ID   MTMC2_METAC             Reviewed;         217 AA.
AC   P58868;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Monomethylamine corrinoid protein 2;
DE            Short=MMCP 2;
GN   Name=mtmC2; OrderedLocusNames=MA_2971;
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 MtmB and MtbA.
CC       {ECO:0000250}.
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from methylamine.
CC   -!- SUBUNIT: Can form a complex with MtmB. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methylamine corrinoid protein family.
CC       {ECO:0000305}.
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DR   EMBL; AE010299; AAM06344.1; -; Genomic_DNA.
DR   RefSeq; WP_011022912.1; NC_003552.1.
DR   AlphaFoldDB; P58868; -.
DR   SMR; P58868; -.
DR   STRING; 188937.MA_2971; -.
DR   EnsemblBacteria; AAM06344; AAM06344; MA_2971.
DR   GeneID; 1474865; -.
DR   KEGG; mac:MA_2971; -.
DR   HOGENOM; CLU_082102_1_0_2; -.
DR   InParanoid; P58868; -.
DR   OMA; LMCAKAM; -.
DR   OrthoDB; 84994at2157; -.
DR   PhylomeDB; P58868; -.
DR   UniPathway; UPA00643; -.
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="Monomethylamine corrinoid protein 2"
FT                   /id="PRO_0000216470"
FT   DOMAIN          1..91
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00667"
FT   DOMAIN          93..217
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"
SQ   SEQUENCE   217 AA;  23273 MW;  C235EF2ADF2CF55D CRC64;
     MTNTEIFEKL TNAIVTQNIA GCVQLTQEAL DAGIPPIDII TKGLSPGMKI IGDKFEAAEI
     FLPQIMMSAK AMSSAMEILT PELEKSKVEG EETGLAITFV AEGDIHDIGH RLVTTMLGAN
     GFEILDLGVD VLNENVVEEA AKHKGQKVIL VGSALMTTSM LGQKDLMDRL REEKLRDSLK
     CMFGGAPVSS KWIEEIGADA TAENAAEAAK VALNIMK