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Database: UniProt
Entry: MCRX_METJA
LinkDB: MCRX_METJA
Original site: MCRX_METJA 
ID   MCRX_METJA              Reviewed;         552 AA.
AC   Q60391;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-OCT-2017, entry version 113.
DE   RecName: Full=Methyl-coenzyme M reductase II subunit alpha;
DE            Short=MCR II alpha;
DE            EC=2.8.4.1;
DE   AltName: Full=Coenzyme-B sulfoethylthiotransferase alpha;
GN   Name=mrtA; Synonyms=mtrA; OrderedLocusNames=MJ0083;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 /
OS   JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D.,
RA   Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
RA   Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
RA   Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
RA   Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
RA   Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
RA   Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
RA   Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Reduction of methyl-coenzyme M (2-(methylthio)
CC       ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate
CC       to methane and a heterodisulfide.
CC   -!- CATALYTIC ACTIVITY: Methyl-CoM + CoB = CoM-S-S-CoB + methane.
CC   -!- COFACTOR:
CC       Name=coenzyme F430; Xref=ChEBI:CHEBI:60540;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 coenzyme F430 noncovalently per subunit. Coenzyme
CC       F430 is a yellow nickel porphinoid. {ECO:0000250};
CC   -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction;
CC       methane from methyl-coenzyme M: step 1/1.
CC   -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains.
CC       {ECO:0000250}.
DR   EMBL; L77117; AAB98063.1; -; Genomic_DNA.
DR   PIR; C64310; C64310.
DR   RefSeq; WP_010869575.1; NC_000909.1.
DR   ProteinModelPortal; Q60391; -.
DR   SMR; Q60391; -.
DR   STRING; 243232.MJ_0083; -.
DR   EnsemblBacteria; AAB98063; AAB98063; MJ_0083.
DR   GeneID; 1450922; -.
DR   KEGG; mja:MJ_0083; -.
DR   eggNOG; arCOG04857; Archaea.
DR   eggNOG; COG4058; LUCA.
DR   InParanoid; Q60391; -.
DR   KO; K00399; -.
DR   OMA; QVWLGSY; -.
DR   OrthoDB; POG093Z00ZI; -.
DR   PhylomeDB; Q60391; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Complete proteome; Metal-binding; Methanogenesis; Methylation; Nickel;
KW   Reference proteome; Transferase.
FT   CHAIN         1    552       Methyl-coenzyme M reductase II subunit
FT                                alpha.
FT                                /FTId=PRO_0000147453.
FT   METAL       150    150       Nickel. {ECO:0000250}.
FT   MOD_RES     260    260       Pros-methylhistidine. {ECO:0000250}.
FT   MOD_RES     274    274       5-methylarginine. {ECO:0000250}.
SQ   SEQUENCE   552 AA;  61241 MW;  DB66781796B987CE CRC64;
     MDVEKKLFLK ALKEKFEEDP KEKYTKFYIF GGWRQSARKR EFVEFAQKLI EKRGGIPFYN
     PDIGVPLGQR KLMTYKISGT DAFVEGDDLH FCNNAAIQQL VDDIKRTVIV GMDTAHAVLE
     KRLGVEVTPE TINEYMETIN HALPGGAVVQ EHMVEVHPGL VWDCYAKIFT GNDELADEID
     KRFLIDINKE FPEEQAEQIK KYIGNRTYQV SRVPTIVVRC CDGGTVSRWS AMQIGMSFIT
     AYKLCAGEAA IADFSYAAKH ADVIQMGMIL PARRARGPNE PGGVPFGIFA DIIQTSRVSD
     DPAQVTLEVI GAAATFYDQV WLGSYMSGGV GFTQYASATY TDDILDDFVY YGMDYVEKKY
     GLCGVKPSME VVKDIATEVT LYGLEQYDEY PALLEDHFGG SQRAGVTAAA AGCSVAFATG
     NSNAGINGWY LSQILHKEYH SRLGFYGYDL QDQCGAANSL SIRSDEGLLH ECRGPNYPNY
     AMNVGHQPEY AGIAQAPHAA RGDAFCLNPI IKVAFADDNL IFDFKWPRKC IAKGALREFE
     PAGERDLIIP AA
//
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