ID   HDRE_METBF              Reviewed;         263 AA.
AC   P96796; Q46C48; Q9UWK1;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   02-SEP-2026, entry version 135.
DE   RecName: Full=Dihydromethanophenazine:CoB--CoM heterodisulfide reductase subunit E {ECO:0000305};
DE            EC=1.8.98.1 {ECO:0000250|UniProtKB:A0A0E3NFS5};
DE   AltName: Full=CoB--CoM heterodisulfide reductase subunit E {ECO:0000305};
DE   AltName: Full=Coenzyme B:coenzyme M:methanophenazine oxidoreductase subunit E {ECO:0000305};
GN   Name=hdrE; OrderedLocusNames=Mbar_A1598;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-24, FUNCTION, AND
RP   SUBUNIT.
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=9063468; DOI=10.1111/j.1432-1033.1997.00226.x;
RA   Kuenkel A., Vaupel M., Heim S., Thauer R.K., Hedderich R.;
RT   "Heterodisulfide reductase from methanol-grown cells of Methanosarcina
RT   barkeri is not a flavoenzyme.";
RL   Eur. J. Biochem. 244:226-234(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-24, FUNCTION, AND SUBUNIT.
RX   PubMed=8174566; DOI=10.1111/j.1432-1033.1994.tb18800.x;
RA   Heiden S., Hedderich R., Setzke E., Thauer R.K.;
RT   "Purification of a two-subunit cytochrome-b-containing heterodisulfide
RT   reductase from methanol-grown Methanosarcina barkeri.";
RL   Eur. J. Biochem. 221:855-861(1994).
CC   -!- FUNCTION: Part of a complex that catalyzes the reversible reduction of
CC       CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB
CC       (coenzyme B). HdrE may be responsible for anchoring the complex to the
CC       membrane. {ECO:0000305|PubMed:8174566, ECO:0000305|PubMed:9063468}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=methanophenazine + coenzyme B + coenzyme M =
CC         dihydromethanophenazine + coenzyme M-coenzyme B heterodisulfide;
CC         Xref=Rhea:RHEA:18085, ChEBI:CHEBI:29118, ChEBI:CHEBI:50375,
CC         ChEBI:CHEBI:58319, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=1.8.98.1;
CC         Evidence={ECO:0000250|UniProtKB:A0A0E3NFS5};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:A0A0E3NFS5};
CC       Note=Binds 2 heme b (iron(II)-protoporphyrin IX) groups per subunit.
CC       {ECO:0000250|UniProtKB:A0A0E3NFS5};
CC   -!- PATHWAY: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide
CC       reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B
CC       heterodisulfide: step 1/1. {ECO:0000305}.
CC   -!- SUBUNIT: The dihydromethanophenazine:CoB--CoM heterodisulfide reductase
CC       is composed of two subunits; HdrD and HdrE.
CC       {ECO:0000269|PubMed:8174566, ECO:0000269|PubMed:9063468}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the HdrE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAZ70544.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Y09870; CAA70996.1; -; Genomic_DNA.
DR   EMBL; CP000099; AAZ70544.1; ALT_INIT; Genomic_DNA.
DR   PIR; S43469; S43469.
DR   AlphaFoldDB; P96796; -.
DR   STRING; 269797.Mbar_A1598; -.
DR   TCDB; 3.D.7.1.1; the h2:heterodisulfide oxidoreductase (hho) family.
DR   PaxDb; 269797-Mbar_A1598; -.
DR   KEGG; mba:Mbar_A1598; -.
DR   eggNOG; arCOG05014; Archaea.
DR   HOGENOM; CLU_1072042_0_0_2; -.
DR   BioCyc; MetaCyc:HDREMBARK-MONOMER; -.
DR   BRENDA; 1.8.98.1; 3250.
DR   UniPathway; UPA00647; UER00700.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IDA:UniProtKB.
DR   GO; GO:0015948; P:methanogenesis; IDA:UniProtKB.
DR   Gene3D; 1.20.950.20; Transmembrane di-heme cytochromes, Chain C; 1.
DR   InterPro; IPR064030; HdrE.
DR   InterPro; IPR036197; NarG-like_sf.
DR   Pfam; PF30025; HdrE; 1.
DR   SUPFAM; SSF103501; Respiratory nitrate reductase 1 gamma chain; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Heme; Iron; Membrane;
KW   Metal-binding; Methanogenesis; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..263
FT                   /note="Dihydromethanophenazine:CoB--CoM heterodisulfide
FT                   reductase subunit E"
FT                   /id="PRO_0000150083"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        1..2
FT                   /note="MS -> K (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   263 AA;  29734 MW;  8202887145462E08 CRC64;
     MSEEMLYFSG LSDVLRMTFV QIMIFSTIAI VIFLYGLISN FQKWGTGVTG YALEPQEGKK
     GSAITFLKTW WSQVTAESHH RGESILEILI LDILFQRRIL KRSPFRWVMH LFIFGGWMTL
     FALSGMMFAV EMTEKIGIAL PFTPAEFRDF LSIPNYIFGY ILLIGVLVAL VRRLFVSEVR
     EASIMYDWVL IGIVFLVTIS GFIADGIRTG FIWSFGLDPS VAPPAALFHS IFSLLFCIAF
     IPYSKYIHII AIPLALLANK GGE
//