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Database: UniProt
Entry: Q8PY84
LinkDB: Q8PY84
Original site: Q8PY84 
ID   HDRC_METMA              Reviewed;         161 AA.
AC   Q8PY84;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   10-APR-2019, entry version 107.
DE   RecName: Full=Ferredoxin:CoB-CoM heterodisulfide reductase subunit C {ECO:0000250|UniProtKB:Q8TLB1};
DE            EC=1.8.7.3 {ECO:0000250|UniProtKB:Q8TLB1};
GN   Name=hdrC; OrderedLocusNames=MM_0979;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 /
OS   JCM 11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   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).
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:Q8TLB1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coenzyme B + coenzyme M + 2 oxidized [2Fe-2S]-
CC         [ferredoxin] = coenzyme M-coenzyme B heterodisulfide + 2 H(+) +
CC         2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:55160,
CC         Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:58319,
CC         ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=1.8.7.3;
CC         Evidence={ECO:0000250|UniProtKB:Q8TLB1};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC       Note=Binds 2 [4Fe-4S] cluster. {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:Q8TLB1}.
CC   -!- SUBUNIT: The ferredoxin:CoB-CoM heterodisulfide reductase is
CC       composed of three subunits; HdrA, HdrB and HdrC.
CC       {ECO:0000250|UniProtKB:Q8TLB1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TLB1}.
CC   -!- SIMILARITY: Belongs to the HdrC family. {ECO:0000305}.
DR   EMBL; AE008384; AAM30675.1; -; Genomic_DNA.
DR   RefSeq; WP_011032929.1; NC_003901.1.
DR   ProteinModelPortal; Q8PY84; -.
DR   SMR; Q8PY84; -.
DR   STRING; 192952.MM_0979; -.
DR   EnsemblBacteria; AAM30675; AAM30675; MM_0979.
DR   GeneID; 24880189; -.
DR   KEGG; mma:MM_0979; -.
DR   PATRIC; fig|192952.21.peg.1154; -.
DR   eggNOG; arCOG00964; Archaea.
DR   eggNOG; COG1150; LUCA.
DR   HOGENOM; HOG000237015; -.
DR   KO; K03390; -.
DR   OMA; WLCTTCY; -.
DR   OrthoDB; 102216at2157; -.
DR   BioCyc; MMAZ192952:G1FZI-1026-MONOMER; -.
DR   UniPathway; UPA00647; UER00700.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051186; P:cofactor metabolic process; IEA:InterPro.
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; IPR017680; CoB/CoM_hetero-S_Rdtase_csu.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   TIGRFAMs; TIGR03290; CoB_CoM_SS_C; 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; Cytoplasm; Iron; Iron-sulfur;
KW   Metal-binding; Methanogenesis; Oxidoreductase; Repeat.
FT   CHAIN         1    161       Ferredoxin:CoB-CoM heterodisulfide
FT                                reductase subunit C.
FT                                /FTId=PRO_0000150076.
FT   DOMAIN       10     40       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       51     82       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        19     19       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        22     22       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        25     25       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        29     29       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        62     62       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        65     65       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        68     68       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        72     72       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
SQ   SEQUENCE   161 AA;  18120 MW;  40F05C2B90FC23BA CRC64;
     MSEELLKVLK AAGLDVLSCM HCGTCTGSCP SGRHTGLNTR RIIRDARKNR ATVLSDDALW
     LCTTCYTCQE RCPRGIPITD ALLELRRLAV RKGFMRPEHR RVSELVLECG HAVPLDEETK
     KKREELGLDP IPETVQKYPE ALEELKALLK TCKFDELAAE K
//
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