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Database: UniProt
Entry: A0A0E3NEE1
LinkDB: A0A0E3NEE1
Original site: A0A0E3NEE1 
ID   HDRD_METTT              Reviewed;         409 AA.
AC   A0A0E3NEE1;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 17.
DE   RecName: Full=Dihydromethanophenazine:CoB--CoM heterodisulfide reductase subunit D {ECO:0000305};
DE            EC=1.8.98.1 {ECO:0000269|PubMed:11034998, ECO:0000269|PubMed:9654152, ECO:0000305|PubMed:9665708};
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; ORFNames=MSTHT_2244 {ECO:0000312|EMBL:AKB14002.1};
OS   Methanosarcina thermophila (strain ATCC 43570 / DSM 1825 / OCM 12 /
OS   VKM B-1830 / TM-1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=523844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / VKM B-1830 / TM-1;
RA   Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA   Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT   "Methanogenic archaea and the global carbon cycle.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-21, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / VKM B-1830 / TM-1;
RX   PubMed=9665708; DOI=10.1021/bi9726483;
RA   Simianu M., Murakami E., Brewer J.M., Ragsdale S.W.;
RT   "Purification and properties of the heme- and iron-sulfur-containing
RT   heterodisulfide reductase from Methanosarcina thermophila.";
RL   Biochemistry 37:10027-10039(1998).
RN   [3]
RP   FUNCTION, SOURCE OF ELECTRONS, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / VKM B-1830 / TM-1;
RX   PubMed=9654152; DOI=10.1016/S0014-5793(98)00555-9;
RA   Baeumer S., Murakami E., Brodersen J., Gottschalk G., Ragsdale S.W.,
RA   Deppenmeier U.;
RT   "The F420H2:heterodisulfide oxidoreductase system from Methanosarcina
RT   species. 2-Hydroxyphenazine mediates electron transfer from F420H2
RT   dehydrogenase to heterodisulfide reductase.";
RL   FEBS Lett. 428:295-298(1998).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   PATHWAY.
RC   STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / VKM B-1830 / TM-1;
RX   PubMed=11034998; DOI=10.1074/jbc.M004809200;
RA   Murakami E., Deppenmeier U., Ragsdale S.W.;
RT   "Characterization of the intramolecular electron transfer pathway from
RT   2-hydroxyphenazine to the heterodisulfide reductase from
RT   Methanosarcina thermophila.";
RL   J. Biol. Chem. 276:2432-2439(2001).
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) (PubMed:9654152, PubMed:9665708,
CC       PubMed:11034998). Electrons probably transfer from phenazine to
CC       the high potential 4Fe cluster in HdrD subunit, then to the low
CC       potential heme in HdrE subunit and finally to CoM-S-S-CoB
CC       (PubMed:11034998). {ECO:0000269|PubMed:11034998,
CC       ECO:0000269|PubMed:9654152, ECO:0000269|PubMed:9665708}.
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:0000269|PubMed:11034998,
CC         ECO:0000269|PubMed:9654152, ECO:0000305|PubMed:9665708};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00711,
CC         ECO:0000269|PubMed:9665708};
CC       Note=Binds 2 [4Fe-4S] cluster. {ECO:0000255|PROSITE-
CC       ProRule:PRU00711, ECO:0000269|PubMed:9665708};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=92 uM for reduced 2-hydroxyphenazine
CC         {ECO:0000269|PubMed:11034998};
CC         KM=144 uM for CoM-S-S-CoB {ECO:0000269|PubMed:11034998};
CC         Note=kcat is 74 sec(-1) at 25 degrees Celsius.
CC         {ECO:0000269|PubMed:11034998};
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:0000305|PubMed:11034998}.
CC   -!- SUBUNIT: The dihydromethanophenazine:CoB--CoM heterodisulfide
CC       reductase is composed of two subunits; HdrD and HdrE.
CC       {ECO:0000269|PubMed:9665708}.
CC   -!- MISCELLANEOUS: Methanophenazine seems to mediate electron transfer
CC       from F(420)H(2) dehydrogenase to the dihydromethanophenazine:CoB--
CC       CoM heterodisulfide reductase. {ECO:0000305|PubMed:9654152}.
CC   -!- SIMILARITY: Belongs to the HdrD family. {ECO:0000305}.
DR   EMBL; CP009501; AKB14002.1; -; Genomic_DNA.
DR   RefSeq; WP_048167969.1; NZ_CP009501.1.
DR   EnsemblBacteria; AKB14002; AKB14002; MSTHT_2244.
DR   GeneID; 24849247; -.
DR   KEGG; mthr:MSTHT_2244; -.
DR   PATRIC; fig|523844.20.peg.2748; -.
DR   KO; K08264; -.
DR   OrthoDB; 21885at2157; -.
DR   UniPathway; UPA00647; UER00700.
DR   Proteomes; UP000066529; 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; 1.
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.
FT   CHAIN         2    409       Dihydromethanophenazine:CoB--CoM
FT                                heterodisulfide reductase subunit D.
FT                                /FTId=PRO_0000443856.
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;  45454 MW;  3D93654EC149FF32 CRC64;
     MAKRNPSIDT KNLTAVQLME LDACVRCGEC VKWCPTYAAS GEKPGLAPRD KILRWRQYMN
     KSYGLKARLF GPQEIPISEL EEFKDDVHGC TTCGICSTVC EAGINTVELW ESMRANLVKK
     GIGPYGKQNM FPKLIGQYRN PYMKDQKDRL AWVPPDVKIE DKADIVYFTG CTAGYNQLAL
     AFATSRVLNK LGIKFAMLGE DEWCCGSALI RTGQAHINNV PYELAKHNVE AIQKKGAKKV
     LFACAGCFRA AKVDWPRLLG KELPFEVVHV SEFLAGLIKE GKIKWEKSIN KTVTYHDPCH
     LGRHVGVFDA PRYVLSHIPG VKFVEMDRIK EFQRCCGAGG GVKAGLPDLA MAVAESRVKD
     ALDTKADILS SCCPFCKRNL MDGRDSLKVD LVVEDVIELV AEALNLETK
//
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