ID A0A1F8RKQ2_9CHLR Unreviewed; 304 AA.
AC A0A1F8RKQ2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Methyltetrahydrofolate--corrinoid methyltransferase {ECO:0000313|EMBL:OGO48222.1};
GN ORFNames=A2W37_14370 {ECO:0000313|EMBL:OGO48222.1};
OS Chloroflexi bacterium RBG_16_63_12.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797657 {ECO:0000313|EMBL:OGO48222.1, ECO:0000313|Proteomes:UP000176692};
RN [1] {ECO:0000313|EMBL:OGO48222.1, ECO:0000313|Proteomes:UP000176692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGO48222.1}.
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DR EMBL; MGNY01000076; OGO48222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8RKQ2; -.
DR STRING; 1797657.A2W37_14370; -.
DR Proteomes; UP000176692; 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:OGO48222.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OGO48222.1}.
FT DOMAIN 20..264
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT REGION 283..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 304 AA; 32306 MW; 9FB7F63AB76C6007 CRC64;
METLLTSPTQ EVRIGPDHPF VIIGERINPT GRKRLAAEMA AGNYDRVRND AFAQVAAGAH
VLDVNAGIPL ADEPAILAEA IRIVQSVVDA PLSIDSSIVK ALEAGLAAYQ GKPLVNSVTG
EEERLETVLP LVAQYKAAVI GISNDETGIS EDPDVRIAIA KKIVERAESY GIPRADVLID
PLAMPVGAVR YAGATLFKIV RRVREELGVN TICGASNISF GLPDRPTLNA AFIAMAIAAG
MTCAITNPLE PEIKKMILAA DVMMGHDENC SAWLKAHRAA REGGGEAAAG RATRRERRRT
ESAS
//
