ID   METF_BUCBP              Reviewed;         295 AA.
AC   Q89B13;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=5,10-methylenetetrahydrofolate reductase;
DE            EC=1.5.1.20;
GN   Name=metF; OrderedLocusNames=bbp_047;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-
CC         methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:19817, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:18608, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.20;
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=1.5.1.20;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC   -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family.
CC       {ECO:0000305}.
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DR   EMBL; AE016826; AAO26786.1; -; Genomic_DNA.
DR   RefSeq; WP_011091187.1; NC_004545.1.
DR   AlphaFoldDB; Q89B13; -.
DR   SMR; Q89B13; -.
DR   STRING; 224915.bbp_047; -.
DR   EnsemblBacteria; AAO26786; AAO26786; bbp_047.
DR   GeneID; 56470591; -.
DR   KEGG; bab:bbp_047; -.
DR   eggNOG; COG0685; Bacteria.
DR   HOGENOM; CLU_025841_0_0_6; -.
DR   OMA; EMHPQAR; -.
DR   OrthoDB; 1425269at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000601; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0106312; F:methylenetetrahydrofolate reductase NADH activity; IEA:RHEA.
DR   GO; GO:0106313; F:methylenetetrahydrofolate reductase NADPH 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   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR003171; Mehydrof_redctse-like.
DR   InterPro; IPR004620; MTHF_reductase_bac.
DR   Pfam; PF02219; MTHFR; 1.
DR   SUPFAM; SSF51730; SSF51730; 1.
DR   TIGRFAMs; TIGR00676; fadh2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; FAD; Flavoprotein; Methionine biosynthesis; NAD;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..295
FT                   /note="5,10-methylenetetrahydrofolate reductase"
FT                   /id="PRO_0000190260"
FT   ACT_SITE        28
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         28..33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..62
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..60
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         119..121
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         132..133
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..160
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         166..173
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   295 AA;  33770 MW;  D34F60F04D44AED3 CRC64;
     MKLVYKNYHE TLNQHLMNIC EKVNISFEFF PPNNILSEKN LWQVIDKLKL LTPKFFSVTH
     GTNSKIRATC TSNIVKKIKK YTGIETVPHL TCINSTEEEL KVIAKTYWDS GIRHILALRG
     DIFNTNCKPK IYAVDLIKLL KSIANFEISV AAYPEVHPEA VNAKYDIINL KRKVEAGATR
     AITQFFFNID CFLRFRDLCV KNNITIDIVP GIFPISNFKQ LLKFSSVSNV SIPKWLCCMF
     HGLDNDLNTS RIIGSSIAID MVKVLYSEGI RSFHFYTLNK SEISFAICKI LENKS