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Database: UniProt
Entry: Q8TSV7
LinkDB: Q8TSV7
Original site: Q8TSV7 
ID   HDRD_METAC              Reviewed;         409 AA.
AC   Q8TSV7;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   10-APR-2019, entry version 103.
DE   RecName: Full=Dihydromethanophenazine:CoB--CoM heterodisulfide reductase subunit D {ECO:0000250|UniProtKB:A0A0E3NEE1};
DE            EC=1.8.98.1 {ECO:0000250|UniProtKB:A0A0E3NEE1};
DE   AltName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit D {ECO:0000250|UniProtKB:A0A0E3NEE1};
DE   AltName: Full=Coenzyme B:coenzyme M:methanophenazine oxidoreductase subunit D {ECO:0000250|UniProtKB:A0A0E3NEE1};
GN   Name=hdrD; OrderedLocusNames=MA_0688;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P.,
RA   FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A.,
RA   Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R.,
RA   Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W.,
RA   Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M.,
RA   Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A.,
RA   Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K.,
RA   Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C.,
RA   Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T.,
RA   Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E.,
RA   Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic
RT   and physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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:0000250|UniProtKB:A0A0E3NEE1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coenzyme B + coenzyme M + methanophenazine = coenzyme M-
CC         coenzyme B heterodisulfide + dihydromethanophenazine;
CC         Xref=Rhea:RHEA:18085, ChEBI:CHEBI:29118, ChEBI:CHEBI:50375,
CC         ChEBI:CHEBI:58319, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596;
CC         EC=1.8.98.1; Evidence={ECO:0000250|UniProtKB:A0A0E3NEE1};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00711};
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.
CC       {ECO:0000250|UniProtKB:A0A0E3NEE1}.
CC   -!- SUBUNIT: The dihydromethanophenazine:CoB--CoM heterodisulfide
CC       reductase is composed of two subunits; HdrD and HdrE.
CC       {ECO:0000250|UniProtKB:P96797}.
CC   -!- SIMILARITY: Belongs to the HdrD family. {ECO:0000305}.
DR   EMBL; AE010299; AAM04128.1; -; Genomic_DNA.
DR   RefSeq; WP_011020733.1; NC_003552.1.
DR   ProteinModelPortal; Q8TSV7; -.
DR   PRIDE; Q8TSV7; -.
DR   EnsemblBacteria; AAM04128; AAM04128; MA_0688.
DR   GeneID; 1472580; -.
DR   KEGG; mac:MA_0688; -.
DR   eggNOG; arCOG00333; Archaea.
DR   eggNOG; COG0247; LUCA.
DR   InParanoid; Q8TSV7; -.
DR   KO; K08264; -.
DR   OMA; GALHVHA; -.
DR   OrthoDB; 21885at2157; -.
DR   PhylomeDB; Q8TSV7; -.
DR   BioCyc; MACE188937:G1FZT-729-MONOMER; -.
DR   UniPathway; UPA00647; UER00700.
DR   Proteomes; UP000002487; 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; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   Pfam; PF02754; CCG; 2.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding;
KW   Methanogenesis; Oxidoreductase; Reference proteome; Repeat.
FT   CHAIN         1    409       Dihydromethanophenazine:CoB--CoM
FT                                heterodisulfide reductase subunit D.
FT                                /FTId=PRO_0000150079.
FT   DOMAIN       14     44       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       81    110       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        24     24       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        27     27       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        30     30       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        34     34       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        90     90       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        93     93       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        96     96       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       100    100       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
SQ   SEQUENCE   409 AA;  45202 MW;  579201A5293BC83F CRC64;
     MAKKTPSIDT KNLTAVQLME LDSCTRCGEC VKWCPTYAAS GQKPGLAPRD KILRWRQYMN
     KSYGLKAKLF GPTEIPQSEL EEFKDDVHGC TTCGICATVC ESGINTVELW ESLRTNLVKK
     GIGPFGKQGM FPKLIGQYHN PYLLDQKDRL AWVPPDVKIA DKANIVYFTG CTAGYKQLAL
     AFATSRVLNK LGIEFTMLGE DEWCCGSALI RTGQVHVNDV AKELAKHNVE AIKAKGATKV
     LYACAGCFRA SKVDWPRLLG EELPFEVVHI TEFLEDLIKK DKIKWEKSLD KTVTYHDPCH
     LGRHVGVFEP PRYVLSHIPG VKFVEMDRVK EFQRCCGAGG GVKAGIPDLA LSVAESRVKD
     ALDTNADVLS SACPFCKRNL MDGRDSLKAD IEVEDVIVLV AQALGLSVE
//
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