GenomeNet

Database: UniProt
Entry: MCRX_METTH
LinkDB: MCRX_METTH
Original site: MCRX_METTH 
ID   MCRX_METTH              Reviewed;         553 AA.
AC   P21110; O27201; Q50487;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 3.
DT   28-MAR-2018, entry version 122.
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; OrderedLocusNames=MTH_1129;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 /
OS   JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=7929010; DOI=10.1128/jb.176.20.6384-6391.1994;
RA   Pihl T.D., Sharma S., Reeve J.N.;
RT   "Growth phase-dependent transcription of the genes that encode the two
RT   methyl coenzyme M reductase isoenzymes and N5-
RT   methyltetrahydromethanopterin:coenzyme M methyltransferase in
RT   Methanobacterium thermoautotrophicum delta H.";
RL   J. Bacteriol. 176:6384-6391(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K.,
RA   Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D.,
RA   Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R.,
RA   Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S.,
RA   McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M.,
RA   Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum
RT   deltaH: functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-15.
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=2269306; DOI=10.1111/j.1432-1033.1990.tb19481.x;
RA   Rospert S., Linder D., Ellermann J., Thauer R.K.;
RT   "Two genetically distinct methyl-coenzyme M reductases in
RT   Methanobacterium thermoautotrophicum strain Marburg and delta H.";
RL   Eur. J. Biochem. 194:871-877(1990).
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   -!- DEVELOPMENTAL STAGE: There are two MCR complexes in this bacteria.
CC       MCR II is expressed in the early growth phase. Late growth cells
CC       contains mostly MCR I.
DR   EMBL; U09990; AAA73439.1; -; Genomic_DNA.
DR   EMBL; AE000666; AAB85618.1; -; Genomic_DNA.
DR   PIR; C69017; C69017.
DR   PIR; T45150; T45150.
DR   RefSeq; WP_010876753.1; NC_000916.1.
DR   ProteinModelPortal; P21110; -.
DR   SMR; P21110; -.
DR   IntAct; P21110; 2.
DR   STRING; 187420.MTH1129; -.
DR   EnsemblBacteria; AAB85618; AAB85618; MTH_1129.
DR   GeneID; 1471537; -.
DR   KEGG; mth:MTH_1129; -.
DR   PATRIC; fig|187420.15.peg.1106; -.
DR   eggNOG; arCOG04857; Archaea.
DR   eggNOG; COG4058; LUCA.
DR   KO; K00399; -.
DR   OMA; VGHQPEY; -.
DR   OrthoDB; POG093Z00ZI; -.
DR   BioCyc; MetaCyc:MRTAMAUTO-MONOMER; -.
DR   BioCyc; MTHE187420:G1G16-1090-MONOMER; -.
DR   UniPathway; UPA00646; UER00699.
DR   Proteomes; UP000005223; 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   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Metal-binding;
KW   Methanogenesis; Methylation; Nickel; Reference proteome; Transferase.
FT   CHAIN         1    553       Methyl-coenzyme M reductase II subunit
FT                                alpha.
FT                                /FTId=PRO_0000147457.
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}.
FT   CONFLICT      6      6       L -> H (in Ref. 1; AAA73439).
FT                                {ECO:0000305}.
FT   CONFLICT     24     24       Y -> I (in Ref. 1; AAA73439).
FT                                {ECO:0000305}.
FT   CONFLICT    168    168       I -> V (in Ref. 1; AAA73439).
FT                                {ECO:0000305}.
FT   CONFLICT    200    200       K -> KEQLK (in Ref. 1). {ECO:0000305}.
SQ   SEQUENCE   553 AA;  60707 MW;  8A3511715F7EFE00 CRC64;
     MDEKKLFLTA LKKKFEVEDP DEKYTNFYCF GGWEQSARKK EFTEYAKKAA EKRGGIPFYN
     PDIGVPLGQR KLMAYRVSGT DAYVEGDDLH FVNNAAIQQM VDDIKRTVIV GMDTAHAVLE
     KRLGVEVTPE TINEYMEAIN HALPGGAVVQ EHMVEVHPGL VEDCYAKIFT GDDNLADELD
     KRILIDINKE FPEEQAEQLK SYIGNRTYQV NRVPTIVVRT CDGGTVSRWS AMQIGMSFIS
     AYKLCAGEAA IADFSYAAKH ADVIEMGTIM PARRARGPNE PGGVAFGTFA DIVQASRVSD
     DPAKISLEVI AGAAALYDQV WLGSYMSGGV GFTQYATAAY TDDILDDFVY YGMEYVDDKY
     GICGTKPTMD VVRDISTEVT LYSLEQYEEY PTLLEDHFGG SQRAAVAAAA AGCSTAFATG
     NSNAGINGWY LSQILHKEAH SRLGFYGYDL QDQCGASNSL SIRSDEGLIH ELRGPNYPNY
     AMNVGHQPEY AGIAQAPHAA RGDAFCTNPL IKVAFADKDL SFDFTSPRKS IAAGALREFM
     PEGERDLIIP AGK
//
DBGET integrated database retrieval system