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Database: UniProt
Entry: Q50754
LinkDB: Q50754
Original site: Q50754 
ID   HDRC_METTM              Reviewed;         185 AA.
AC   Q50754; D9PV03;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 6.
DT   10-APR-2019, entry version 107.
DE   RecName: Full=H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit C {ECO:0000305};
DE            EC=1.8.98.5 {ECO:0000269|PubMed:21262829, ECO:0000305|PubMed:8119281};
DE   AltName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit C {ECO:0000305};
GN   Name=hdrC; OrderedLocusNames=MTBMA_c04490;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-25.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=7925445; DOI=10.1111/j.1432-1033.1994.00253.x;
RA   Hedderich R., Koch J., Linder D., Thauer R.K.;
RT   "The heterodisulfide reductase from Methanobacterium
RT   thermoautotrophicum contains sequence motifs characteristic of
RT   pyridine-nucleotide-dependent thioredoxin reductases.";
RL   Eur. J. Biochem. 225:253-261(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/JB.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A.,
RA   Seedorf H., Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-25, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP   ASSOCIATION WITH F420-NON-REDUCING HYDROGENASE.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=8119281; DOI=10.1111/j.1432-1033.1994.tb18608.x;
RA   Setzke E., Hedderich R., Heiden S., Thauer R.K.;
RT   "H2: heterodisulfide oxidoreductase complex from Methanobacterium
RT   thermoautotrophicum. Composition and properties.";
RL   Eur. J. Biochem. 220:139-148(1994).
RN   [4]
RP   FUNCTION, COFACTOR, AND SUBUNIT.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=2121478; DOI=10.1111/j.1432-1033.1990.tb19331.x;
RA   Hedderich R., Berkessel A., Thauer R.K.;
RT   "Purification and properties of heterodisulfide reductase from
RT   Methanobacterium thermoautotrophicum (strain Marburg).";
RL   Eur. J. Biochem. 193:255-261(1990).
RN   [5]
RP   ASSOCIATION WITH F420-NON-REDUCING HYDROGENASE.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=12856108; DOI=10.1007/s00203-003-0577-9;
RA   Stojanowic A., Mander G.J., Duin E.C., Hedderich R.;
RT   "Physiological role of the F420-non-reducing hydrogenase (Mvh) from
RT   Methanothermobacter marburgensis.";
RL   Arch. Microbiol. 180:194-203(2003).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=21262829; DOI=10.1073/pnas.1016761108;
RA   Kaster A.K., Moll J., Parey K., Thauer R.K.;
RT   "Coupling of ferredoxin and heterodisulfide reduction via electron
RT   bifurcation in hydrogenotrophic methanogenic archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2981-2986(2011).
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:2121478,
CC       ECO:0000269|PubMed:21262829, ECO:0000269|PubMed:8119281}.
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:21262829,
CC         ECO:0000305|PubMed:8119281};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00711,
CC         ECO:0000305|PubMed:2121478};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00711, ECO:0000305|PubMed:2121478};
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. It forms a complex with the F420-
CC       non-reducing hydrogenase (Mvh), which provides the reducing
CC       equivalents to the heterodisulfide reductase.
CC       {ECO:0000269|PubMed:12856108, ECO:0000269|PubMed:2121478,
CC       ECO:0000269|PubMed:21262829, ECO:0000269|PubMed:8119281}.
CC   -!- SIMILARITY: Belongs to the HdrC family. {ECO:0000305}.
DR   EMBL; X81133; CAA57037.1; -; Genomic_DNA.
DR   EMBL; CP001710; ADL58050.1; -; Genomic_DNA.
DR   PIR; S78508; S78508.
DR   RefSeq; WP_013295276.1; NC_014408.1.
DR   SMR; Q50754; -.
DR   DIP; DIP-59608N; -.
DR   IntAct; Q50754; 1.
DR   EnsemblBacteria; ADL58050; ADL58050; MTBMA_c04490.
DR   GeneID; 9704155; -.
DR   KEGG; mmg:MTBMA_c04490; -.
DR   PATRIC; fig|79929.8.peg.439; -.
DR   eggNOG; arCOG00964; Archaea.
DR   eggNOG; COG1150; LUCA.
DR   HOGENOM; HOG000237015; -.
DR   KO; K03390; -.
DR   OMA; WLCTTCY; -.
DR   OrthoDB; 102216at2157; -.
DR   BioCyc; MMAR79929:G1GML-447-MONOMER; -.
DR   BRENDA; 1.8.98.1; 7427.
DR   UniPathway; UPA00647; UER00700.
DR   Proteomes; UP000000345; 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; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; NAS:UniProtKB.
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   SUPFAM; SSF46548; SSF46548; 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; Complete proteome; Direct protein sequencing; Iron;
KW   Iron-sulfur; Metal-binding; Methanogenesis; Oxidoreductase; Repeat.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:7925445,
FT                                ECO:0000269|PubMed:8119281}.
FT   CHAIN         2    185       H(2):CoB-CoM heterodisulfide,ferredoxin
FT                                reductase subunit C.
FT                                /FTId=PRO_0000150078.
FT   DOMAIN       25     55       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       68     99       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        35     35       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        38     38       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        41     41       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        45     45       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        79     79       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        82     82       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        85     85       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        89     89       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   CONFLICT     84     84       S -> Y (in Ref. 1; CAA57037).
FT                                {ECO:0000305}.
FT   CONFLICT    119    119       V -> L (in Ref. 1; CAA57037).
FT                                {ECO:0000305}.
SQ   SEQUENCE   185 AA;  20520 MW;  7DD936AFA7537588 CRC64;
     MTLLQREENI IRKGNIDKEF SEKIKAAGGD SLEYCFQCGT CTGSCPSGRR TPYRVRQIIR
     KANVGLKDEI ISDPTLWMCT TCYSCQERCP RKVKIVDVVK LARNEAAKAG FMAPAHKAVG
     SFVIKTGHGV PINDATMELR KAVGLGELPP TTHQFPEALE EVQKIIKATG FDQLIGYNWE
     TGELE
//
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