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Database: UniProt
Entry: A5ULZ2_METS3
LinkDB: A5ULZ2_METS3
Original site: A5ULZ2_METS3 
ID   A5ULZ2_METS3            Unreviewed;       551 AA.
AC   A5ULZ2;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   25-OCT-2017, entry version 51.
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=Msm_1015 {ECO:0000313|EMBL:ABQ87220.1};
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 /
OS   PS).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247 {ECO:0000313|EMBL:ABQ87220.1, ECO:0000313|Proteomes:UP000001992};
RN   [1] {ECO:0000313|EMBL:ABQ87220.1, ECO:0000313|Proteomes:UP000001992}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS
RC   {ECO:0000313|Proteomes:UP000001992};
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M.,
RA   Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K.,
RA   Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to
RT   the human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ87220.1; -; Genomic_DNA.
DR   RefSeq; WP_011954235.1; NC_009515.1.
DR   ProteinModelPortal; A5ULZ2; -.
DR   STRING; 420247.Msm_1015; -.
DR   EnsemblBacteria; ABQ87220; ABQ87220; Msm_1015.
DR   GeneID; 5215711; -.
DR   KEGG; msi:Msm_1015; -.
DR   PATRIC; fig|420247.28.peg.1013; -.
DR   eggNOG; arCOG04857; Archaea.
DR   eggNOG; COG4058; LUCA.
DR   HOGENOM; HOG000225809; -.
DR   KO; K00399; -.
DR   OMA; GRVCDGG; -.
DR   OrthoDB; POG093Z00ZI; -.
DR   BioCyc; MSMI420247:GHWZ-1040-MONOMER; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000001992; 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:UP000001992};
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:UP000001992};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000262}.
FT   DOMAIN        3    268       MCR_alpha_N. {ECO:0000259|Pfam:PF02745}.
FT   DOMAIN      316    442       MCR_alpha. {ECO:0000259|Pfam:PF02249}.
FT   METAL       147    147       Nickel. {ECO:0000256|PIRSR:PIRSR000262-
FT                                1}.
FT   MOD_RES     257    257       Pros-methylhistidine. {ECO:0000256|PIRSR:
FT                                PIRSR000262-2}.
FT   MOD_RES     271    271       5-methylarginine. {ECO:0000256|PIRSR:
FT                                PIRSR000262-2}.
SQ   SEQUENCE   551 AA;  60483 MW;  D2509B607F1EAA45 CRC64;
     MADKKFLDAM KNKFSEGPTD KRTTFYNMGG WKQSERKSAF VKEGKEIAEK RGIPMYNPDI
     GTPLGQRALM SYQLSTTDTY VEGDDLHFIN NAAIQQAWDD IRRTVIVGLN TAHNVLEKRL
     GIEVTPETIT EYLETVNHAM PGAAVVQEHM VETDPLVVQD SYVKVFTGDD ELADEIDSAF
     VLDINKEFNE EQAAALKEEV GGSVWQAVRI PAIVGRVCDG GTTSRWSAMQ IGMSMISAYN
     QCAGEGATGD FAYASKHAEV IHMGTYLPVR RARAENELGG VPFGFMADIC QSSRVNADDP
     VRSTLDVVAL GAALYDQIWL GSYMSGGVGF TQYATAAYTD DVLDDFTYYG KDYVEDKYGG
     LTEAPNNMDT VLDVGSEVSF YALEQYEEYP ALLETHFGGS QRASVISAAA GCSTAFATGN
     AQTGLSAWYL GMYLHKEQHS RLGFYGYDLQ DQCGAANVFS IRNDEGLPLE MRGPNYPNYA
     MNVGHQGEYA GIAQAPHAAR GDAWSFNPLV KIAFADKNLV FDFSKPREEF AKGALREFEP
     SGERTVITPA K
//
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