ID   MTTC2_METAC             Reviewed;         217 AA.
AC   Q8TS74;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Trimethylamine corrinoid protein 2;
DE            Short=TCP 2;
GN   Name=mttC2; OrderedLocusNames=MA_0931;
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 probably as a methyl group carrier between MttB and
CC       either MtbA or MtaA. {ECO:0000250}.
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from trimethylamine.
CC   -!- SUBUNIT: Can form a complex with MttB. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methylamine corrinoid protein family.
CC       {ECO:0000305}.
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DR   EMBL; AE010299; AAM04364.1; -; Genomic_DNA.
DR   RefSeq; WP_011020969.1; NC_003552.1.
DR   AlphaFoldDB; Q8TS74; -.
DR   SMR; Q8TS74; -.
DR   STRING; 188937.MA_0931; -.
DR   EnsemblBacteria; AAM04364; AAM04364; MA_0931.
DR   GeneID; 1472821; -.
DR   KEGG; mac:MA_0931; -.
DR   HOGENOM; CLU_082102_1_0_2; -.
DR   InParanoid; Q8TS74; -.
DR   OMA; MAGKEEI; -.
DR   OrthoDB; 95903at2157; -.
DR   PhylomeDB; Q8TS74; -.
DR   UniPathway; UPA00645; -.
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..217
FT                   /note="Trimethylamine corrinoid protein 2"
FT                   /id="PRO_0000216483"
FT   DOMAIN          1..92
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00667"
FT   DOMAIN          94..217
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT   BINDING         107
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   217 AA;  23118 MW;  78CE5C16CB38874A CRC64;
     MAGKEEIIAK AKDSITEFDE EMAQEAANEA LVAGLDPVEI IEHGYTAGMQ YVGDQFEQGT
     LFLPHVLAAA EAMKAGIEVL QPEMEKRKAK TTTLGTVIIG TIEGDIHSIG KDIVASMLNI
     AGFEVVDLGR DVAIKTFVEK AKELKPDIVA TSALMTTTMV NQIQLEEQLK EAGIRGQVKT
     MVGGAPVTQG WADKIGADIY GESATDAVNK IKAAIKS