ID   MTBC_METBA              Reviewed;         213 AA.
AC   O93657;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Dimethylamine corrinoid protein;
GN   Name=mtbC {ECO:0000303|PubMed:10762254};
OS   Methanosarcina barkeri.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2208;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, AND INDUCTION BY
RP   TRIMETHYLAMINE.
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   PubMed=10762254; DOI=10.1128/jb.182.9.2520-2529.2000;
RA   Paul L., Ferguson D.J. Jr., Krzycki J.A.;
RT   "The trimethylamine methyltransferase gene and multiple dimethylamine
RT   methyltransferase genes of Methanosarcina barkeri contain in-frame and
RT   read-through amber codons.";
RL   J. Bacteriol. 182:2520-2529(2000).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-16, FUNCTION, AND SUBUNIT.
RC   STRAIN=ATCC 43569 / MS / DSM 800 / JCM 10043 / NBRC 100474;
RX   PubMed=10852929; DOI=10.1074/jbc.m910218199;
RA   Ferguson D.J. Jr., Gorlatova N., Grahame D.A., Krzycki J.A.;
RT   "Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete
RT   corrinoid protein and two methyltransferases purified from Methanosarcina
RT   barkeri.";
RL   J. Biol. Chem. 275:29053-29060(2000).
CC   -!- FUNCTION: Acts as a methyl group carrier between MtbB1 and MtbA. Binds
CC       1 corrinoid cofactor per protein, is subsequently demethylated by MtbA.
CC       {ECO:0000269|PubMed:10852929}.
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from dimethylamine.
CC       {ECO:0000305|PubMed:10762254}.
CC   -!- SUBUNIT: Copurifies with MtbA. {ECO:0000269|PubMed:10852929}.
CC   -!- INDUCTION: Induced by growth on trimethylamine but not methanol or
CC       monomethylamine. Part of the mtbC-mttB-mttC and mtbC-mttB-mttC-mttP-
CC       mtbB1 operons. {ECO:0000269|PubMed:10762254}.
CC   -!- SIMILARITY: Belongs to the methylamine corrinoid protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF102623; AAD14629.1; -; Genomic_DNA.
DR   AlphaFoldDB; O93657; -.
DR   SMR; O93657; -.
DR   BioCyc; MetaCyc:MON-12211; -.
DR   UniPathway; UPA00644; -.
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: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   1: Evidence at protein level;
KW   Cobalt; Direct protein sequencing; Metal-binding; Methanogenesis; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10852929"
FT   CHAIN           2..213
FT                   /note="Dimethylamine corrinoid protein"
FT                   /id="PRO_0000216473"
FT   DOMAIN          1..90
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00667"
FT   DOMAIN          91..213
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00666"
FT   BINDING         104
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   213 AA;  22504 MW;  592DE5FA496FE093 CRC64;
     MSKEELLQEL ADAIISCKKD TVLAVVEKAK GELEPSEIIE KGLAAGMNEV GVRFERGKLF
     LPHVMMAADA MTAGVAALKD LMPEGASGSK LGVIVNGTVE GDVHDIGKAI VSTMLQSAGF
     EVHDIGRDVP IRNFIEKAKE VNADMIGISA LMTTTLQGQK SVIELLKEEG LRDKVKVMVG
     GAPATQAWAD KIGADCYAEN ATEAVAKAKE LLA