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Database: UniProt
Entry: Q8THH1_METAC
LinkDB: Q8THH1_METAC
Original site: Q8THH1_METAC 
ID   Q8THH1_METAC            Unreviewed;       570 AA.
AC   Q8THH1;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   28-FEB-2018, entry version 84.
DE   RecName: Full=Methyl-coenzyme M reductase subunit alpha {ECO:0000256|PIRNR:PIRNR000262};
DE            EC=2.8.4.1 {ECO:0000256|PIRNR:PIRNR000262};
GN   OrderedLocusNames=MA_4546 {ECO:0000313|EMBL:AAM07885.1};
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM07885.1, ECO:0000313|Proteomes:UP000002487};
RN   [1] {ECO:0000313|EMBL:AAM07885.1, ECO:0000313|Proteomes:UP000002487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC   {ECO:0000313|Proteomes:UP000002487};
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P.,
RA   FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A.,
RA   Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R.,
RA   Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W.,
RA   Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.,
RA   Hedderich R., Ingram-Smith C., Kuettner C.H., Krzycki J.A.,
RA   Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K.,
RA   Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C.,
RA   Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.,
RA   Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E.,
RA   Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic
RT   and physiological diversity.";
RL   Genome Res. 12:532-542(2002).
CC   -!- FUNCTION: Reduction of methyl-coenzyme M (2-(methylthio)
CC       ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate
CC       to methane and a heterodisulfide. {ECO:0000256|PIRNR:PIRNR000262}.
CC   -!- CATALYTIC ACTIVITY: Methyl-CoM + CoB = CoM-S-S-CoB + methane.
CC       {ECO:0000256|PIRNR:PIRNR000262}.
CC   -!- COFACTOR:
CC       Name=coenzyme F430; Xref=ChEBI:CHEBI:60540;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000262};
CC       Note=Binds 1 coenzyme F430 noncovalently per subunit. Coenzyme
CC       F430 is a yellow nickel porphinoid.
CC       {ECO:0000256|PIRNR:PIRNR000262};
CC   -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction;
CC       methane from methyl-coenzyme M: step 1/1.
CC       {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; AE010299; AAM07885.1; -; Genomic_DNA.
DR   RefSeq; WP_011024419.1; NC_003552.1.
DR   ProteinModelPortal; Q8THH1; -.
DR   SMR; Q8THH1; -.
DR   STRING; 188937.MA4546; -.
DR   PRIDE; Q8THH1; -.
DR   EnsemblBacteria; AAM07885; AAM07885; MA_4546.
DR   GeneID; 1476440; -.
DR   KEGG; mac:MA_4546; -.
DR   eggNOG; arCOG04857; Archaea.
DR   eggNOG; COG4058; LUCA.
DR   InParanoid; Q8THH1; -.
DR   KO; K00399; -.
DR   OMA; GRVCDGG; -.
DR   OrthoDB; POG093Z00ZI; -.
DR   PhylomeDB; Q8THH1; -.
DR   BioCyc; MACE188937:G1FZT-4838-MONOMER; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000002487; 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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002487};
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-
KW   1}; Reference proteome {ECO:0000313|Proteomes:UP000002487};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000262}.
FT   DOMAIN       15    282       MCR_alpha_N. {ECO:0000259|Pfam:PF02745}.
FT   DOMAIN      329    461       MCR_alpha. {ECO:0000259|Pfam:PF02249}.
FT   METAL       161    161       Nickel. {ECO:0000256|PIRSR:PIRSR000262-
FT                                1}.
FT   MOD_RES     271    271       Pros-methylhistidine. {ECO:0000256|PIRSR:
FT                                PIRSR000262-2}.
FT   MOD_RES     285    285       5-methylarginine. {ECO:0000256|PIRSR:
FT                                PIRSR000262-2}.
SQ   SEQUENCE   570 AA;  62075 MW;  D7B7CCD2899E48D3 CRC64;
     MAADIFAKFK KSMEVKFTQE YGSNKQAGGD ITGKTEKFLR LGPEQDARKQ EMIKAGKEIA
     EKRGIAFYNP MMHMGAPLGQ RAITPYTISG TDIVAEPDDL HYVNNAAMQQ MWDDIRRTCI
     VGLDMAHETL EKRLGKEVTP ETINHYLETL NHAMPGAAVV QEMMVETHPA LVDDCYVKIF
     TGDDELADEI DKQYVINVNK MFSEEQAAQI KASIGKTTWQ AIHIPTIVSR TTDGAQTSRW
     AAMQIGMSFI SAYAMCAGEA AVADLSFAAK HAALVSMGEM LPARRARGPN EPGGLSFGHL
     SDIVQTSRVS KDPAKIALEV VGAGCMLYDQ IWLGSYMSGG VGFTQYATAA YTDDILDNNT
     YYDVDYINDK YNGAANLGTD NKVKATLDVV KDIATESTLY GIETYEKFPT ALEDHFGGSQ
     RATVLAAASG VACALATGNA NAGLSGWYLS MYVHKEAWGR LGFFGFDLQD QCGATNVLSY
     QGDEGLPDEL RGPNYPNYAM NVGHQGGYAG IAQAAHSGRG DAFTVNPLLK VCFADELMPF
     NFAEPRREFG RGAIREFMPA GERSLVIPAK
//
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