HDRC1_METMP
ID HDRC1_METMP Reviewed; 192 AA.
AC Q6LY39;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=H(2)/formate:CoB-CoM heterodisulfide,ferredoxin reductase subunit C1 {ECO:0000305};
DE EC=1.8.98.5 {ECO:0000269|PubMed:24039260};
DE EC=1.8.98.6 {ECO:0000269|PubMed:20534465, ECO:0000269|PubMed:24039260};
DE AltName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit C1 {ECO:0000305};
GN Name=hdrC1 {ECO:0000303|PubMed:20534465};
GN OrderedLocusNames=MMP1154 {ECO:0000312|EMBL:CAF30710.1};
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=S2 / LL;
RX PubMed=20534465; DOI=10.1073/pnas.1003653107;
RA Costa K.C., Wong P.M., Wang T., Lie T.J., Dodsworth J.A., Swanson I.,
RA Burn J.A., Hackett M., Leigh J.A.;
RT "Protein complexing in a methanogen suggests electron bifurcation and
RT electron delivery from formate to heterodisulfide reductase.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11050-11055(2010).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=S2 / LL;
RX PubMed=24039260; DOI=10.1128/jb.00895-13;
RA Costa K.C., Lie T.J., Xia Q., Leigh J.A.;
RT "VhuD facilitates electron flow from H2 or formate to heterodisulfide
RT reductase in Methanococcus maripaludis.";
RL J. Bacteriol. 195:5160-5165(2013).
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:20534465,
CC ECO:0000269|PubMed:24039260}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coenzyme B + coenzyme M + 2 H(+) + 2 reduced [2Fe-2S]-
CC [ferredoxin] = coenzyme M-coenzyme B heterodisulfide + 2 H2 + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:55748, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18276, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:58319, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=1.8.98.5;
CC Evidence={ECO:0000269|PubMed:24039260};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 CO2 + coenzyme B + coenzyme M + 2 reduced [2Fe-2S]-
CC [ferredoxin] = coenzyme M-coenzyme B heterodisulfide + 2 formate + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:55752, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:58319, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=1.8.98.6;
CC Evidence={ECO:0000269|PubMed:20534465, ECO:0000269|PubMed:24039260};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC Note=Binds 2 [4Fe-4S] cluster. {ECO:0000255|PROSITE-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 heterodisulfide reductase is composed of three subunits;
CC HdrA, HdrB and HdrC. B1 and B2 subunits are interchangeable, as are the
CC C1 and C2 subunits. The heterodisulfide reductase forms a supercomplex
CC with formylmethanofuran dehydrogenase (Fwd), F(420)-non-reducing
CC hydrogenase (Vhu) and formate dehydrogenase (Fdh).
CC {ECO:0000269|PubMed:20534465, ECO:0000269|PubMed:24039260}.
CC -!- SIMILARITY: Belongs to the HdrC family. {ECO:0000305}.
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DR EMBL; BX950229; CAF30710.1; -; Genomic_DNA.
DR RefSeq; WP_011171098.1; NC_005791.1.
DR AlphaFoldDB; Q6LY39; -.
DR SMR; Q6LY39; -.
DR STRING; 267377.MMP1154; -.
DR EnsemblBacteria; CAF30710; CAF30710; MMP1154.
DR GeneID; 41279737; -.
DR KEGG; mmp:MMP1154; -.
DR PATRIC; fig|267377.15.peg.1187; -.
DR eggNOG; arCOG00964; Archaea.
DR HOGENOM; CLU_121273_0_0_2; -.
DR OMA; DPDLWLC; -.
DR OrthoDB; 102216at2157; -.
DR BioCyc; MetaCyc:MON-20167; -.
DR BioCyc; MMAR267377:MMP_RS05955-MON; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000000590; Chromosome.
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:InterPro.
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; IPR017680; CoB/CoM_hetero-S_Rdtase_csu.
DR InterPro; IPR009051; Helical_ferredxn.
DR Pfam; PF13183; Fer4_8; 1.
DR TIGRFAMs; TIGR03290; CoB_CoM_SS_C; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methanogenesis; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..192
FT /note="H(2)/formate:CoB-CoM heterodisulfide,ferredoxin
FT reductase subunit C1"
FT /id="PRO_0000443939"
FT DOMAIN 25..54
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 34
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 37
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 40
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 44
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 77
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 80
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 87
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 192 AA; 21600 MW; B94538648DF69B33 CRC64;
MVLKSSEFNP DFPKQIIESG EWIFGDHASS FQKCYQCGTC TGACPSGRIT ALRTRKLIRS
ALAGIDSILS GDDLWMCTTC YECYEKCPRE VKITDIIKII RNIAAEKGYI AEPHRKTSLL
VFKTGHAVPV NDEIKKARLA IGLTEIPPTT HKYPEALEIV RDIMEDLNFC KKVGICRETM
DLEPLNVQKS EE
