HDRA_METTM
ID HDRA_METTM Reviewed; 659 AA.
AC Q50756; D9PYN8; Q50752;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit A {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 A {ECO:0000305};
GN Name=hdrA; OrderedLocusNames=MTBMA_c17680;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-18; 210-226;
RP 425-435; 455-459 AND 641-650.
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 651-659.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=8617278; DOI=10.1111/j.1432-1033.1996.00294.x;
RA Vaupel M., Dietz H., Linder D., Thauer R.K.;
RT "Primary structure of cyclohydrolase (Mch) from Methanobacterium
RT thermoautotrophicum (strain Marburg) and functional expression of the mch
RT gene in Escherichia coli.";
RL Eur. J. Biochem. 236:294-300(1996).
RN [4]
RP PROTEIN SEQUENCE OF 2-18, 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 [5] {ECO:0000305}
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 [6]
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 [7]
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 4 [4Fe-4S] clusters per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00711, ECO:0000305|PubMed:2121478};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={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 HdrA family. {ECO:0000305}.
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DR EMBL; X81134; CAA57039.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL59336.1; -; Genomic_DNA.
DR EMBL; X92083; CAA63065.1; -; Genomic_DNA.
DR PIR; S48720; S48720.
DR RefSeq; WP_013296546.1; NC_014408.1.
DR AlphaFoldDB; Q50756; -.
DR SMR; Q50756; -.
DR DIP; DIP-59606N; -.
DR IntAct; Q50756; 5.
DR STRING; 79929.MTBMA_c17680; -.
DR EnsemblBacteria; ADL59336; ADL59336; MTBMA_c17680.
DR GeneID; 9705479; -.
DR KEGG; mmg:MTBMA_c17680; -.
DR PATRIC; fig|79929.8.peg.1705; -.
DR HOGENOM; CLU_020302_0_0_2; -.
DR OMA; TAKHAML; -.
DR OrthoDB; 1148at2157; -.
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; 3.50.50.60; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR039650; HdrA-like.
DR PANTHER; PTHR43498; PTHR43498; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF13237; Fer4_10; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 4.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; FAD; Flavoprotein; Iron; Iron-sulfur;
KW Metal-binding; Methanogenesis; Oxidoreductase; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7925445,
FT ECO:0000269|PubMed:8119281"
FT CHAIN 2..659
FT /note="H(2):CoB-CoM heterodisulfide,ferredoxin reductase
FT subunit A"
FT /id="PRO_0000150062"
FT DOMAIN 244..274
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 292..321
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 581..610
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 611..640
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 158..181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 254
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 257
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 260
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 264
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 301
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 304
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 307
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 311
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 591
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 594
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 597
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 601
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 620
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 623
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 626
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 630
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 659 AA; 72182 MW; FC01196FEE3A5F9E CRC64;
MAEEKKETME EPKIGVYVCH CGVNIGGVVD VEAVRDYAAK LPNVVIAKDY KYYCSDPGQL
EIQKDIKELG INRVVVAACS PRLHEPTFRR CVEEAGLNQF LFEFANIREH DSWVHMDNPE
GATEKAKDLV RMAVAKARLL EPLEASKVSV DDKALVIGGG VAGIQAALDL ADMGFKTYMV
EKRPSISGRM GQLDKTFPTL DCSMCILAPK MVDVGKHDNI ELITYAEVKE VDGYIGNFKV
KIEKKPRYID EELCTGCGSC VEVCPIEMPN YFDEGIGMTK AVYIPFPQAV PLCATIDKDY
CIECMLCDEV CERGAVKHDQ EPEEIEIEVG TIIVATGYDA YDPTEKLEYG YGRHTNVITG
LELERMINAS GPTDGKVLKP SDGEKPKRVA FIHCVGSRDE QIGKPYCSRV CCMYIMKNAQ
LIKDKMPDTE VTLYYMDIRA FGKGFEEFYK RSQEKYGIKF IRGRPAEVIE NPDLTLTVRS
EDTLLGKVTE YDYDMVVLGV GLVPPEGAET LRQTIGLSKS ADGFLMEAHP KLRPVDTLTD
GVYLAGVAQG PKDIPDAVAQ ASGAAARAAI PMVKGEVEIE PIIAVTDSDV CGGCEVCIEL
CPFGAISIEE GHANVNVALC KGCGTCVAAC PSGAMDQQHF KTEQIMAQIE AALNEPASK
