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Database: UniProt
Entry: Q6LWL2
LinkDB: Q6LWL2
Original site: Q6LWL2 
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   16-JAN-2019, entry version 101.
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;
OC   Methanococcales; 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.,
RA   Hackett M., Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J.,
RA   Major T.A., Moore B.C., Porat I., Palmeiri A., Rouse G.,
RA   Saenphimmachak C., Soell D., Van Dien S., Wang T., Whitman W.B.,
RA   Xia Q., Zhang Y., Larimer F.W., Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable
RT   hydrogenotrophic 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
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: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;
CC         EC=1.8.98.5; 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
CC         + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:55752,
CC         Rhea:RHEA-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;
CC         EC=1.8.98.6; Evidence={ECO:0000269|PubMed:20534465,
CC         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
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. B1 and B2 subunits are
CC       interchangeable, as are the C1 and C2 subunits. The
CC       heterodisulfide reductase forms a supercomplex with
CC       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}.
DR   EMBL; BX950229; CAF31253.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q6LWL2; -.
DR   STRING; 267377.MMP1697; -.
DR   PRIDE; Q6LWL2; -.
DR   EnsemblBacteria; CAF31253; CAF31253; MMP1697.
DR   KEGG; mmp:MMP1697; -.
DR   PATRIC; fig|267377.15.peg.1739; -.
DR   eggNOG; arCOG02235; Archaea.
DR   eggNOG; COG1148; LUCA.
DR   HOGENOM; HOG000230698; -.
DR   KO; K03388; -.
DR   OMA; CTPKIHE; -.
DR   BioCyc; MetaCyc:MONOMER-20165; -.
DR   BioCyc; MMAR267377:MMP_RS08740-MONOMER; -.
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; Complete proteome; FAD; Flavoprotein; Iron; Iron-sulfur;
KW   Metal-binding; Methanogenesis; Oxidoreductase; Reference proteome;
KW   Repeat; Selenocysteine.
FT   CHAIN         1    658       H(2)/formate:CoB-CoM
FT                                heterodisulfide,ferredoxin reductase
FT                                subunit A.
FT                                /FTId=PRO_0000318646.
FT   DOMAIN      236    267       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      284    313       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      575    604       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      607    637       4Fe-4S ferredoxin-type 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   NP_BIND     150    173       FAD. {ECO:0000255}.
FT   METAL       246    246       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       249    249       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       252    252       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       256    256       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       293    293       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       296    296       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       299    299       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       303    303       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       584    584       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       587    587       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       590    590       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       594    594       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       617    617       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       620    620       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       623    623       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       627    627       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   NON_STD     197    197       Selenocysteine. {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
//
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