HDRD_METMA
ID HDRD_METMA Reviewed; 409 AA.
AC Q8PVW3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Dihydromethanophenazine:CoB--CoM heterodisulfide reductase subunit D {ECO:0000305};
DE EC=1.8.98.1 {ECO:0000269|PubMed:9555882};
DE AltName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit D {ECO:0000305};
DE AltName: Full=Coenzyme B:coenzyme M:methanophenazine oxidoreductase subunit D {ECO:0000305};
GN Name=hdrD; OrderedLocusNames=MM_1844;
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). {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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00711};
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:P96797}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9555882}.
CC Note=Membrane-bound. {ECO:0000269|PubMed:9555882}.
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 HdrD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM31540.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008384; AAM31540.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048045886.1; NC_003901.1.
DR AlphaFoldDB; Q8PVW3; -.
DR SMR; Q8PVW3; -.
DR STRING; 192952.MM_1844; -.
DR EnsemblBacteria; AAM31540; AAM31540; MM_1844.
DR GeneID; 24840594; -.
DR KEGG; mma:MM_1844; -.
DR PATRIC; fig|192952.21.peg.2129; -.
DR eggNOG; arCOG00333; Archaea.
DR HOGENOM; CLU_023081_2_0_2; -.
DR OMA; FQRCCGA; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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 Gene3D; 1.10.1060.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004017; Cys_rich_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR Pfam; PF02754; CCG; 2.
DR Pfam; PF13183; Fer4_8; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Methanogenesis; Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..409
FT /note="Dihydromethanophenazine:CoB--CoM heterodisulfide
FT reductase subunit D"
FT /id="PRO_0000150081"
FT DOMAIN 14..44
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 81..110
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 24
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 27
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 30
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 34
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 90
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 93
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 96
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 100
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 409 AA; 45377 MW; F74FA592197FAC46 CRC64;
MAKKTPSIDT KNLTAVQLME LDSCTRCGEC VKWCPTYAAS GQKPGLAPRD KILRWRQFMN
KSYGIKAKLF GPTEIPQSEL EEFKDDVHGC TTCGICATVC ESGINTVELW EALRTNLVKK
GIGPFGKQNM FPKLIGQYHN PYMKDQKDRL NWVPPDVKIE DKADVVYFTG CTAGYNQLAL
AFATARVLNK LGVKFSMLGE EEWCCGSALI RTGQVHVDDV PRELARHNVE ALKKKGAKKV
LYACAGCFRA SKVDWPRLLG EELPFEVVHV AEFLADLIKQ DKIKWEKSIN KTVTYHDPCH
LGRHVGVFDA PRYVLSHIPG VKFVEMDRVK EFQRCCGAGG GVKAGIPDLA LGVAESRVKD
AVATDADILS SCCPFCKRNL MDGRDSLKVD MVVEDVIELV AEALGLETK
