ID   MTGC_DESHY              Reviewed;         216 AA.
AC   Q24SP8;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Corrinoid protein DSY3155 {ECO:0000303|PubMed:25313086};
GN   OrderedLocusNames=DSY3155 {ECO:0000312|EMBL:BAE84944.1};
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.
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: Probably harbors a corrinoid prosthetic group and acts as a
CC       methyl group carrier between MtgB and MtgA. A methyl group from glycine
CC       betaine is likely first transferred to the corrinoid prosthetic group
CC       of the enzyme by MtgB, and then transferred to tetrahydrofolate (THF)
CC       by MtgA. The methyl group may then be ultimately converted to carbon
CC       dioxide, and its oxidation would also provide reducing equivalents for
CC       anaerobic respiration. Thus, may function in the pathway that allows
CC       anaerobic methylotrophic growth of D.hafniense using glycine betaine.
CC       {ECO:0000305|PubMed:25313086}.
CC   -!- SIMILARITY: Belongs to the methylamine corrinoid protein family.
CC       {ECO:0000305}.
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DR   EMBL; AP008230; BAE84944.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q24SP8; -.
DR   SMR; Q24SP8; -.
DR   STRING; 138119.DSY3155; -.
DR   EnsemblBacteria; BAE84944; BAE84944; DSY3155.
DR   KEGG; dsy:DSY3155; -.
DR   eggNOG; COG5012; Bacteria.
DR   HOGENOM; CLU_082102_2_0_9; -.
DR   OMA; WADEIKA; -.
DR   BioCyc; MetaCyc:MON-21033; -.
DR   Proteomes; UP000001946; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProt.
DR   GO; GO:0015948; P:methanogenesis; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1240.10; -; 1.
DR   InterPro; IPR003759; Cbl-bd_cap.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR012741; Corrinoid_p.
DR   InterPro; IPR036594; Meth_synthase_dom.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF02607; B12-binding_2; 1.
DR   SMART; SM01018; B12-binding_2; 1.
DR   SUPFAM; SSF47644; SSF47644; 1.
DR   SUPFAM; SSF52242; SSF52242; 1.
DR   TIGRFAMs; TIGR02370; pyl_corrinoid; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS51337; B12_BINDING_NTER; 1.
PE   3: Inferred from homology;
KW   Cobalt; Metal-binding; One-carbon metabolism; Reference proteome.
FT   CHAIN           1..216
FT                   /note="Corrinoid protein DSY3155"
FT                   /id="PRO_0000441379"
FT   DOMAIN          1..90
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00667"
FT   DOMAIN          93..216
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT   BINDING         106
FT                   /ligand="methylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:28115"
FT                   /ligand_part="Co"
FT                   /ligand_part_id="ChEBI:CHEBI:27638"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:Q46EH4"
SQ   SEQUENCE   216 AA;  22943 MW;  7B628947B43EFE0B CRC64;
     MIMSLLDELK QAIIDGDEDI VAELSQKAVD EDLDLVDTVQ SGLVKGIEVV GTAWKEGEMF
     LPDVMMSAEA MKVGLAILEP EIAKKGMSEG ESKGKIVLGT VEGDIHDIGK NITGAMFTAA
     GYKVIDLGTD IKAEGFVAKA QEVGADIIGA SALLTTTMIK QKELIEYLKE KNLRDSYKVL
     VGGGPTSQVW ADEIGADGWA ETADDAVELA NKILGK