MTGB_DESHY
ID MTGB_DESHY Reviewed; 479 AA.
AC Q24SP7;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Glycine betaine methyltransferase {ECO:0000303|PubMed:25313086};
DE Short=GB methyltransferase {ECO:0000303|PubMed:25313086};
DE EC=2.1.1.- {ECO:0000269|PubMed:25313086};
DE AltName: Full=Glycine betaine--corrinoid protein Co-methyltransferase {ECO:0000305|PubMed:25313086};
DE AltName: Full=Glycine betaine:cob(I)alamin methyltransferase {ECO:0000303|PubMed:25313086};
DE AltName: Full=Glycine betaine:corrinoid methyltransferase {ECO:0000303|PubMed:25313086};
GN Name=mtgB {ECO:0000303|PubMed:25313086};
GN OrderedLocusNames=DSY3156 {ECO:0000312|EMBL:BAE84945.1};
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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND INDUCTION.
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).
RN [3] {ECO:0007744|PDB:2QNE}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 4-479.
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of putative methyltransferase (ZP_00558420.1) from
RT Desulfitobacterium hafniense Y51 at 2.30 A resolution.";
RL Submitted (JUL-2007) to the PDB data bank.
CC -!- FUNCTION: Methyltransferase able to methylate free cob(I)alamin in
CC vitro, using glycine betaine as the methyl donor, yealding
CC methylcobalamin (methylCbl) and dimethylglycine. In vivo, probably
CC carries out the methylation of a corrinoid protein, likely the
CC adjacently encoded DSY3155, with glycine betaine, to then supply methyl
CC groups to tetrahydrofolate (THF) for ultimate conversion to carbon
CC dioxide; oxidation of the methyl group 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. Cannot use quaternary amines such as carnitine
CC and choline as substrates, nor tertiary amines such as dimethylglycine
CC or trimethylamine. {ECO:0000269|PubMed:25313086}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.96 mM for glycine betaine {ECO:0000269|PubMed:25313086};
CC Vmax=1.49 umol/min/mg enzyme for the methylation of free cob(I)alamin
CC with glycine betaine {ECO:0000269|PubMed:25313086};
CC -!- INDUCTION: Highly up-regulated during growth on glycine betaine.
CC {ECO:0000269|PubMed:25313086}.
CC -!- MISCELLANEOUS: In contrast to a small clade of this large protein
CC family whose members have trimethylamine:corrinoid methyltransferase
CC activity and have a genetically encoded pyrrolysine residue essential
CC for catalysis, MtgB lacks pyrrolysine and uses a quaternary amine as
CC substrate. {ECO:0000305|PubMed:25313086}.
CC -!- SIMILARITY: Belongs to the trimethylamine methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AP008230; BAE84945.1; -; Genomic_DNA.
DR PDB; 2QNE; X-ray; 2.30 A; A/B=4-479.
DR PDBsum; 2QNE; -.
DR AlphaFoldDB; Q24SP7; -.
DR SMR; Q24SP7; -.
DR STRING; 138119.DSY3156; -.
DR EnsemblBacteria; BAE84945; BAE84945; DSY3156.
DR KEGG; dsy:DSY3156; -.
DR eggNOG; COG5598; Bacteria.
DR HOGENOM; CLU_033581_0_0_9; -.
DR OMA; NQACIIS; -.
DR BRENDA; 2.1.1.376; 1880.
DR EvolutionaryTrace; Q24SP7; -.
DR Proteomes; UP000001946; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015948; P:methanogenesis; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.480; -; 1.
DR InterPro; IPR038601; MttB-like_sf.
DR InterPro; IPR010426; MTTB_MeTrfase.
DR Pfam; PF06253; MTTB; 1.
DR PIRSF; PIRSF037567; MTTB_MeTrfase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; One-carbon metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..479
FT /note="Glycine betaine methyltransferase"
FT /id="PRO_0000441377"
FT HELIX 13..29
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2QNE"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:2QNE"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 211..222
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:2QNE"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 243..264
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:2QNE"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 291..307
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 325..340
FT /evidence="ECO:0007829|PDB:2QNE"
FT STRAND 344..353
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 361..379
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 390..396
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 406..415
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 427..430
FT /evidence="ECO:0007829|PDB:2QNE"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 437..451
FT /evidence="ECO:0007829|PDB:2QNE"
FT HELIX 459..476
FT /evidence="ECO:0007829|PDB:2QNE"
SQ SEQUENCE 479 AA; 52577 MW; A93FB1A31004B02F CRC64;
MGQLLPKYNI LTEDQVQKIH ENTMKILEEI GIEFEYEPAL EVFRREGQKV EGKRVYLTRE
FVESKLKSAP AEFTLHARNP ENNVVIGGDN IVFMPGYGAP FIYELDGSRR KTTLQDYENF
AKLAGASKNM HLSGGTMAEP QDIPDGVRHL QMLYSSIKNS DKCFMGSAEG KERAEDSVEI
AAILFGGKDV IKEKPVLVSL INSLTPLKYD ERMLGALMAY AEAGQAVIIA SLVMAGSTGP
ASLAGTLSLQ NAEVLAGISL AQSINPGTPV IYGSTSALSD MRSGSLSIGS PECALFISAS
AQLARFYGVP SRSGGGLNDS KTVDAQAGYE SMMTLMAANL TGVNFVLHTA GILQYFMAMS
YEKFIMDDEI AGMLLHYMKG YTFDEDGMAF DVIEKVGPGG HFLTQKHTRK NHKREFYTPT
LSDRSAYDTW AKEKLETKQR AHARWQQILA NYVPPALDPE IDAKLQAFIA QRGKEVGEE
