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MTTB1_METMA
ID   MTTB1_METMA             Reviewed;         495 AA.
AC   P58973;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   23-FEB-2022, entry version 99.
DE   RecName: Full=Trimethylamine methyltransferase MttB1;
DE            Short=TMA methyltransferase 1;
DE            EC=2.1.1.250;
DE   AltName: Full=Trimethylamine--corrinoid protein methyltransferase 1;
GN   Name=mttB1; OrderedLocusNames=MM_1688/MM_1689;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM31384.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAM31385.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE008384; AAM31384.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AE008384; AAM31385.1; ALT_SEQ; Genomic_DNA.
DR   STRING; 192952.MM_1688; -.
DR   EnsemblBacteria; AAM31384; AAM31384; MM_1688.
DR   EnsemblBacteria; AAM31385; AAM31385; MM_1689.
DR   KEGG; mma:MM_1688; -.
DR   KEGG; mma:MM_1689; -.
DR   PATRIC; fig|192952.21.peg.1958; -.
DR   eggNOG; arCOG03406; Archaea.
DR   HOGENOM; CLU_841265_0_0_2; -.
DR   BRENDA; 2.1.1.250; 3270.
DR   UniPathway; UPA00645; -.
DR   Proteomes; UP000000595; Chromosome.
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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..495
FT                   /note="Trimethylamine methyltransferase MttB1"
FT                   /id="PRO_0000216574"
FT   NON_STD         334
FT                   /note="Pyrrolysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   495 AA;  53853 MW;  C0797CD6AD40CD04 CRC64;
     MAKCNAVAGF NALNGVQLNL FTTDELKAIH YATMEVLMDP GIQVSDPEAR QIFKENGCEV
     NEQTNVVKIP EYLVRRALQL APSRFVLWGR DKKYNTVQEA GGKVHWTCFG TGVKMCKYQE
     GKYVTVDSVE QDIADIAKLC DWAENIDYFS LPVSARDIAG QGAQDVHETF TPLTNTAKHF
     HHIDPVGENV EYYRDIVNAY YGGDEEEARK KPIFSMLLCP TSPLELSVNA CQVIIKGARF
     GMPVNVLSMA MSGGSSPVYL AGTLVTHNAE VLAGITLAQL TVPGAKVWYG SSTTTFDLKK
     GTAPVGSPEL GLISASVAKL AQFYGLPAFV AGTOSDAKIP DNQAGHEKTM TCLLPALAGA
     NTLYGAGMLE LGMTFSMEQL VIDNDIIKMT KKALQGVPVN EETLAVESIQ KVGIGNNFLA
     LKQTRQLVNY PSDPMLIDRR MFGDWAAAGS KDLAAAAHEK VVDVLKNHVV KPIDADILKD
     MKAVVDKADK AFRGM
 
 
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