(data stored in ACNUC10043 zone)

SWISSPROT: D1YVW6_METPS

ID   D1YVW6_METPS            Unreviewed;       557 AA.
AC   D1YVW6;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 42.
DE   RecName: Full=Methyl-coenzyme M reductase subunit alpha {ECO:0000256|PIRNR:PIRNR000262};
DE            EC=2.8.4.1 {ECO:0000256|PIRNR:PIRNR000262};
GN   Name=mcrA {ECO:0000313|EMBL:BAI60588.1};
GN   OrderedLocusNames=MCP_0516 {ECO:0000313|EMBL:BAI60588.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60588.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: Component of the methyl-coenzyme M reductase (MCR) I that
CC       catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2-
CC       (methylthio)ethanesulfonate) using coenzyme B (CoB or 7-
CC       mercaptoheptanoylthreonine phosphate) as reductant which results in the
CC       production of methane and the mixed heterodisulfide of CoB and CoM
CC       (CoM-S-S-CoB). This is the final step in methanogenesis.
CC       {ECO:0000256|PIRNR:PIRNR000262}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coenzyme B + methyl-coenzyme M = coenzyme M-coenzyme B
CC         heterodisulfide + methane; Xref=Rhea:RHEA:12532, ChEBI:CHEBI:16183,
CC         ChEBI:CHEBI:58286, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596; EC=2.8.4.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000262};
CC   -!- COFACTOR:
CC       Name=coenzyme F430; Xref=ChEBI:CHEBI:60540;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000262};
CC       Note=Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme
CC       F430 is a yellow nickel porphinoid. Methyl-coenzyme-M reductase is
CC       activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I)
CC       oxidation state. {ECO:0000256|PIRNR:PIRNR000262};
CC   -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; methane
CC       from methyl-coenzyme M: step 1/1. {ECO:0000256|PIRNR:PIRNR000262}.
CC   -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains.
CC       {ECO:0000256|PIRNR:PIRNR000262}.
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DR   EMBL; AP011532; BAI60588.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0516; -.
DR   EnsemblBacteria; BAI60588; BAI60588; MCP_0516.
DR   KEGG; mpd:MCP_0516; -.
DR   PATRIC; fig|304371.9.peg.531; -.
DR   eggNOG; arCOG04857; Archaea.
DR   eggNOG; COG4058; LUCA.
DR   HOGENOM; HOG000225809; -.
DR   KO; K00399; -.
DR   OMA; AHSARGD; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.840.10; -; 1.
DR   Gene3D; 3.30.70.470; -; 1.
DR   Gene3D; 3.90.390.10; -; 1.
DR   InterPro; IPR016212; Me_CoM_Rdtase_asu.
DR   InterPro; IPR008924; Me_CoM_Rdtase_asu/bsu_C.
DR   InterPro; IPR009047; Me_CoM_Rdtase_asu_C.
DR   InterPro; IPR003183; Me_CoM_Rdtase_asu_N.
DR   InterPro; IPR015811; Me_CoM_Rdtase_asu_N_sub1.
DR   InterPro; IPR015823; Me_CoM_Rdtase_asu_N_sub2.
DR   InterPro; IPR009024; Me_CoM_Rdtase_Fd-like_fold.
DR   Pfam; PF02249; MCR_alpha; 1.
DR   Pfam; PF02745; MCR_alpha_N; 1.
DR   PIRSF; PIRSF000262; MCR_alpha; 1.
DR   SUPFAM; SSF48081; SSF48081; 1.
DR   SUPFAM; SSF55088; SSF55088; 1.
DR   TIGRFAMs; TIGR03256; met_CoM_red_alp; 1.
PE   4: Predicted;
DR   PRODOM; D1YVW6.
DR   SWISS-2DPAGE; D1YVW6.
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000262,
KW   ECO:0000256|PIRSR:PIRSR000262-1};
KW   Methanogenesis {ECO:0000256|PIRNR:PIRNR000262};
KW   Nickel {ECO:0000256|PIRNR:PIRNR000262, ECO:0000256|PIRSR:PIRSR000262-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000262}.
FT   DOMAIN          7..275
FT                   /note="MCR_alpha_N"
FT                   /evidence="ECO:0000259|Pfam:PF02745"
FT   DOMAIN          323..448
FT                   /note="MCR_alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02249"
FT   METAL           154
FT                   /note="Nickel"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000262-1"
FT   MOD_RES         264
FT                   /note="Pros-methylhistidine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000262-2"
FT   MOD_RES         278
FT                   /note="5-methylarginine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000262-2"
SQ   SEQUENCE   557 AA;  60792 MW;  E468823855704C42 CRC64;
     MSVKETQKRF IKAMKKKFAG EDPTSTTTVY KYEGYTQSKR KVEFKKAGDA IAKKRGISAY
     NPMVHMGGIP LGQRQLTPYV VSGTDVVVEG DDLHFVNNAA MQQFWDEIRR TVIVGLDTAH
     ATLEKRLGKT VTPETISNYL AILNHAMPGA AVVQEHMVET NPALTDDCFV KVFTGDDELA
     DSIDKQYVLD INKAFPKDQA AALKKAVGKS LYQAVHIPTT VVRTCDGGTT SRWSAMQIGM
     SFIDAYKMCA GEAAVADLAF AAKHASLVEM ADILPARRAR GPNEPGGLSF GFLADIVQTN
     RKYPDDPCKS SLEVVAAGCM LYDQIWLGSY MSGGVGFTQY ATAAYTDDIL DDFTYYGYDY
     AKGKYKIGQT KPTMDIVNDL STEVTLYGIE QYEKYPTTLE DHFGGSQRAT VLSAAAGVTT
     AIATGNSNAG LSGWYMSMYL HKEAWGRLGF FGYDLQDQCG ATNVFSCRSD EGAIDELRGP
     NYPNYAMNVG HQGGYAGIAG AAHFGRGDAW TASPLIKICF ADKSLAFDFT EPRKEFARGA
     IREFMPAGER TLVIPAK
//

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