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Entry: A0A120K0D9_9EURY
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ID   A0A120K0D9_9EURY        Unreviewed;       551 AA.
AC   A0A120K0D9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   25-OCT-2017, entry version 13.
DE   RecName: Full=Methyl-coenzyme M reductase subunit alpha {ECO:0000256|PIRNR:PIRNR000262};
DE            EC=2.8.4.1 {ECO:0000256|PIRNR:PIRNR000262};
GN   ORFNames=TL18_09320 {ECO:0000313|EMBL:AMD18197.1};
OS   Methanobrevibacter sp. YE315.
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=1609968 {ECO:0000313|EMBL:AMD18197.1, ECO:0000313|Proteomes:UP000057992};
RN   [1] {ECO:0000313|EMBL:AMD18197.1, ECO:0000313|Proteomes:UP000057992}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YE315 {ECO:0000313|EMBL:AMD18197.1,
RC   ECO:0000313|Proteomes:UP000057992};
RA   Ouwerkerk D., Gilbert R.A., Klieve A.V., Martinez E.;
RT   "Genome sequence of Methanobrevibacter sp. YE315.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; CP010834; AMD18197.1; -; Genomic_DNA.
DR   RefSeq; WP_067044659.1; NZ_CP010834.1.
DR   EnsemblBacteria; AMD18197; AMD18197; TL18_09320.
DR   GeneID; 28488058; -.
DR   KEGG; meye:TL18_09320; -.
DR   PATRIC; fig|1609968.3.peg.1899; -.
DR   KO; K00399; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000057992; 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:UP000057992};
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}; 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;  60344 MW;  EB6D7E8064097A3D CRC64;
     MADKKFLDAM KKKFVEDPTE KTTQFYNMGG WTQSERKTAF VNEGKEIAEK RGIPMYNPDI
     GSPLGQRALM SYQLSTTDTF VEGDDLHYIN NAAIQQAWDD IRRTVIVGLN TAHNVLEKRL
     GIEVTPETIT NYLETVNHAM PGAAVVQEHM VETDPLVVAD SYVKVFTGDD ELADEIDSAF
     VLDINKEFPE DQAEALKAEV GGAIWQAVRI PSIVGRVCDG GNTSRWSAMQ IGMSMISAYN
     QCAGEGATGD FAYASKHAEV VHMGTYLPVR RARAENELGG VPFGFMADIC QGSRAYPDDP
     VRSTLEVVAL GAALYDQIWL GSYMSGGVGF TQYATAAYTD NVLDDFTYYG KDYVEDKYGD
     LCSAPNNMDT VLDVGSEVAF YALEQYESYP ALLETHFGGS QRASVISAAA GCSTAFATGN
     AQTGLSAWYL SMYLHKEQHS RLGFYGFDLQ DQCGAANVFS IRNDEGLPLE MRGPNYPNYA
     MNVGHQGEYA GISQAPHSAR GDAWAFNPLV KIAFADKNLC FDFSQVRAQF AKGALREFEP
     AGERTAITPA K
//
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