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Database: UniProt
Entry: A0A0F2S6T6_9FIRM
LinkDB: A0A0F2S6T6_9FIRM
Original site: A0A0F2S6T6_9FIRM 
ID   A0A0F2S6T6_9FIRM        Unreviewed;       267 AA.
AC   A0A0F2S6T6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Methyltetrahydrofolate:corrinoid methyltransferase {ECO:0000313|EMBL:KJS46624.1};
GN   ORFNames=VR66_24345 {ECO:0000313|EMBL:KJS46624.1};
OS   Peptococcaceae bacterium BRH_c23.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629714 {ECO:0000313|EMBL:KJS46624.1, ECO:0000313|Proteomes:UP000033503};
RN   [1] {ECO:0000313|EMBL:KJS46624.1, ECO:0000313|Proteomes:UP000033503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c23 {ECO:0000313|EMBL:KJS46624.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC       family. {ECO:0000256|ARBA:ARBA00010398}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJS46624.1}.
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DR   EMBL; LADV01000306; KJS46624.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2S6T6; -.
DR   PATRIC; fig|1629714.3.peg.4015; -.
DR   Proteomes; UP000033503; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR   InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR   PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:KJS46624.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KJS46624.1}.
FT   DOMAIN          1..267
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
SQ   SEQUENCE   267 AA;  29077 MW;  AEAB2FA19C3DAC92 CRC64;
     MLVVGELINA SRKAVGEAIK AQDAAYIQQV AKDEYEAGAD FIDVNAGIFV GKEPEYLQWL
     VKTVQEAVDA PCCIDSPDPK AIEAALSVHK GIAMINSISL EKERYNALIP VVAGTDLKVV
     ALCMSDEGMP ETMDARLRIA EKLIDGLVKN NVPLNNIYVD PLVQPVSTNS TFAVEFINSV
     EAIMTRFKGV HTICGLSNVS YGLPVRKFMN HAFAIMAIGK GLDGLIINPL DKMMMASLVT
     AEALAGRDDY CVKYLKAFRN KQFDFLG
//
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