ID   METF_ECOLI              Reviewed;         296 AA.
AC   P0AEZ1; P00394; Q2M8N7;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   16-JUN-2009, entry version 36.
DE   RecName: Full=5,10-methylenetetrahydrofolate reductase;
DE            EC=1.5.1.20;
GN   Name=metF; OrderedLocusNames=b3941, JW3913;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   MEDLINE=84041480; PubMed=6356036; DOI=10.1093/nar/11.19.6723;
RA   Saint-Girons I., Duchange N., Zakin M.M., Park I., Margarita D.,
RA   Ferrara P., Cohen G.N.;
RT   "Nucleotide sequence of metF, the E. coli structural gene for 5-10
RT   methylene tetrahydrofolate reductase and of its control region.";
RL   Nucleic Acids Res. 11:6723-6732(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=93347969; PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA   Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. III. DNA sequence of the
RT   region from 87.2 to 89.2 minutes.";
RL   Nucleic Acids Res. 21:3391-3398(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   MEDLINE=99215588; PubMed=10201405; DOI=10.1038/7594;
RA   Guenther B.D., Sheppard C.A., Tran P., Rozen R., Matthews R.G.,
RA   Ludwig M.L.;
RT   "The structure and properties of methylenetetrahydrofolate reductase
RT   from Escherichia coli suggest how folate ameliorates human
RT   hyperhomocysteinemia.";
RL   Nat. Struct. Biol. 6:359-365(1999).
CC   -!- CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)(+) = 5,10-
CC       methylenetetrahydrofolate + NAD(P)H.
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate pathway.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the methylenetetrahydrofolate reductase
CC       family.
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DR   EMBL; V01502; CAA24747.1; -; Genomic_DNA.
DR   EMBL; L19201; AAB03073.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76923.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77369.1; -; Genomic_DNA.
DR   PIR; A00462; RDECMH.
DR   RefSeq; AP_003868.1; -.
DR   RefSeq; NP_418376.1; -.
DR   PDB; 1B5T; X-ray; 2.50 A; A/B/C=21-294.
DR   PDB; 1ZP3; X-ray; 1.85 A; A/B/C=1-296.
DR   PDB; 1ZP4; X-ray; 1.85 A; A/B/C=1-296.
DR   PDB; 1ZPT; X-ray; 1.95 A; A/B/C=1-296.
DR   PDB; 1ZRQ; X-ray; 2.20 A; A/B/C=1-296.
DR   PDB; 2FMN; X-ray; 2.05 A; A/B/C=1-296.
DR   PDB; 2FMO; X-ray; 2.25 A; A/B/C=1-296.
DR   PDBsum; 1B5T; -.
DR   PDBsum; 1ZP3; -.
DR   PDBsum; 1ZP4; -.
DR   PDBsum; 1ZPT; -.
DR   PDBsum; 1ZRQ; -.
DR   PDBsum; 2FMN; -.
DR   PDBsum; 2FMO; -.
DR   GeneID; 948432; -.
DR   GenomeReviews; AP009048_GR; JW3913.
DR   GenomeReviews; U00096_GR; b3941.
DR   KEGG; ecj:JW3913; -.
DR   KEGG; eco:b3941; -.
DR   EchoBASE; EB0580; -.
DR   EcoGene; EG10585; metF.
DR   HOGENOM; P0AEZ1; -.
DR   OMA; P0AEZ1; FFPPKTP.
DR   BioCyc; EcoCyc:METHYLENETHFREDUCT-MON; -.
DR   BioCyc; MetaCyc:METHYLENETHFREDUCT-MON; -.
DR   GO; GO:0004489; F:methylenetetrahydrofolate reductase (NADPH)...; IEA:EC.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR003171; Mehydrof_redctse.
DR   InterPro; IPR004620; MTHF_reductase_bac.
DR   Pfam; PF02219; MTHFR; 1.
DR   TIGRFAMs; TIGR00676; fadh2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Complete proteome; FAD;
KW   Flavoprotein; Methionine biosynthesis; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    296       5,10-methylenetetrahydrofolate reductase.
FT                                /FTId=PRO_0000190261.
FT   HELIX         5     17
FT   STRAND       24     29
FT   HELIX        35     49
FT   STRAND       54     58
FT   HELIX        67     80
FT   STRAND       85     89
FT   STRAND       91     93
FT   HELIX        96    107
FT   TURN        108    110
FT   STRAND      113    116
FT   HELIX       132    142
FT   STRAND      146    151
FT   HELIX       162    174
FT   STRAND      179    182
FT   HELIX       188    200
FT   HELIX       217    227
FT   HELIX       233    239
FT   HELIX       246    266
FT   STRAND      271    275
FT   HELIX       281    289
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
//