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Database: UniProt
Entry: Q6LY39
LinkDB: Q6LY39
Original site: Q6LY39 
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   16-JAN-2019, entry version 82.
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;
OC   Methanococcales; 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.,
RA   Hackett M., Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J.,
RA   Major T.A., Moore B.C., Porat I., Palmeiri A., Rouse G.,
RA   Saenphimmachak C., Soell D., Van Dien S., Wang T., Whitman W.B.,
RA   Xia Q., Zhang Y., Larimer F.W., Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable
RT   hydrogenotrophic 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
CC       reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme
CC       M) and H-S-CoB (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;
CC         EC=1.8.98.5; 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
CC         + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:55752,
CC         Rhea:RHEA-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;
CC         EC=1.8.98.6; Evidence={ECO:0000269|PubMed:20534465,
CC         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-
CC       ProRule:PRU00711};
CC   -!- PATHWAY: Cofactor metabolism; coenzyme M-coenzyme B
CC       heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme
CC       M-coenzyme B heterodisulfide: step 1/1. {ECO:0000305}.
CC   -!- SUBUNIT: The heterodisulfide reductase is composed of three
CC       subunits; HdrA, HdrB and HdrC. B1 and B2 subunits are
CC       interchangeable, as are the C1 and C2 subunits. The
CC       heterodisulfide reductase forms a supercomplex with
CC       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}.
DR   EMBL; BX950229; CAF30710.1; -; Genomic_DNA.
DR   RefSeq; WP_011171098.1; NC_005791.1.
DR   ProteinModelPortal; Q6LY39; -.
DR   STRING; 267377.MMP1154; -.
DR   EnsemblBacteria; CAF30710; CAF30710; MMP1154.
DR   GeneID; 37875745; -.
DR   KEGG; mmp:MMP1154; -.
DR   PATRIC; fig|267377.15.peg.1187; -.
DR   eggNOG; arCOG00964; Archaea.
DR   eggNOG; COG1150; LUCA.
DR   HOGENOM; HOG000237015; -.
DR   KO; K03390; -.
DR   OMA; WLCTTCY; -.
DR   OrthoDB; 102216at2157; -.
DR   BioCyc; MetaCyc:MONOMER-20167; -.
DR   BioCyc; MMAR267377:MMP_RS05955-MONOMER; -.
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:0051186; P:cofactor metabolic process; IEA:InterPro.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   Gene3D; 3.40.50.2030; -; 2.
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   InterPro; IPR016099; Prismane-like_a/b-sand.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   TIGRFAMs; TIGR03290; CoB_CoM_SS_C; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding;
KW   Methanogenesis; Oxidoreductase; Reference proteome.
FT   CHAIN         1    192       H(2)/formate:CoB-CoM
FT                                heterodisulfide,ferredoxin reductase
FT                                subunit C1.
FT                                /FTId=PRO_0000443939.
FT   DOMAIN       25     54       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        34     34       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        37     37       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        40     40       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        44     44       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        77     77       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        80     80       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        83     83       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        87     87       Iron-sulfur 1 (4Fe-4S).
FT                                {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
//
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