NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
PubMed=12125824 [NCBI, ExPASy, EBI, Israel, Japan]
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., Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.;
"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.";
J. Mol. Microbiol. Biotechnol. 4:453-461(2002).

[2]

FUNCTION, AND SOURCE OF ELECTRONS.
STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
DOI=10.1016/S0014-5793(98)00555-9; PubMed=9654152 [NCBI, ExPASy, EBI, Israel, Japan]
Baeumer S., Murakami E., Brodersen J., Gottschalk G., Ragsdale S.W., Deppenmeier U.;
"The F420H2:heterodisulfide oxidoreductase system from Methanosarcina species. 2-Hydroxyphenazine mediates electron transfer from F420H2 dehydrogenase to heterodisulfide reductase.";
FEBS Lett. 428:295-298(1998).

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 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.
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

AE008384; AAM31539.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_633867.1; -.

3D structure databases

ModBase

Q8PVW4.

Enzyme and pathway databases

BioCyc

MMAZ192952:MM1843-MON; -.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0051912;	Molecular function: CoB--CoM heterodisulfide reductase activity (inferred from electronic annotation from EC).
GO:0015948;	Biological process: methanogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

ProtoNet

Q8PVW4.

Genome annotation databases

GeneID

1480185; -.

GenomeReviews

AE008384_GR; MM_1843.

KEGG

mma:MM_1843; -.

NMPDR

fig|192952.1.peg.1843; -.

Phylogenomic databases

HOGENOM

Q8PVW4; -.

Genome annotation databases

CMR

Q8PVW4; MM_1843.

Other

UniRef

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

Keywords

Cell membrane; Complete proteome; Membrane; Methanogenesis; Oxidoreductase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 259`	`259`	`CoB--CoM heterodisulfide reductase 2 subunit E.`	`PRO_0000150084`
`TRANSMEM`	`15 35`	`21`	`Potential.`
`TRANSMEM`	`104 124`	`21`	`Potential.`
`TRANSMEM`	`147 167`	`21`	`Potential.`
`TRANSMEM`	`180 200`	`21`	`Potential.`
`TRANSMEM`	`218 238`	`21`	`Potential.`

Sequence information

Length: 259 AA [This is the length of the unprocessed precursor]

Molecular weight: 28989 Da [This is the MW of the unprocessed precursor]

CRC64: A328ADE9E99406F9 [This is a checksum on the sequence]

        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

Q8PVW4 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