HDRC1_METAC
ID HDRC1_METAC Reviewed; 247 AA.
AC Q8TLB1;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Ferredoxin:CoB-CoM heterodisulfide reductase subunit C {ECO:0000305};
DE EC=1.8.7.3 {ECO:0000305|PubMed:19968794};
GN Name=hdrC1 {ECO:0000303|PubMed:19968794};
GN OrderedLocusNames=MA_3127 {ECO:0000312|EMBL:AAM06500.1};
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., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=19968794; DOI=10.1111/j.1365-2958.2009.06990.x;
RA Buan N.R., Metcalf W.W.;
RT "Methanogenesis by Methanosarcina acetivorans involves two structurally and
RT functionally distinct classes of heterodisulfide reductase.";
RL Mol. Microbiol. 75:843-853(2010).
CC -!- FUNCTION: Part of a complex that catalyzes the reversible reduction of
CC CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB
CC (coenzyme B). Probably involved in methylotrophic methanogenesis but
CC not in aceticlastic methanogenesis. {ECO:0000269|PubMed:19968794}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coenzyme B + coenzyme M + 2 oxidized [2Fe-2S]-[ferredoxin] =
CC coenzyme M-coenzyme B heterodisulfide + 2 H(+) + 2 reduced [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:55160, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:58319, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=1.8.7.3;
CC Evidence={ECO:0000305|PubMed:19968794};
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-ProRule:PRU00711};
CC -!- PATHWAY: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide
CC reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B
CC heterodisulfide: step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: The ferredoxin:CoB-CoM heterodisulfide reductase is composed
CC of three subunits; HdrA1, HdrB1 and HdrC1.
CC {ECO:0000269|PubMed:19968794}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced on trimethylamine or methanol, but not on acetate as
CC the sole energy source. {ECO:0000269|PubMed:19968794}.
CC -!- DISRUPTION PHENOTYPE: Triple hdrA1C1B1 deletion decreases methane
CC production from methanol, but does not affect methanogenesis from
CC acetate. Deletion results in up-regulation of CoB-SH and CoM-SH
CC synthesis and transport, and methylsulfide methyltransferases.
CC {ECO:0000269|PubMed:19968794}.
CC -!- SIMILARITY: Belongs to the HdrC family. {ECO:0000305}.
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DR EMBL; AE010299; AAM06500.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TLB1; -.
DR SMR; Q8TLB1; -.
DR STRING; 188937.MA_3127; -.
DR EnsemblBacteria; AAM06500; AAM06500; MA_3127.
DR KEGG; mac:MA_3127; -.
DR HOGENOM; CLU_100474_0_0_2; -.
DR OMA; CPRNNSP; -.
DR PhylomeDB; Q8TLB1; -.
DR BioCyc; MetaCyc:MON-20158; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000002487; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; 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; IPR009051; Helical_ferredxn.
DR Pfam; PF13183; Fer4_8; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Methanogenesis;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..247
FT /note="Ferredoxin:CoB-CoM heterodisulfide reductase subunit
FT C"
FT /id="PRO_0000443938"
FT DOMAIN 32..62
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT REGION 216..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 44
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 47
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 84
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 87
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 90
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 94
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 247 AA; 27921 MW; 6D84A05F18333381 CRC64;
MIPYVKMMPY VNEYDTPECK TLAETAKKSI RTPESLGLDR CIQCGACTAS CPAARFTDYS
PRQIVKKVLE NDRSVLESEM IWSCFYCYSC NLRCPRNNSP VTIVQVLRQM AINEGIRVEK
LAYFLEIGEH LGENGASKVP GAGIKNMEKD LGERWIGIKR KLEPIRSELG LSARDVRNTH
GEVQAILEST GYFEREKWIK ARVQEKGIRG FLKTDRTGTS CTEKKKNSGD LGFESDREYT
GQEALTV
