MTTC2_METMA
ID MTTC2_METMA Reviewed; 218 AA.
AC P58983;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Trimethylamine corrinoid protein 2;
DE Short=TCP 2;
GN Name=mttC2; OrderedLocusNames=MM_2047;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(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; AE008384; AAM31743.1; -; Genomic_DNA.
DR RefSeq; WP_011033979.1; NC_003901.1.
DR AlphaFoldDB; P58983; -.
DR SMR; P58983; -.
DR STRING; 192952.MM_2047; -.
DR EnsemblBacteria; AAM31743; AAM31743; MM_2047.
DR GeneID; 44088323; -.
DR GeneID; 66136476; -.
DR KEGG; mma:MM_2047; -.
DR PATRIC; fig|192952.21.peg.2349; -.
DR eggNOG; arCOG02028; Archaea.
DR HOGENOM; CLU_082102_1_0_2; -.
DR OMA; MAGKEEI; -.
DR UniPathway; UPA00645; -.
DR Proteomes; UP000000595; Chromosome.
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 3: Inferred from homology;
KW Cobalt; Metal-binding; Methanogenesis; Reference proteome; Repeat.
FT CHAIN 1..218
FT /note="Trimethylamine corrinoid protein 2"
FT /id="PRO_0000216485"
FT DOMAIN 1..92
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00667"
FT DOMAIN 94..218
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 218 AA; 23065 MW; B342159B1FC01C03 CRC64;
MAGKEEIIAK AKNSITEFDE ELAAEVAEEA LAAGVDPVEL IEKGFTAGME EVGEQFGQGA
LFLPHVLAAA EAMKAGIEVI TPEMEKRKSQ TKNLGTVIIG TIEGDIHSIG KDIVASMLNI
AGFKVVDLGR DVAIKTFVEK VKELKPQVVA SSALMTTTMV NQIQIEEQLK EAGVRDQVKT
MVGGAPVTQD WADKIGADIY GESANDAVAK VKAALKVG
