ID   HDRD_METMA              Reviewed;         409 AA.
AC   Q8PVW3;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   24-MAR-2009, entry version 49.
DE   RecName: Full=CoB--CoM heterodisulfide reductase 2 iron-sulfur subunit D;
DE            EC=1.8.98.1;
GN   Name=hdrD; OrderedLocusNames=MM_1844;
OS   Methanosarcina mazei (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2209;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
RX   MEDLINE=22120827; PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene
RT   transfer between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN   [2]
RP   FUNCTION, AND SOURCE OF ELECTRONS.
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
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).
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). HdrD may act as the catalytic
CC       subunit.
CC   -!- CATALYTIC ACTIVITY: Coenzyme B + coenzyme M + methanophenazine =
CC       N-(7-((2-sulfoethyl)dithio)heptanoyl)-O(3)-phospho-L-threonine +
CC       dihydromethanophenazine.
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters per subunit (By similarity).
CC   -!- PATHWAY: Cofactor metabolism; coenzyme B/coenzyme M regeneration;
CC       coenzyme B and coenzyme M from CoB-CoM heterodisulfide: step 1/1.
CC   -!- SUBUNIT: The heterodisulfide reductase 2 is composed of two
CC       subunits; hdrD and hdrE (By similarity).
CC   -!- MISCELLANEOUS: Methanophenazine seems to mediate electron transfer
CC       from a F420-non-reducing hydrogenase to the heterodisulfide
CC       reductase 2.
CC   -!- SIMILARITY: Belongs to the hdrD family.
CC   -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
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DR   EMBL; AE008384; AAM31540.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_633868.1; -.
DR   GeneID; 1480186; -.
DR   GenomeReviews; AE008384_GR; MM_1844.
DR   KEGG; mma:MM_1844; -.
DR   NMPDR; fig|192952.1.peg.1844; -.
DR   HOGENOM; Q8PVW3; -.
DR   BioCyc; MMAZ192952:MM1844-MON; -.
DR   BRENDA; 1.8.98.1; 261165.
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:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_region.
DR   InterPro; IPR012285; Fum_reductase_C.
DR   Gene3D; G3DSA:1.10.1060.10; Fum_reductase_C; 1.
DR   Pfam; PF02754; CCG; 2.
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; Repeat.
FT   CHAIN         1    409       CoB--CoM heterodisulfide reductase 2
FT                                iron-sulfur subunit D.
FT                                /FTId=PRO_0000150081.
FT   DOMAIN       14     44       4Fe-4S ferredoxin-type 1.
FT   DOMAIN       81    110       4Fe-4S ferredoxin-type 2.
FT   METAL        24     24       Iron-sulfur 1 (4Fe-4S) (Potential).
FT   METAL        27     27       Iron-sulfur 1 (4Fe-4S) (Potential).
FT   METAL        30     30       Iron-sulfur 1 (4Fe-4S) (Potential).
FT   METAL        34     34       Iron-sulfur 2 (4Fe-4S) (Potential).
FT   METAL        90     90       Iron-sulfur 2 (4Fe-4S) (Potential).
FT   METAL        93     93       Iron-sulfur 2 (4Fe-4S) (Potential).
FT   METAL        96     96       Iron-sulfur 2 (4Fe-4S) (Potential).
FT   METAL       100    100       Iron-sulfur 1 (4Fe-4S) (Potential).
SQ   SEQUENCE   409 AA;  45377 MW;  F74FA592197FAC46 CRC64;
     MAKKTPSIDT KNLTAVQLME LDSCTRCGEC VKWCPTYAAS GQKPGLAPRD KILRWRQFMN
     KSYGIKAKLF GPTEIPQSEL EEFKDDVHGC TTCGICATVC ESGINTVELW EALRTNLVKK
     GIGPFGKQNM FPKLIGQYHN PYMKDQKDRL NWVPPDVKIE DKADVVYFTG CTAGYNQLAL
     AFATARVLNK LGVKFSMLGE EEWCCGSALI RTGQVHVDDV PRELARHNVE ALKKKGAKKV
     LYACAGCFRA SKVDWPRLLG EELPFEVVHV AEFLADLIKQ DKIKWEKSIN KTVTYHDPCH
     LGRHVGVFDA PRYVLSHIPG VKFVEMDRVK EFQRCCGAGG GVKAGIPDLA LGVAESRVKD
     AVATDADILS SCCPFCKRNL MDGRDSLKVD MVVEDVIELV AEALGLETK
//