MTGA_DESHY
ID MTGA_DESHY Reviewed; 306 AA.
AC Q24SP6;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Methylcorrinoid:tetrahydrofolate methyltransferase {ECO:0000303|PubMed:25313086};
DE EC=2.1.1.- {ECO:0000269|PubMed:25313086};
DE AltName: Full=Methylcobalamin:tetrahydrofolate methyltransferase {ECO:0000303|PubMed:25313086};
DE Short=MethylCbl:THF methyltransferase {ECO:0000303|PubMed:25313086};
GN Name=mtgA {ECO:0000303|PubMed:25313086};
GN OrderedLocusNames=DSY3157 {ECO:0000312|EMBL:BAE84946.1};
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51;
RX PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Y51;
RX PubMed=25313086; DOI=10.1073/pnas.1409642111;
RA Ticak T., Kountz D.J., Girosky K.E., Krzycki J.A., Ferguson D.J. Jr.;
RT "A nonpyrrolysine member of the widely distributed trimethylamine
RT methyltransferase family is a glycine betaine methyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E4668-E4676(2014).
CC -!- FUNCTION: Methyltransferase able to catalyze the transfer of a methyl
CC group from methylcobalamin (methylCbl) to tetrahydrofolate (THF) in
CC vitro, to generate methyl-THF and cob(I)alamin. In vivo, the methyl
CC group probably comes from the adjacently encoded methylated corrinoid
CC protein DSY3155. The methyl group may then be ultimately converted to
CC carbon dioxide, and its oxidation would also provide reducing
CC equivalents for anaerobic respiration. Thus, may function in the
CC pathway that allows anaerobic methylotrophic growth of D.hafniense
CC using glycine betaine. {ECO:0000269|PubMed:25313086}.
CC -!- SIMILARITY: Belongs to the MtrH family. {ECO:0000305}.
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DR EMBL; AP008230; BAE84946.1; -; Genomic_DNA.
DR RefSeq; WP_005816523.1; NC_007907.1.
DR PDB; 6SK4; X-ray; 1.55 A; A/B/C/D=2-306.
DR PDBsum; 6SK4; -.
DR AlphaFoldDB; Q24SP6; -.
DR SMR; Q24SP6; -.
DR STRING; 138119.DSY3157; -.
DR EnsemblBacteria; BAE84946; BAE84946; DSY3157.
DR KEGG; dsy:DSY3157; -.
DR eggNOG; COG1962; Bacteria.
DR HOGENOM; CLU_048697_0_0_9; -.
DR OMA; YARHKIV; -.
DR OrthoDB; 898687at2; -.
DR BRENDA; 2.1.1.378; 1880.
DR Proteomes; UP000001946; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.20; -; 1.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR InterPro; IPR023467; MeTrfase_MtrH/MtxH.
DR Pfam; PF02007; MtrH; 1.
DR PIRSF; PIRSF004960; MtrH_MtxH; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; One-carbon metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..306
FT /note="Methylcorrinoid:tetrahydrofolate methyltransferase"
FT /id="PRO_0000441378"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:6SK4"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:6SK4"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:6SK4"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:6SK4"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6SK4"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:6SK4"
FT HELIX 51..68
FT /evidence="ECO:0007829|PDB:6SK4"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:6SK4"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:6SK4"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:6SK4"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:6SK4"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:6SK4"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:6SK4"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:6SK4"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6SK4"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:6SK4"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:6SK4"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:6SK4"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:6SK4"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:6SK4"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:6SK4"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:6SK4"
FT HELIX 242..256
FT /evidence="ECO:0007829|PDB:6SK4"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:6SK4"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:6SK4"
FT HELIX 270..286
FT /evidence="ECO:0007829|PDB:6SK4"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:6SK4"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:6SK4"
SQ SEQUENCE 306 AA; 33459 MW; 5922881E7E848D37 CRC64;
MFKFTAQQHV YDINGVKVGG QPGEYPTVLI GSIFYRGHKI VSDGQKGIFD KDAAKALLDQ
EAELSAETGN PFIIDVLGES VEALTKYVEF ILENTTAPFL LDSISPDVRV GALKNLGKDP
EIQKRLIYNS IEEHYTEEEL AAIKEAGLKT AVILAFSKKA LKPNARIDLL QGKDDKEGLI
AAAKRAGIEQ FLVDPGVLDV ASNSWTTEAI NVVKEQFGYP GGCAPSNAVY LWKKMRSKGT
PFFEVAGAAV FTYPITQGAD FILYGPMMNA PWVYRAIATT DAMIAYNNKL TGVKMGTTEH
PLLKIF
