ID   HDRD_METBF              Reviewed;         409 AA.
AC   P96797; Q46C47; Q9UWK2;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   04-NOV-2026, entry version 156.
DE   RecName: Full=Dihydromethanophenazine:CoB--CoM heterodisulfide reductase subunit D {ECO:0000305};
DE            EC=1.8.98.1 {ECO:0000250|UniProtKB:A0A0E3NEE1};
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=Mbar_A1599;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, AND 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 2-20, 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). {ECO:0000305|PubMed:8174566, ECO:0000305|PubMed:9063468}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=methanophenazine + coenzyme B + coenzyme M =
CC         dihydromethanophenazine + coenzyme M-coenzyme B heterodisulfide;
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:A0A0E3NEE1};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00711,
CC         ECO:0000305|PubMed:9063468};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00711, ECO:0000305|PubMed:9063468};
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   -!- SIMILARITY: Belongs to the HdrD family. {ECO:0000305}.
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DR   EMBL; Y09870; CAA70997.1; -; Genomic_DNA.
DR   EMBL; CP000099; AAZ70545.1; -; Genomic_DNA.
DR   PIR; S43468; S43468.
DR   AlphaFoldDB; P96797; -.
DR   SMR; P96797; -.
DR   STRING; 269797.Mbar_A1599; -.
DR   TCDB; 3.D.7.1.1; the h2:heterodisulfide oxidoreductase (hho) family.
DR   PaxDb; 269797-Mbar_A1599; -.
DR   KEGG; mba:Mbar_A1599; -.
DR   eggNOG; arCOG00333; Archaea.
DR   HOGENOM; CLU_023081_2_0_2; -.
DR   OMA; AAGCGCM; -.
DR   OrthoDB; 42878at2157; -.
DR   BioCyc; MetaCyc:HDRDMBARK-MONOMER; -.
DR   UniPathway; UPA00647; UER00700.
DR   GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IDA:UniProtKB.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0015948; P:methanogenesis; IDA:UniProtKB.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR051278; HdrB/HdrD_reductase.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   PANTHER; PTHR42947; COB--COM HETERODISULFIDE REDUCTASE SUBUNIT B 1; 1.
DR   PANTHER; PTHR42947:SF1; COB--COM HETERODISULFIDE REDUCTASE SUBUNIT B 1; 1.
DR   Pfam; PF02754; CCG; 2.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW   Methanogenesis; Oxidoreductase; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8174566"
FT   CHAIN           2..409
FT                   /note="Dihydromethanophenazine:CoB--CoM heterodisulfide
FT                   reductase subunit D"
FT                   /id="PRO_0000150080"
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"
FT   CONFLICT        43..44
FT                   /note="KP -> HQ (in Ref. 1; CAA70997)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   409 AA;  45055 MW;  1AC01503AA1F5BDE CRC64;
     MAKRTPSIDT KNLTAVQLME LDACVRCGEC VKWCPTYAAS GGKPGLAPRD KILRWRQYMN
     KSYGLKAKLF GPQEVSPSEL EEFKDDVHGC TTCGVCATVC EAGINTVEIW EAIRTNLVKK
     GIGPYGKQSA FPKLVGQYHN PYMKDQKDRL AWVPPDVKIE DKADIVYFTG CTAGYNQLAL
     AFATSRVLNK LGIKFAMLGE EEWCCGSALI RTGQVHVDDV ARELARHNVE ALQKKGAKKV
     LFACAGCFRA AKIDWPRLLG KELPFEVIHI TQFLADLIQA DKIKWEKPIN KTITYHDPCH
     LGRHVGVFNA PRYVLSHIPG VKFVEMDRSK EFQRCCGAGG GVKAGMPDLA VAMGESRVKD
     ALETNADILS SACPFCKRNL SDGRDALKSD IVVEDIIELV AEALGLSTS
//