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Database: UniProt
Entry: A7I5T9_METB6
LinkDB: A7I5T9_METB6
Original site: A7I5T9_METB6 
ID   A7I5T9_METB6            Unreviewed;       561 AA.
AC   A7I5T9;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   25-OCT-2017, entry version 56.
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=Mboo_0582 {ECO:0000313|EMBL:ABS55100.1};
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
OC   Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442 {ECO:0000313|EMBL:ABS55100.1, ECO:0000313|Proteomes:UP000002408};
RN   [1] {ECO:0000313|EMBL:ABS55100.1, ECO:0000313|Proteomes:UP000002408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8
RC   {ECO:0000313|Proteomes:UP000002408};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Zinder S., Richardson P.;
RT   "Complete sequence of Candidatus Methanoregula boonei 6A8.";
RL   Submitted (JUL-2007) 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; CP000780; ABS55100.1; -; Genomic_DNA.
DR   RefSeq; WP_012106121.1; NC_009712.1.
DR   ProteinModelPortal; A7I5T9; -.
DR   STRING; 456442.Mboo_0582; -.
DR   EnsemblBacteria; ABS55100; ABS55100; Mboo_0582.
DR   GeneID; 5411511; -.
DR   KEGG; mbn:Mboo_0582; -.
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; UP000002408; 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:UP000002408};
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:UP000002408};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000262,
KW   ECO:0000313|EMBL:ABS55100.1}.
FT   DOMAIN       10    278       MCR_alpha_N. {ECO:0000259|Pfam:PF02745}.
FT   DOMAIN      326    452       MCR_alpha. {ECO:0000259|Pfam:PF02249}.
FT   METAL       157    157       Nickel. {ECO:0000256|PIRSR:PIRSR000262-
FT                                1}.
FT   MOD_RES     267    267       Pros-methylhistidine. {ECO:0000256|PIRSR:
FT                                PIRSR000262-2}.
FT   MOD_RES     281    281       5-methylarginine. {ECO:0000256|PIRSR:
FT                                PIRSR000262-2}.
SQ   SEQUENCE   561 AA;  61510 MW;  F271B6C5C24A1E9E CRC64;
     MAKAKIERTQ KLFLKAMKEK FAEDPQATST VFARAGLEQS PRKMEFLKEG QKVALDRGIS
     MYDPKRCHCG GIPLGQRQLM TYEVSGTGVF VEGDDLHFVN NAAMQQMWDD IRRTIIVSLD
     LAHGTLQKRL GKEVTPETIN EYLHVLNHAM PGAAVVQEHM VETHPALVDD CYVKIFTGDD
     EMADDIEPQF VLNLDKLFPA KQAAALKAAV GKSMWQAVHI PTTVSRTCDG GTTSRWSAMQ
     IGMSFIGAYK MCAGEAAVSD LAFAAKHAGV IQMADILPAR RARGPNEPGG IKFGHFGDMI
     QADRKYPNDP VKATLEVVGA GAMLFDQIWL GSYMSGGVGF TQYATAAYTD NILDDYCYYG
     LDYVKKNHGG LGKAKLTQEA VSDIASEVTL YGMEQYEQYP TALEDHFGGS QRASVLAAAS
     GISASLGTFN SNAGLNAWYQ SMLLHKEGWS RLGFFGYDLQ DQCGSANCMS VRPDEGCLGE
     LRGPNYPNYA MNVGHQGEYA AIASAAHYGR QDAWVLSPLM KITFADPSLK FDFSEPRREF
     ARGAIREFMP AGERSLIIPA R
//
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