[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-24. PubMed=9063468 [NCBI, ExPASy, EBI, Israel, Japan] Kuenkel A., Vaupel M., Heim S., Thauer R.K., Hedderich R.; "Heterodisulfide reductase from methanol-grown cells of Methanosarcina barkeri is not a flavoenzyme."; Eur. J. Biochem. 244:226-234(1997).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1128/JB.00810-06; PubMed=16980466 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes."; J. Bacteriol. 188:7922-7931(2006).
[3]	FUNCTION, SUBUNIT, AND PROTEIN SEQUENCE OF 1-24. PubMed=8174566 [NCBI, ExPASy, EBI, Israel, Japan] Heiden S., Hedderich R., Setzke E., Thauer R.K.; "Purification of a two-subunit cytochrome-b-containing heterodisulfide reductase from methanol-grown Methanosarcina barkeri."; Eur. J. Biochem. 221:855-861(1994).

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.
CATALYTIC ACTIVITY: Coenzyme B + coenzyme M + methanophenazine = N-(7-((2-sulfoethyl)dithio)heptanoyl)-O³-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: The heterodisulfide reductase is composed of two subunits; hdrD and hdrE.
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein (Potential).
SIMILARITY: Belongs to the hdrE family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Y09870; CAA70996.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000099; AAZ70544.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S43469; S43469.

RefSeq

YP_305124.1; -.

3D structure databases

ModBase

P96796.

Enzyme and pathway databases

BioCyc

MBAR269797:MBAR_A1598-MON; -.

Ontologies

GO:0016021;	Cellular component: integral to membrane (non-traceable author statement from UniProtKB).
GO:0051912;	Molecular function: CoB--CoM heterodisulfide reductase activity (inferred from direct assay from UniProtKB).
GO:0015948;	Biological process: methanogenesis (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

BLOCKS

P96796.

Genome annotation databases

GeneID

3624317; -.

GenomeReviews

CP000099_GR; Mbar_A1598.

KEGG

mba:Mbar_A1598; -.

NMPDR

fig|269797.3.peg.1906; -.

Phylogenomic databases

HOGENOM

P96796; -.

Genome annotation databases

CMR

P96796; Mbar_A1598.

Other

ProtoNet

P96796.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell membrane; Complete proteome; Direct protein sequencing; Membrane; Methanogenesis; Oxidoreductase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 263`	`263`	`CoB--CoM heterodisulfide reductase subunit E.`	`PRO_0000150083`
`TRANSMEM`	`18 38`	`21`	`Potential.`
`TRANSMEM`	`108 128`	`21`	`Potential.`
`TRANSMEM`	`150 170`	`21`	`Potential.`
`TRANSMEM`	`184 204`	`21`	`Potential.`
`TRANSMEM`	`221 241`	`21`	`Potential.`
`CONFLICT`	`1 2`		`MS -> K (in Ref. 3; AA sequence).`

Sequence information

Length: 263 AA [This is the length of the unprocessed precursor]

Molecular weight: 29734 Da [This is the MW of the unprocessed precursor]

CRC64: 8202887145462E08 [This is a checksum on the sequence]

        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

P96796 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools