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MTTB_METTE
ID   MTTB_METTE              Reviewed;         483 AA.
AC   Q9P995;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 4.
DT   23-FEB-2022, entry version 50.
DE   RecName: Full=Trimethylamine methyltransferase MttB;
DE            Short=TMA methyltransferase;
DE            EC=2.1.1.250;
DE   AltName: Full=Trimethylamine--corrinoid protein methyltransferase;
DE   Flags: Fragment;
GN   Name=mttB;
OS   Methanosarcina thermophila.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2210;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / TM-1;
RX   PubMed=10762254; DOI=10.1128/jb.182.9.2520-2529.2000;
RA   Paul L., Ferguson D.J. Jr., Krzycki J.A.;
RT   "The trimethylamine methyltransferase gene and multiple dimethylamine
RT   methyltransferase genes of Methanosarcina barkeri contain in-frame and
RT   read-through amber codons.";
RL   J. Bacteriol. 182:2520-2529(2000).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from trimethylamine
CC       to the corrinoid cofactor of MttC. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Co(I)-[trimethylamine-specific corrinoid protein] + H(+) +
CC         trimethylamine = dimethylamine + methyl-Co(III)-[trimethylamine-
CC         specific corrinoid protein]; Xref=Rhea:RHEA:39287, Rhea:RHEA-
CC         COMP:11124, Rhea:RHEA-COMP:11126, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58040, ChEBI:CHEBI:58389, ChEBI:CHEBI:85033,
CC         ChEBI:CHEBI:85035; EC=2.1.1.250;
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from trimethylamine.
CC   -!- SUBUNIT: Can form a complex with MttC. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the trimethylamine methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF153452; AAD38789.1; -; Genomic_DNA.
DR   BRENDA; 2.1.1.250; 3281.
DR   UniPathway; UPA00645; -.
DR   GO; GO:0043834; F:trimethylamine methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.480; -; 1.
DR   InterPro; IPR038601; MttB-like_sf.
DR   InterPro; IPR012740; MttB_Methanosar.
DR   InterPro; IPR010426; MTTB_MeTrfase.
DR   Pfam; PF06253; MTTB; 1.
DR   PIRSF; PIRSF037567; MTTB_MeTrfase; 1.
DR   TIGRFAMs; TIGR02369; trimeth_pyl; 1.
PE   3: Inferred from homology;
KW   Methanogenesis; Methyltransferase; Pyrrolysine; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..>483
FT                   /note="Trimethylamine methyltransferase MttB"
FT                   /id="PRO_0000216571"
FT   NON_STD         334
FT                   /note="Pyrrolysine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         483
SQ   SEQUENCE   483 AA;  52555 MW;  3D066D65411BF225 CRC64;
     MAKTNAVAGF NALNGVELNL FTNEELKAIH YATMEVLMNP GVQVSDPEAR QIFKENGCEV
     DEETKVVKIP EYIVRKALQL APSRFVLWGR DKKYNTVQEC GGKVHWTCFG TGVKMCKYQD
     GKYVTVDSVE QDIADIAKLC DWAENIDYFS LPVSARDVAG QGAQDVHETF TPIVNTSKHY
     HHIDPVGENV EYYWDIVKAY YGGDEEEARK KPIFSMLLCP TSPLELSVNA CQVIIKGARL
     GIPVNVLSMA MSGGSSPVYL AGTLVTHNAE VLSGIVLAQL TAPGSKVWYG SSTTTFDLKK
     GTAPVGSPEL GLISAAVAKL AQFYGLPSFV AGSOSDAKIP DSQAGHEKTI TTLLPALAGA
     NTIYGAGMLE LGMTFSMEQL VIDNDIISMV KKAMEGIPVS EETLSVESIQ KVGIGNNFLA
     LKQTRQLIDY PSSPMLIDRR MYGDWAASGS KDLAAVAHEK VVDVLKNHQV KPIDADILKD
     MQA
 
 
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