HDRE_METMA
ID HDRE_METMA Reviewed; 259 AA.
AC Q8PVW4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Dihydromethanophenazine:CoB--CoM heterodisulfide reductase subunit E {ECO:0000305};
DE EC=1.8.98.1 {ECO:0000269|PubMed:9555882};
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=MM_1843;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=9555882; DOI=10.1128/jb.180.8.2027-2032.1998;
RA Abken H.J., Tietze M., Brodersen J., Baeumer S., Beifuss U.,
RA Deppenmeier U.;
RT "Isolation and characterization of methanophenazine and function of
RT phenazines in membrane-bound electron transport of Methanosarcina mazei
RT Goe1.";
RL J. Bacteriol. 180:2027-2032(1998).
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:0000269|PubMed:9555882}.
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:0000269|PubMed:9555882};
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:0000250|UniProtKB:P96796}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9555882};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Methanophenazine seems to mediate electron transfer from
CC F(420)H(2) dehydrogenase to the dihydromethanophenazine:CoB--CoM
CC heterodisulfide reductase. {ECO:0000305|PubMed:9555882}.
CC -!- SIMILARITY: Belongs to the HdrE family. {ECO:0000305}.
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DR EMBL; AE008384; AAM31539.1; -; Genomic_DNA.
DR RefSeq; WP_011033778.1; NC_003901.1.
DR AlphaFoldDB; Q8PVW4; -.
DR STRING; 192952.MM_1843; -.
DR EnsemblBacteria; AAM31539; AAM31539; MM_1843.
DR GeneID; 44088525; -.
DR GeneID; 66136680; -.
DR KEGG; mma:MM_1843; -.
DR PATRIC; fig|192952.21.peg.2128; -.
DR eggNOG; arCOG05014; Archaea.
DR HOGENOM; CLU_1072042_0_0_2; -.
DR OMA; KYIHVIA; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000000595; 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; IPR023234; NarG-like_domain.
DR InterPro; IPR036197; NarG-like_sf.
DR Pfam; PF02665; Nitrate_red_gam; 1.
DR SUPFAM; SSF103501; SSF103501; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Heme; Iron; Membrane; Metal-binding; Methanogenesis;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..259
FT /note="Dihydromethanophenazine:CoB--CoM heterodisulfide
FT reductase subunit E"
FT /id="PRO_0000150084"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 259 AA; 28989 MW; A328ADE9E99406F9 CRC64;
MAYFSGLSDA LRLTFVQIMI LSAIAVVIFL YGMIGNFQKW GAGVTGYALE PPTGKKGSAI
RFLKTWWAQV RAESHHHGKP ILEVLILDIF FQRRILKRSP IRWFMHFTIF AGWMSLFALS
GLMFAVEMTE KIGIELPFTP AEFREMLSLP NYIFGYILLI GVMIAVVRRL FVSEVREASI
MYDWVLLGGV FIVTISGFIA DGIRTGIIWG FGLDPVTAPP AALFHSVISL LFCIAYIPYS
KYIHVIATPL AILANKGGE
