HDRE_METBF
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 03-AUG-2022, entry version 125.
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; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC 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=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: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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 EnsemblBacteria; AAZ70544; AAZ70544; Mbar_A1598.
DR KEGG; mba:Mbar_A1598; -.
DR eggNOG; arCOG05014; Archaea.
DR HOGENOM; CLU_1072042_0_0_2; -.
DR BioCyc; MetaCyc:HDREMBARK-MON; -.
DR BRENDA; 1.8.98.1; 3250.
DR UniPathway; UPA00647; UER00700.
DR GO; GO:0016021; C:integral component of 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015948; P:methanogenesis; IDA:UniProtKB.
DR InterPro; IPR036197; NarG-like_sf.
DR SUPFAM; SSF103501; SSF103501; 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
