HDRC2_METMP
ID HDRC2_METMP Reviewed; 184 AA.
AC Q6LYD7;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=H(2)/formate:CoB-CoM heterodisulfide,ferredoxin reductase subunit C2 {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 C2 {ECO:0000305};
GN Name=hdrC2 {ECO:0000303|PubMed:20534465};
GN OrderedLocusNames=MMP1054 {ECO:0000312|EMBL:CAF30610.1};
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; CAF30610.1; -; Genomic_DNA.
DR RefSeq; WP_011170998.1; NC_005791.1.
DR AlphaFoldDB; Q6LYD7; -.
DR SMR; Q6LYD7; -.
DR STRING; 267377.MMP1054; -.
DR EnsemblBacteria; CAF30610; CAF30610; MMP1054.
DR GeneID; 2762781; -.
DR KEGG; mmp:MMP1054; -.
DR PATRIC; fig|267377.15.peg.1087; -.
DR eggNOG; arCOG00964; Archaea.
DR HOGENOM; CLU_121273_0_0_2; -.
DR OMA; AQKGNMA; -.
DR OrthoDB; 102216at2157; -.
DR BioCyc; MMAR267377:MMP_RS05450-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; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methanogenesis; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..184
FT /note="H(2)/formate:CoB-CoM heterodisulfide,ferredoxin
FT reductase subunit C2"
FT /id="PRO_0000443940"
FT DOMAIN 24..54
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 65..97
FT /note="4Fe-4S ferredoxin-type 2"
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 184 AA; 20452 MW; E431BCAC4DC02E14 CRC64;
MMKAEELNKG FVNEIIEAGT PVPGEKEVAS LKSCYQCGTC TGSCPSGRRT AYRTRKVIRQ
ALLGIDSVLD SDDIWKCTTC YTCYERCPRD VKVTEIIKTI RNLAAQKGNM AKPHKMTAVY
VLKAGHAVPA NDDTAKLRKS IGLAEKAPIA QFSQKDMDEL RTLAKNLKFD ELIGFDWKTM
GLKQ
