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MTTB1_METAC
ID   MTTB1_METAC             Reviewed;         495 AA.
AC   Q8TTA9;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 4.
DT   23-FEB-2022, entry version 88.
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=MA_0528;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(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}.
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DR   EMBL; AE010299; AAM03972.1; -; Genomic_DNA.
DR   STRING; 188937.MA_0528; -.
DR   KEGG; mac:MA_0528; -.
DR   HOGENOM; CLU_033581_1_0_2; -.
DR   InParanoid; Q8TTA9; -.
DR   UniPathway; UPA00645; -.
DR   Proteomes; UP000002487; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..495
FT                   /note="Trimethylamine methyltransferase MttB1"
FT                   /id="PRO_0000216572"
FT   NON_STD         334
FT                   /note="Pyrrolysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   495 AA;  53838 MW;  11766FE64BBCC23C CRC64;
     MAKNNAVAGF NALNGVELNL FTTDELKAIH YATMDVLMNP GVQVSDPEAR QIFKENGCEV
     DEKTNVVKIP EYLVRRALQL APSRFVLWGR DKKFNTVQEC GGKVHWTCFG TGVKMCKYQD
     GKYVTVDSVE QDIADIAKLC DWAENIDYFS LPVSARDIAG QGAQDVHETL TPIANTAKHY
     HHIDPVGENV EYYRDIVTAY YGGDEEEARK KPIFSMLLCP TSPLELSVNA CQVIIKGARF
     GMPVNVLSMA MSGGSSPVYL AGTLVTHNAE VLAGITLAQL TVPGTKVWYG SSTTTFDLKK
     GTAPVGSPEL GLISASVAKL AQFYGLPAFV AGTOSDAKIP DNQAGHEKTM TCLLPALAGA
     NTLYGAGMLE LGMTFSMEQL VIDNDIIKMT KKALQGVPVN EETLAVESIQ KVGIGNNFLA
     LKQTRQLVNY PSDPMLIDRR MFGDWAAAGS KDLASAAHDK VVDVLKNHVV KPIDADILKD
     MQAVVDRADK AFRGM
 
 
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