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Database: UniProt
Entry: Q8PXH8_METMA
LinkDB: Q8PXH8_METMA
Original site: Q8PXH8_METMA 
ID   Q8PXH8_METMA            Unreviewed;       570 AA.
AC   Q8PXH8;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   18-JUL-2018, entry version 90.
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=MM_1240 {ECO:0000313|EMBL:AAM30936.1};
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 /
OS   JCM 11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952 {ECO:0000313|EMBL:AAM30936.1, ECO:0000313|Proteomes:UP000000595};
RN   [1] {ECO:0000313|EMBL:AAM30936.1, ECO:0000313|Proteomes:UP000000595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
RC   {ECO:0000313|Proteomes:UP000000595};
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baumer S., Jacobi C.,
RA   Bruggemann H., Lienard T., Christmann A., Bomeke 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: 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; AE008384; AAM30936.1; -; Genomic_DNA.
DR   RefSeq; WP_011033189.1; NC_003901.1.
DR   ProteinModelPortal; Q8PXH8; -.
DR   STRING; 192952.MM_1240; -.
DR   EnsemblBacteria; AAM30936; AAM30936; MM_1240.
DR   GeneID; 24837655; -.
DR   KEGG; mma:MM_1240; -.
DR   PATRIC; fig|192952.21.peg.1445; -.
DR   eggNOG; arCOG04857; Archaea.
DR   eggNOG; COG4058; LUCA.
DR   HOGENOM; HOG000225809; -.
DR   KO; K00399; -.
DR   OMA; GRVCDGG; -.
DR   OrthoDB; POG093Z00ZI; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000000595; 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:UP000000595};
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}; Oxidoreductase {ECO:0000313|EMBL:AAM30936.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000595};
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;  61914 MW;  41D392ED080CA9BC CRC64;
     MAADIFSKFK KSMEVKFTQE YGSNQQAGGD ITGKTAKFLR LGPEQDARKA EMIKAGKEIA
     EKRGIAFYNP MMHSGAPLGQ RAITPYTLSG TDIVAEPDDL HYVNNAAMQQ MWDDIRRTCI
     VGLDMAHETL EKRLGKEVTP ETINHYLEVL NHAMPGAAVV QEMMVETHPA LVDDCYVKVF
     TGDDELADEI DKQYVININK MFSEEQAAQI KASMGKTTWQ AIHIPTIVSR TTDGAQTSRW
     AAMQIGMSFI SAYAMCAGEA AVADLSFAAK HAALVSMGEM LPARRARGPN EPGGLSFGHL
     ADIIQTSRVS QDPAKIALEV VGAGCMLYDQ IWLGSYMSGG VGFTQYATAA YTDDILDNNT
     YYDVDYINDK YNGAANLGTD NKVKATLDVV KDIATESTLY GIETYEKFPT ALEDHFGGSQ
     RATVLAAASG VACALATGNA NAGLSGWYLS MYVHKEAWGR LGFFGFDLQD QCGATNVLSY
     QGDEGLPDEL RGPNYPNYAM NVGHQGGYAG IAQAAHSGRG DAFTVNPLIK VCFADDLMPF
     NFAEPRREFG RGAIREFVPA GERSLIIPAK
//
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