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Database: UniProt
Entry: P96797
LinkDB: P96797
Original site: P96797 
ID   HDRD_METBF              Reviewed;         409 AA.
AC   P96797; Q46C47; Q9UWK2;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   10-APR-2019, entry version 129.
DE   RecName: Full=Dihydromethanophenazine:CoB--CoM heterodisulfide reductase subunit D {ECO:0000305};
DE            EC=1.8.98.1 {ECO:0000250|UniProtKB:A0A0E3NEE1};
DE   AltName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit D {ECO:0000305};
DE   AltName: Full=Coenzyme B:coenzyme M:methanophenazine oxidoreductase subunit D {ECO:0000305};
GN   Name=hdrD; OrderedLocusNames=Mbar_A1599;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, AND SUBUNIT.
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=9063468; DOI=10.1111/j.1432-1033.1997.00226.x;
RA   Kuenkel A., Vaupel M., Heim S., Thauer R.K., Hedderich R.;
RT   "Heterodisulfide reductase from methanol-grown cells of Methanosarcina
RT   barkeri is not a flavoenzyme.";
RL   Eur. J. Biochem. 244:226-234(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/JB.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-20, FUNCTION, AND SUBUNIT.
RX   PubMed=8174566; DOI=10.1111/j.1432-1033.1994.tb18800.x;
RA   Heiden S., Hedderich R., Setzke E., Thauer R.K.;
RT   "Purification of a two-subunit cytochrome-b-containing heterodisulfide
RT   reductase from methanol-grown Methanosarcina barkeri.";
RL   Eur. J. Biochem. 221:855-861(1994).
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:0000305|PubMed:8174566,
CC       ECO:0000305|PubMed:9063468}.
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         ECO:0000305|PubMed:9063468};
CC       Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00711, ECO:0000305|PubMed:9063468};
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 dihydromethanophenazine:CoB--CoM heterodisulfide
CC       reductase is composed of two subunits; HdrD and HdrE.
CC       {ECO:0000269|PubMed:8174566, ECO:0000269|PubMed:9063468}.
CC   -!- SIMILARITY: Belongs to the HdrD family. {ECO:0000305}.
DR   EMBL; Y09870; CAA70997.1; -; Genomic_DNA.
DR   EMBL; CP000099; AAZ70545.1; -; Genomic_DNA.
DR   PIR; S43468; S43468.
DR   RefSeq; WP_011306591.1; NC_007355.1.
DR   ProteinModelPortal; P96797; -.
DR   STRING; 269797.Mbar_A1599; -.
DR   TCDB; 3.D.7.1.1; the h2:heterodisulfide oxidoreductase (hho) family.
DR   EnsemblBacteria; AAZ70545; AAZ70545; Mbar_A1599.
DR   GeneID; 3624318; -.
DR   KEGG; mba:Mbar_A1599; -.
DR   eggNOG; arCOG00333; Archaea.
DR   eggNOG; COG0247; LUCA.
DR   HOGENOM; HOG000227862; -.
DR   KO; K08264; -.
DR   OMA; GALHVHA; -.
DR   OrthoDB; 21885at2157; -.
DR   BioCyc; MetaCyc:HDRDMBARK-MONOMER; -.
DR   UniPathway; UPA00647; UER00700.
DR   Proteomes; UP000008156; 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; 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   1: Evidence at protein level;
KW   4Fe-4S; Complete proteome; Direct protein sequencing; Iron;
KW   Iron-sulfur; Metal-binding; Methanogenesis; Oxidoreductase; Repeat.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:8174566}.
FT   CHAIN         2    409       Dihydromethanophenazine:CoB--CoM
FT                                heterodisulfide reductase subunit D.
FT                                /FTId=PRO_0000150080.
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}.
FT   CONFLICT     43     44       KP -> HQ (in Ref. 1; CAA70997).
FT                                {ECO:0000305}.
SQ   SEQUENCE   409 AA;  45055 MW;  1AC01503AA1F5BDE CRC64;
     MAKRTPSIDT KNLTAVQLME LDACVRCGEC VKWCPTYAAS GGKPGLAPRD KILRWRQYMN
     KSYGLKAKLF GPQEVSPSEL EEFKDDVHGC TTCGVCATVC EAGINTVEIW EAIRTNLVKK
     GIGPYGKQSA FPKLVGQYHN PYMKDQKDRL AWVPPDVKIE DKADIVYFTG CTAGYNQLAL
     AFATSRVLNK LGIKFAMLGE EEWCCGSALI RTGQVHVDDV ARELARHNVE ALQKKGAKKV
     LFACAGCFRA AKIDWPRLLG KELPFEVIHI TQFLADLIQA DKIKWEKPIN KTITYHDPCH
     LGRHVGVFNA PRYVLSHIPG VKFVEMDRSK EFQRCCGAGG GVKAGMPDLA VAMGESRVKD
     ALETNADILS SACPFCKRNL SDGRDALKSD IVVEDIIELV AEALGLSTS
//
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