HDRC_METTM
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 03-AUG-2022, entry version 119.
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 thermoautotrophicum
RT contains sequence motifs characteristic of pyridine-nucleotide-dependent
RT 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., Seedorf H.,
RA 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 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:2121478, ECO:0000269|PubMed:21262829,
CC 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; EC=1.8.98.5;
CC Evidence={ECO:0000269|PubMed:21262829, 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 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. It forms a complex with the F420-non-reducing
CC hydrogenase (Mvh), which provides the reducing equivalents to the
CC heterodisulfide reductase. {ECO:0000269|PubMed:12856108,
CC ECO:0000269|PubMed:2121478, ECO:0000269|PubMed:21262829,
CC ECO:0000269|PubMed:8119281}.
CC -!- SIMILARITY: Belongs to the HdrC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; Q50754; -.
DR SMR; Q50754; -.
DR DIP; DIP-59608N; -.
DR IntAct; Q50754; 1.
DR STRING; 79929.MTBMA_c04490; -.
DR EnsemblBacteria; ADL58050; ADL58050; MTBMA_c04490.
DR GeneID; 9704155; -.
DR KEGG; mmg:MTBMA_c04490; -.
DR PATRIC; fig|79929.8.peg.439; -.
DR HOGENOM; CLU_121273_0_0_2; -.
DR OMA; DPDLWLC; -.
DR OrthoDB; 102216at2157; -.
DR BRENDA; 1.8.98.5; 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:0015948; P:methanogenesis; IDA: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 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; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW Methanogenesis; Oxidoreductase; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7925445,
FT ECO:0000269|PubMed:8119281"
FT CHAIN 2..185
FT /note="H(2):CoB-CoM heterodisulfide,ferredoxin reductase
FT subunit C"
FT /id="PRO_0000150078"
FT DOMAIN 25..55
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 68..99
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 35
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 38
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 41
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 79
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 82
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT CONFLICT 84
FT /note="S -> Y (in Ref. 1; CAA57037)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="V -> L (in Ref. 1; CAA57037)"
FT /evidence="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
