HDRB_METTM
ID HDRB_METTM Reviewed; 302 AA.
AC Q50755; D9PV04;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit B {ECO:0000305};
DE EC=1.8.98.5 {ECO:0000269|PubMed:21262829, ECO:0000305|PubMed:8119281};
DE AltName: Full=CoB--CoM heterodisulfide reductase subunit B {ECO:0000305};
GN Name=hdrB; OrderedLocusNames=MTBMA_c04500;
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 1-33.
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 1-27, 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, 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 -!- 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 HdrB family. {ECO:0000305}.
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DR EMBL; X81133; CAA57038.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL58051.1; -; Genomic_DNA.
DR PIR; S78509; S78509.
DR RefSeq; WP_013295277.1; NC_014408.1.
DR AlphaFoldDB; Q50755; -.
DR SMR; Q50755; -.
DR DIP; DIP-59607N; -.
DR IntAct; Q50755; 1.
DR STRING; 79929.MTBMA_c04500; -.
DR EnsemblBacteria; ADL58051; ADL58051; MTBMA_c04500.
DR GeneID; 9704156; -.
DR KEGG; mmg:MTBMA_c04500; -.
DR PATRIC; fig|79929.8.peg.440; -.
DR HOGENOM; CLU_052147_1_0_2; -.
DR OMA; PGCVAQG; -.
DR OrthoDB; 73750at2157; -.
DR BRENDA; 1.8.7.3; 7427.
DR BRENDA; 1.8.98.1; 7427.
DR BRENDA; 1.8.98.5; 7427.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000000345; Chromosome.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0015948; P:methanogenesis; IDA:UniProtKB.
DR InterPro; IPR017678; CoB/CoM_hetero-S_Rdtase_bsu.
DR InterPro; IPR004017; Cys_rich_dom.
DR Pfam; PF02754; CCG; 2.
DR TIGRFAMs; TIGR03288; CoB_CoM_SS_B; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Methanogenesis; Oxidoreductase.
FT CHAIN 1..302
FT /note="H(2):CoB-CoM heterodisulfide,ferredoxin reductase
FT subunit B"
FT /id="PRO_0000150070"
SQ SEQUENCE 302 AA; 33458 MW; 6D3FAC11C1969B64 CRC64;
MEIAYFLGCI MNNRYPGIEK ATRVLFDKLG IELKDMEGAS CCPAPGVFGS FDKTTWAAIA
ARNITIAEDM GADIMTECNG CFGSLFETNH LLKEDEEMKA KINEILKETG REYKGEVNVR
HFAEVLYNDV GLDKLSELVE KPLNLNVAVH YGCHFLKPSD EINIDNPERP TILDEIVEVT
GAKSVEYKDK MMCCGAGGGV RSRDLDVALD FTREKLTNMK EAGVDAIVNV CPFCHLQFDV
GQMEIKDKFG EEFDIPVLHL AQLLGLAMGL PKEDLVVDAH QVCVDECLEK LEELDRLAPG
SG
