Reviewed, UniProtKB/Swiss-Prot P96796 (HDRE_METBF)

Names and origin

Protein names

Recommended name:
    CoB--CoM heterodisulfide reductase subunit E
    EC=1.8.98.1

Gene names

Name:	hdrE
Ordered Locus Names:	Mbar_A1598

Organism

Methanosarcina barkeri (strain Fusaro / DSM 804) [Complete proteome] [HAMAP]

Taxonomic identifier

269797 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	263 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
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 is composed of two subunits; hdrD and hdrE.
Subcellular location	Cell membrane; Multi-pass membrane proteinPotential.
Sequence similarities	Belongs to the hdrE family.

Ontologies

Keywords
Biological process	Methanogenesis
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	methanogenesis Ref.3 Inferred from direct assay. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Ref.1 Non-traceable author statement. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	CoB--CoM heterodisulfide reductase activity Ref.3 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 263	263	CoB--CoM heterodisulfide reductase subunit E		PRO_0000150083
Regions
	Transmembrane	18 – 38	21	Potential
	Transmembrane	108 – 128	21	Potential
	Transmembrane	150 – 170	21	Potential
	Transmembrane	184 – 204	21	Potential
	Transmembrane	221 – 241	21	Potential
Experimental info
	Sequence conflict	1 – 2	2	MS → K AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P96796-1 [UniParc]. Last modified January 1, 1998. Version 2. Checksum: 8202887145462E08	FASTA	263	29,734
	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

References

	« Hide 'large scale' referencesShow '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
EMBLGenBankDDBJ	Y09870 Genomic DNA. Translation: CAA70996.1. CP000099 Genomic DNA. Translation: AAZ70544.1. Different initiation.
PIR	S43469.
RefSeq	YP_305124.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3624317.
GenomeReviews	Gene locus Mbar_A1598 in contig CP000099_GR.
KEGG	mba:Mbar_A1598.
NMPDR	fig|269797.3.peg.1906.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P96796.
Enzyme and pathway databases
BioCyc	MBAR269797:MBAR_A1598-MON.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

HDRE_METBF

Accession

Primary (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:	November 25, 2008
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)