HDRC2_METAC
ID HDRC2_METAC Reviewed; 161 AA.
AC Q8TIB9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ferredoxin/F(420)H(2)-dependent CoB-CoM heterodisulfide reductase subunit C {ECO:0000305};
DE EC=1.8.7.3 {ECO:0000269|PubMed:28174314};
DE EC=1.8.98.4 {ECO:0000269|PubMed:28174314};
DE AltName: Full=Coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase subunit C {ECO:0000305};
DE AltName: Full=Ferredoxin:CoB-CoM heterodisulfide reductase subunit C {ECO:0000305};
GN Name=hdrC2 {ECO:0000303|PubMed:28174314}; OrderedLocusNames=MA_4236;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=28174314; DOI=10.1128/mbio.02285-16;
RA Yan Z., Wang M., Ferry J.G.;
RT "A ferredoxin- and F420H2-dependent, electron-bifurcating, heterodisulfide
RT reductase with homologs in the domains Bacteria and Archaea.";
RL MBio 8:E02285-E02285(2017).
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). Catalyzes the transfer of electrons from ferredoxin to
CC CoM-S-S-CoB during methanogenesis from acetate. Electrons transfer from
CC ferredoxin to CoM-S-S-CoB via HdrA2, HdrC2 and HdrB2. In addition, the
CC complex can use electron bifurcation to direct electron pairs from
CC reduced coenzyme F420 towards the reduction of both ferredoxin and CoB-
CC CoM heterodisulfide. This activity may take place during Fe(III)-
CC dependent anaerobic methane oxidation. {ECO:0000269|PubMed:28174314}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coenzyme B + coenzyme M + 2 oxidized [2Fe-2S]-[ferredoxin] =
CC coenzyme M-coenzyme B heterodisulfide + 2 H(+) + 2 reduced [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:55160, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:58319, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=1.8.7.3;
CC Evidence={ECO:0000269|PubMed:28174314};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coenzyme B + coenzyme M + 4 H(+) + 2 oxidized coenzyme F420-
CC (gamma-L-Glu)(n) + 2 reduced [2Fe-2S]-[ferredoxin] = coenzyme M-
CC coenzyme B heterodisulfide + 2 oxidized [2Fe-2S]-[ferredoxin] + 2
CC reduced coenzyme F420-(gamma-L-Glu)(n); Xref=Rhea:RHEA:55744,
CC Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:12939,
CC Rhea:RHEA-COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:58319, ChEBI:CHEBI:58411,
CC ChEBI:CHEBI:58596, ChEBI:CHEBI:133980, ChEBI:CHEBI:139511;
CC EC=1.8.98.4; Evidence={ECO:0000269|PubMed:28174314};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711,
CC ECO:0000269|PubMed:28174314};
CC Note=Binds 2 [4Fe-4S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00711,
CC ECO:0000269|PubMed:28174314};
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 ferredoxin/F(420)H(2)-dependent CoB-CoM heterodisulfide
CC reductase is composed of three subunits; HdrA2, HdrB2 and HdrC2.
CC {ECO:0000269|PubMed:28174314}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28174314}.
CC -!- SIMILARITY: Belongs to the HdrC family. {ECO:0000305}.
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DR EMBL; AE010299; AAM07581.1; -; Genomic_DNA.
DR RefSeq; WP_011024118.1; NC_003552.1.
DR AlphaFoldDB; Q8TIB9; -.
DR SMR; Q8TIB9; -.
DR STRING; 188937.MA_4236; -.
DR EnsemblBacteria; AAM07581; AAM07581; MA_4236.
DR GeneID; 1476130; -.
DR KEGG; mac:MA_4236; -.
DR HOGENOM; CLU_121273_0_0_2; -.
DR InParanoid; Q8TIB9; -.
DR OMA; DPDLWLC; -.
DR OrthoDB; 102216at2157; -.
DR PhylomeDB; Q8TIB9; -.
DR BioCyc; MetaCyc:MON-20161; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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: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; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Methanogenesis;
KW Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..161
FT /note="Ferredoxin/F(420)H(2)-dependent CoB-CoM
FT heterodisulfide reductase subunit C"
FT /id="PRO_0000150072"
FT DOMAIN 10..40
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 51..82
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 29
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 65
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 68
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 72
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 161 AA; 18150 MW; 3D0339845B0DD95C CRC64;
MSEELLKLLK AEGLDLLSCM HCGICTGSCP SGRHTGLNTR RIIRDARKNR AAVLSDYDLW
LCTTCYTCQE RCPRGIPITD AILELRRLAV REGLMLPEHR FVSEMVLECG HAVPLDEETK
KKREELGLDP IPETVQKDPE ALEGLKTLLK TCKFDELVAK K
