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Database: UniProt
Entry: A0A1G1LTB2_9BACT
LinkDB: A0A1G1LTB2_9BACT
Original site: A0A1G1LTB2_9BACT 
ID   A0A1G1LTB2_9BACT        Unreviewed;       289 AA.
AC   A0A1G1LTB2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Methylenetetrahydrofolate reductase {ECO:0000256|RuleBase:RU003862};
DE            EC=1.5.1.54 {ECO:0000256|RuleBase:RU003862};
GN   ORFNames=A2Z88_01450 {ECO:0000313|EMBL:OGX07980.1};
OS   Omnitrophica WOR_2 bacterium GWA2_47_8.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1801840 {ECO:0000313|EMBL:OGX07980.1, ECO:0000313|Proteomes:UP000178620};
RN   [1] {ECO:0000313|EMBL:OGX07980.1, ECO:0000313|Proteomes:UP000178620}
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-
CC         methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH;
CC         Xref=Rhea:RHEA:19821, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:18608, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.5.1.54;
CC         Evidence={ECO:0000256|ARBA:ARBA00034420};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19823;
CC         Evidence={ECO:0000256|ARBA:ARBA00034420};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU003862};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway. {ECO:0000256|ARBA:ARBA00034478}.
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|RuleBase:RU003862}.
CC   -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family.
CC       {ECO:0000256|ARBA:ARBA00006743, ECO:0000256|RuleBase:RU003862}.
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:OGX07980.1}.
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DR   EMBL; MHFY01000054; OGX07980.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1LTB2; -.
DR   STRING; 1801840.A2Z88_01450; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000178620; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0106312; F:methylenetetrahydrofolate reductase NADH activity; IEA:RHEA.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00537; MTHFR; 1.
DR   Gene3D; 3.20.20.220; -; 1.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR003171; Mehydrof_redctse-like.
DR   InterPro; IPR004620; MTHF_reductase_bac.
DR   NCBIfam; TIGR00676; fadh2; 1.
DR   PANTHER; PTHR45754; METHYLENETETRAHYDROFOLATE REDUCTASE; 1.
DR   PANTHER; PTHR45754:SF3; METHYLENETETRAHYDROFOLATE REDUCTASE; 1.
DR   Pfam; PF02219; MTHFR; 1.
DR   SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003862};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003862};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003862}.
SQ   SEQUENCE   289 AA;  32816 MW;  2CB388B70D407809 CRC64;
     MKKLPDIFKT KEKTFSFELF PPKTEEGYQK LLTTVEQLCR LKPDFISCTY GAGGGNRDKT
     LDIVEHIQKK HNIISVAHLT CVLSTKEEIK NIITDIKNRG INNILALRGD PPKEQPDWQP
     GPDNFKYSSE LTAFIRKLFG PHFGIGVAGF PEGHILCRDK DRDAQYLKLK IDAGADFVIT
     QIFFDNTFYF EYIKRLKKLN VHARVIPGIL PITDYQSLLR FCALCGATVP QEVKRIFEPI
     QNDKDATLKE GINFAVRQCQ ELLKNGAPGI HFYCLNKLSP TDAILTAIR
//
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