ID   HDRE_METAC              Reviewed;         264 AA.
AC   Q8TSV8;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=MA_0687;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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:0000250|UniProtKB:A0A0E3NFS5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coenzyme B + coenzyme M + methanophenazine = coenzyme M-
CC         coenzyme B heterodisulfide + dihydromethanophenazine;
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:0000250|UniProtKB:A0A0E3NFS5}.
CC   -!- SUBUNIT: The dihydromethanophenazine:CoB--CoM heterodisulfide reductase
CC       is composed of two subunits; HdrD and HdrE.
CC       {ECO:0000250|UniProtKB:P96796}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the HdrE family. {ECO:0000305}.
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DR   EMBL; AE010299; AAM04127.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TSV8; -.
DR   STRING; 188937.MA_0687; -.
DR   EnsemblBacteria; AAM04127; AAM04127; MA_0687.
DR   KEGG; mac:MA_0687; -.
DR   HOGENOM; CLU_1072042_0_0_2; -.
DR   OMA; KYIHVIA; -.
DR   PhylomeDB; Q8TSV8; -.
DR   UniPathway; UPA00647; UER00700.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR036197; NarG-like_sf.
DR   SUPFAM; SSF103501; SSF103501; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Heme; Iron; Membrane; Metal-binding; Methanogenesis;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..264
FT                   /note="Dihydromethanophenazine:CoB--CoM heterodisulfide
FT                   reductase subunit E"
FT                   /id="PRO_0000150082"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   264 AA;  29527 MW;  EC385BA2219A5FC8 CRC64;
     MSSEMAYFSG LTDALRLTFV QIMILSTIAI VVFLYGMILN FQKWGAGVTG YALEPQAGSK
     GSAIRFLKTW WGQVVEESHH GHGKPILEVL ILDILFQRRI LKRSPLRWFM HFTIFAGWMT
     LFALSGLMFA VEMTEKFGIE LPFTPAEFRE FLSIPNYIFG YILLIGVLIA LVRRIVVSDV
     REASIMYDWI LIGGVFLVTI SGFVADGIRT GIIWGFGLDP TTAPPAALFH SVISLFFCIA
     YIPYSKYIHV IATPLAILAN KGGE