HDRA_METMP
ID HDRA_METMP Reviewed; 658 AA.
AC Q6LWL2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=H(2)/formate:CoB-CoM heterodisulfide,ferredoxin reductase subunit A {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 A {ECO:0000305};
GN Name=hdrA; OrderedLocusNames=MMP1697;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC 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., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT 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 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: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; EC=1.8.98.5;
CC 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 + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:55752, Rhea:RHEA-
CC 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; EC=1.8.98.6;
CC Evidence={ECO:0000269|PubMed:20534465, 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 4 [4Fe-4S] clusters per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00711};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q8TM02};
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. B1 and B2 subunits are interchangeable, as are the
CC C1 and C2 subunits. The heterodisulfide reductase forms a supercomplex
CC with 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 HdrA family. {ECO:0000305}.
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DR EMBL; BX950229; CAF31253.1; -; Genomic_DNA.
DR STRING; 267377.MMP1697; -.
DR KEGG; mmp:MMP1697; -.
DR PATRIC; fig|267377.15.peg.1739; -.
DR eggNOG; arCOG02235; Archaea.
DR HOGENOM; CLU_020302_0_0_2; -.
DR OMA; CPSGAMQ; -.
DR BioCyc; MetaCyc:MON-20165; -.
DR BioCyc; MMAR267377:MMP_RS08740-MON; -.
DR BRENDA; 1.8.98.1; 3262.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
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; PF12838; Fer4_7; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 3.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
PE 1: Evidence at protein level;
KW 4Fe-4S; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW Methanogenesis; Oxidoreductase; Reference proteome; Repeat; Selenocysteine.
FT CHAIN 1..658
FT /note="H(2)/formate:CoB-CoM heterodisulfide,ferredoxin
FT reductase subunit A"
FT /id="PRO_0000318646"
FT DOMAIN 236..267
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 284..313
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 575..604
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 607..637
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 150..173
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 246
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 249
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 252
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 256
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 293
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 296
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 299
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 303
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 584
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 587
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 590
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="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 617
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 627
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT NON_STD 197
FT /note="Selenocysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 658 AA; 71281 MW; 0218716DA82E3866 CRC64;
MSDPKVGVFV CYCGANINGA VDCEAVKDFA SELDGVAVAA TYPFMCADPG QGLIKDAIKE
HGLDRIVVAA CTPKIHEPTF RGCLQDAGIS PYYLEFVNIR EHDAFVHMGD VEGATRKACE
MIAGGVERAK KLEDVPQKVV DVDKSCMVIG AGIAGIQSAL DLGDQGFKVY LVDKDESIGG
RMAQLAKTFP TDDCAMUILA PKMVSAANHP NIELITFAEI KNIDGYIGNF DVTLEKKPRY
VDEDTCTGCG ACAAACPIEV PNEFDLGLGT RKAIYVPFPQ AVPLLYTIDK EHCIDCGLCA
KVCCAEAVRY DQKPQELNIK VGTIITATGY DEFDATKKEE YGYGVYDNVI TTLEVERMIN
PAGPTHGHEI RPSDGKAPKR TVYIQCVGSR DEKVGNPYCS RVCCMFALKN AQLMKMHDPN
AEVYICYMDI RAFGKGYEEY YKRAQDQFGV KFIRGRPANI FEDPETKNLT VRVEDTLMGE
ILEIDADLVV LSAGLEAKKD AGELAKMLGI DRGPEGFFKE LHPKLAPVNT KVDGIAIAGV
AQGPKDIPDT VAQAKGAASA VAIPMSQGQF KIEMIRATVN EEVCGGCKVC ALMCPYNAIT
YEEKDGHLVA ITDDVACKGC GACAAACPSG AMQLRYYRDE QVIGMIDGIL NAAKMLEE
