

GeneID3624317.
GenomeReviewsGene locus Mbar_A1598 in contig CP000099_GR.
KEGGmba:Mbar_A1598.
NMPDRfig|269797.3.peg.1906.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG07835.
HOGENOMHBG538650.

Enzyme and pathway databases

BioCycMBAR269797:MBAR_A1598-MONOMER.
BRENDA1.8.98.1. 9.

Family and domain databases

InterProIPR003816. Nitrate_red_gam.
[Graphical view]
PfamPF02665. Nitrate_red_gam. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHDRE_METBF
AccessionPrimary (citable) accession number: P96796
Secondary accession number(s): Q46C48, Q9UWK1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: January 1, 1998
Last modified: January 19, 2010
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