ID   MTBC2_METAC             Reviewed;         216 AA.
AC   Q8TS71;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Dimethylamine corrinoid protein 2;
GN   Name=mtbC2; OrderedLocusNames=MA_0934;
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: Acts as a methyl group carrier between MtbB and MtbA.
CC       {ECO:0000250}.
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from dimethylamine.
CC   -!- SIMILARITY: Belongs to the methylamine corrinoid protein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM04367.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE010299; AAM04367.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048065003.1; NC_003552.1.
DR   AlphaFoldDB; Q8TS71; -.
DR   SMR; Q8TS71; -.
DR   STRING; 188937.MA_0934; -.
DR   EnsemblBacteria; AAM04367; AAM04367; MA_0934.
DR   GeneID; 1472824; -.
DR   KEGG; mac:MA_0934; -.
DR   HOGENOM; CLU_082102_1_0_2; -.
DR   InParanoid; Q8TS71; -.
DR   OMA; TEIACRH; -.
DR   OrthoDB; 95903at2157; -.
DR   PhylomeDB; Q8TS71; -.
DR   UniPathway; UPA00644; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR   GO; GO:0008705; F:methionine synthase activity; IBA:GO_Central.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
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; Methanogenesis; Reference proteome; Repeat.
FT   CHAIN           1..216
FT                   /note="Dimethylamine corrinoid protein 2"
FT                   /id="PRO_0000216476"
FT   DOMAIN          1..91
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00667"
FT   DOMAIN          92..216
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT   BINDING         105
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"
SQ   SEQUENCE   216 AA;  23101 MW;  F18A97039F4B57FA CRC64;
     MASKEELLQE LSDAIVSCKK DRVIAAVEKA KEVMEPAEII EKGLAAGMNQ VGTLFERGKL
     FLPHVMMAAD SMTAGVNILE AEMPAGTETK KLGVIVNGTV EGDVHDIGKS IVSTMLQSAG
     FEVHDIGRDV PIKNFVEKAK EVNADMIGLS ALMTTTMQGQ RDVIELLKEE GMRERVKVMV
     GGAPATQAWA DKIGADCYAE NASEAVAKAK ELLLGK