ID   MTTC1_METAC             Reviewed;         216 AA.
AC   Q8TTA8;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Trimethylamine corrinoid protein 1;
DE            Short=TCP 1;
GN   Name=mttC1; OrderedLocusNames=MA_0529;
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; AAM03973.1; -; Genomic_DNA.
DR   RefSeq; WP_011020578.1; NC_003552.1.
DR   AlphaFoldDB; Q8TTA8; -.
DR   SMR; Q8TTA8; -.
DR   STRING; 188937.MA_0529; -.
DR   EnsemblBacteria; AAM03973; AAM03973; MA_0529.
DR   GeneID; 1472421; -.
DR   KEGG; mac:MA_0529; -.
DR   HOGENOM; CLU_082102_1_0_2; -.
DR   InParanoid; Q8TTA8; -.
DR   OMA; AKKFVQG; -.
DR   OrthoDB; 95903at2157; -.
DR   PhylomeDB; Q8TTA8; -.
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..216
FT                   /note="Trimethylamine corrinoid protein 1"
FT                   /id="PRO_0000216482"
FT   DOMAIN          1..92
FT                   /note="B12-binding N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00667"
FT   DOMAIN          94..216
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   216 AA;  23130 MW;  3914E4AD405F2EF8 CRC64;
     MASKEEIIAK AKDAITDFDE ELAAEVAEEA LAAGIDPVEL IEKGFTAGMQ EVGEQFEQGS
     LFLPHVLAAA EAMNTGMEVI KPEMEKRKSE TKSLGTVVIG TIEGDIHSIG KDIVASMLNI
     AGFKVVDLGR DVPIKTFVEK AKEVKPQIIA SSALMTTTMV NQIQIEEQLK EAGIRDQVKT
     MVGGAPVTQD WADKIGADLY GESATDVVSK VRAVLL