HDRE_METTT
ID HDRE_METTT Reviewed; 264 AA.
AC A0A0E3NFS5;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 2.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Dihydromethanophenazine:CoB--CoM heterodisulfide reductase subunit E {ECO:0000305};
DE EC=1.8.98.1 {ECO:0000269|PubMed:11034998, ECO:0000269|PubMed:9654152, ECO:0000305|PubMed:9665708};
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; ORFNames=MSTHT_2243 {ECO:0000312|EMBL:AKB14001.1};
OS Methanosarcina thermophila (strain ATCC 43570 / DSM 1825 / OCM 12 / VKM
OS B-1830 / TM-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=523844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / VKM B-1830 / TM-1;
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP SUBUNIT.
RC STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / VKM B-1830 / TM-1;
RX PubMed=9665708; DOI=10.1021/bi9726483;
RA Simianu M., Murakami E., Brewer J.M., Ragsdale S.W.;
RT "Purification and properties of the heme- and iron-sulfur-containing
RT heterodisulfide reductase from Methanosarcina thermophila.";
RL Biochemistry 37:10027-10039(1998).
RN [3]
RP FUNCTION, SOURCE OF ELECTRONS, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / VKM B-1830 / TM-1;
RX PubMed=9654152; DOI=10.1016/s0014-5793(98)00555-9;
RA Baeumer S., Murakami E., Brodersen J., Gottschalk G., Ragsdale S.W.,
RA Deppenmeier U.;
RT "The F420H2:heterodisulfide oxidoreductase system from Methanosarcina
RT species. 2-Hydroxyphenazine mediates electron transfer from F420H2
RT dehydrogenase to heterodisulfide reductase.";
RL FEBS Lett. 428:295-298(1998).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / VKM B-1830 / TM-1;
RX PubMed=11034998; DOI=10.1074/jbc.m004809200;
RA Murakami E., Deppenmeier U., Ragsdale S.W.;
RT "Characterization of the intramolecular electron transfer pathway from 2-
RT hydroxyphenazine to the heterodisulfide reductase from Methanosarcina
RT thermophila.";
RL J. Biol. Chem. 276:2432-2439(2001).
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 (PubMed:9654152, PubMed:9665708, PubMed:11034998). Electrons
CC probably transfer from phenazine to the high potential 4Fe cluster in
CC HdrD subunit, then to the low potential heme in HdrE subunit and
CC finally to CoM-S-S-CoB (PubMed:11034998). {ECO:0000269|PubMed:11034998,
CC ECO:0000269|PubMed:9654152, ECO:0000269|PubMed:9665708}.
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:11034998, ECO:0000269|PubMed:9654152,
CC ECO:0000305|PubMed:9665708};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:9665708};
CC Note=Binds 2 heme b (iron(II)-protoporphyrin IX) groups per subunit.
CC {ECO:0000269|PubMed:9665708};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=92 uM for reduced 2-hydroxyphenazine
CC {ECO:0000269|PubMed:11034998};
CC KM=144 uM for CoM-S-S-CoB {ECO:0000269|PubMed:11034998};
CC Note=kcat is 74 sec(-1) at 25 degrees Celsius.
CC {ECO:0000269|PubMed:11034998};
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|PubMed:11034998}.
CC -!- SUBUNIT: The dihydromethanophenazine:CoB--CoM heterodisulfide reductase
CC is composed of two subunits; HdrD and HdrE.
CC {ECO:0000269|PubMed:9665708}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC 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:9654152}.
CC -!- SIMILARITY: Belongs to the HdrE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AKB14001.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP009501; AKB14001.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A0A0E3NFS5; -.
DR STRING; 523844.MSTHT_2243; -.
DR EnsemblBacteria; AKB14001; AKB14001; MSTHT_2243.
DR KEGG; mthr:MSTHT_2243; -.
DR PATRIC; fig|523844.20.peg.2747; -.
DR HOGENOM; CLU_1072042_0_0_2; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000066529; 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; Direct protein sequencing; Heme; Iron; Membrane;
KW Metal-binding; Methanogenesis; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9665708"
FT CHAIN 2..264
FT /note="Dihydromethanophenazine:CoB--CoM heterodisulfide
FT reductase subunit E"
FT /id="PRO_0000443857"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 264 AA; 29753 MW; 1055ED85E35809FD CRC64;
MSEEMVYFSG LSDALRITFV QMMILSAIAI VIFLYGMIIT LQKWGSGATG YALEPQEGKR
GSAITFLKTW WKQVTEKSPH GHGKPILEIL ILDILFQRRI LKRSGLRWVM HILIFAGWMT
LFALSGLMFS VELTHMIGIE LPFTPHMFRE WLSIPNYIFG YILLIGVLIA IVRRLFVSEV
REASIMYDWV LIGVVFLVTI SGFLADGIRT GLIWDFGLDP SLAPPAALFH SVISLLFCIA
FIPYSKYIHI IAIPLALLAN KGGE
