[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; DOI=10.1093/nar/11.19.6723; PubMed=6356036 [NCBI, ExPASy, EBI, Israel, Japan] Saint-Girons I., Duchange N., Zakin M.M., Park I., Margarita D., Ferrara P., Cohen G.N.; "Nucleotide sequence of metF, the E. coli structural gene for 5-10 methylene tetrahydrofolate reductase and of its control region."; Nucleic Acids Res. 11:6723-6732(1983).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/21.15.3391; PubMed=8346018 [NCBI, ExPASy, EBI, Israel, Japan] Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.; "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."; Nucleic Acids Res. 21:3391-3398(1993).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). DOI=10.1038/7594; PubMed=10201405 [NCBI, ExPASy, EBI, Israel, Japan] Guenther B.D., Sheppard C.A., Tran P., Rozen R., Matthews R.G., Ludwig M.L.; "The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia."; Nat. Struct. Biol. 6:359-365(1999).

Comments

CATALYTIC ACTIVITY: 5-methyltetrahydrofolate + NAD(P)⁺ = 5,10-methylenetetrahydrofolate + NAD(P)H.
COFACTOR: FAD.
PATHWAY: One-carbon metabolism; tetrahydrofolate pathway .
SUBUNIT: Homotetramer.
SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

V01502; CAA24747.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L19201; AAB03073.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76923.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77369.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A00462; RDECMH.

RefSeq

AP_003868.1; -.
NP_418376.1; -.

3D structure databases

PDB

1B5T; X-ray; 2.50 A; A/B/C=21-294.	[ExPASy / RCSB / EBI]
1ZP3; X-ray; 1.85 A; A/B/C=1-296.	[ExPASy / RCSB / EBI]
1ZP4; X-ray; 1.85 A; A/B/C=1-296.	[ExPASy / RCSB / EBI]
1ZPT; X-ray; 1.95 A; A/B/C=1-296.	[ExPASy / RCSB / EBI]
1ZRQ; X-ray; 2.20 A; A/B/C=1-296.	[ExPASy / RCSB / EBI]
2FMN; X-ray; 2.05 A; A/B/C=1-296.	[ExPASy / RCSB / EBI]
2FMO; X-ray; 2.25 A; A/B/C=1-296.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1B5T; -.
1ZP3; -.
1ZP4; -.
1ZPT; -.
1ZRQ; -.
2FMN; -.
2FMO; -.

ModBase

P0AEZ1.

Enzyme and pathway databases

BioCyc

EcoCyc:METHYLENETHFREDUCT-MON; -.
MetaCyc:METHYLENETHFREDUCT-MON; -.

Organism-specific databases

EchoBASE

EB0580; -.

EcoGene

EG10585; metF.

Ontologies

GO:0004489;	Molecular function: methylenetetrahydrofolate reductase (NADPH) activity (inferred from electronic annotation from InterPro).
GO:0009086;	Biological process: methionine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003171; Mehydrof_redctse.
IPR004620; MTHF_reductase_bac.
Graphical view of domain structure.

Pfam

PF02219; MTHFR; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00676; fadh2; 1.

Genome annotation databases

GeneID

948432; -.

GenomeReviews

AP009048_GR; JW3913.
U00096_GR; b3941.

KEGG

ecj:JW3913; -.
eco:b3941; -.

Phylogenomic databases

HOGENOM

P0AEZ1; -.

Other

LinkHub

P0AEZ1; -.

Genome annotation databases

CMR

P0AEZ1; b3941.

Other

ProtoNet

P0AEZ1.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Amino-acid biosynthesis; Complete proteome; FAD; Flavoprotein; Methionine biosynthesis; NAD; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 296`	`296`	`5,10-methylenetetrahydrofolate reductase.`	`PRO_0000190261`
`HELIX`	`5 17`	`13`
`STRAND`	`24 29`	`6`
`HELIX`	`35 49`	`15`
`STRAND`	`54 58`	`5`
`HELIX`	`67 80`	`14`
`STRAND`	`85 89`	`5`
`STRAND`	`91 93`	`3`
`HELIX`	`96 107`	`12`
`TURN`	`108 110`	`3`
`STRAND`	`113 116`	`4`
`HELIX`	`132 142`	`11`
`STRAND`	`146 151`	`6`
`HELIX`	`162 174`	`13`
`STRAND`	`179 182`	`4`
`HELIX`	`188 200`	`13`
`HELIX`	`217 227`	`11`
`HELIX`	`233 239`	`7`
`HELIX`	`246 266`	`21`
`STRAND`	`271 275`	`5`
`HELIX`	`281 289`	`9`

Sequence information

Length: 296 AA [This is the length of the unprocessed precursor]

Molecular weight: 33103 Da [This is the MW of the unprocessed precursor]

CRC64: B702702D2BE9521E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSFFHASQRD ALNQSLAEVQ GQINVSFEFF PPRTSEMEQT LWNSIDRLSS LKPKFVSVTY 

        70         80         90        100        110        120 
GANSGERDRT HSIIKGIKDR TGLEAAPHLT CIDATPDELR TIARDYWNNG IRHIVALRGD 

       130        140        150        160        170        180 
LPPGSGKPEM YASDLVTLLK EVADFDISVA AYPEVHPEAK SAQADLLNLK RKVDAGANRA 

       190        200        210        220        230        240 
ITQFFFDVES YLRFRDRCVS AGIDVEIIPG ILPVSNFKQA KKFADMTNVR IPAWMAQMFD 

       250        260        270        280        290 
GLDDDAETRK LVGANIAMDM VKILSREGVK DFHFYTLNRA EMSYAICHTL GVRPGL

P0AEZ1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools