METF_SHIFL
ID METF_SHIFL Reviewed; 296 AA.
AC P0AEZ2; P00394;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=5,10-methylenetetrahydrofolate reductase;
DE EC=1.5.1.20;
GN Name=metF; OrderedLocusNames=SF4019, S3728;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family.
CC {ECO:0000305}.
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DR EMBL; AE005674; AAN45452.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18748.1; -; Genomic_DNA.
DR RefSeq; NP_709745.1; NC_004337.2.
DR RefSeq; WP_000007523.1; NZ_WPGW01000012.1.
DR AlphaFoldDB; P0AEZ2; -.
DR SMR; P0AEZ2; -.
DR STRING; 198214.SF4019; -.
DR PRIDE; P0AEZ2; -.
DR EnsemblBacteria; AAN45452; AAN45452; SF4019.
DR EnsemblBacteria; AAP18748; AAP18748; S3728.
DR GeneID; 1027371; -.
DR GeneID; 66672148; -.
DR KEGG; sfl:SF4019; -.
DR KEGG; sfx:S3728; -.
DR PATRIC; fig|198214.7.peg.4736; -.
DR HOGENOM; CLU_025841_0_0_6; -.
DR OMA; EMHPQAR; -.
DR OrthoDB; 1425269at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..296
FT /note="5,10-methylenetetrahydrofolate reductase"
FT /id="PRO_0000190265"
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 88
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 118..120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131..132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 156..159
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 165..172
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 296 AA; 33103 MW; B702702D2BE9521E CRC64;
MSFFHASQRD ALNQSLAEVQ GQINVSFEFF PPRTSEMEQT LWNSIDRLSS LKPKFVSVTY
GANSGERDRT HSIIKGIKDR TGLEAAPHLT CIDATPDELR TIARDYWNNG IRHIVALRGD
LPPGSGKPEM YASDLVTLLK EVADFDISVA AYPEVHPEAK SAQADLLNLK RKVDAGANRA
ITQFFFDVES YLRFRDRCVS AGIDVEIIPG ILPVSNFKQA KKFADMTNVR IPAWMAQMFD
GLDDDAETRK LVGANIAMDM VKILSREGVK DFHFYTLNRA EMSYAICHTL GVRPGL
