P0AEZ1 (METF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
5,10-methylenetetrahydrofolate reductase
EC=1.5.1.20

Gene names

Name:	metF
Ordered Locus Names:	b3941, JW3913

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	296 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H.
Cofactor	FAD.
Pathway	One-carbon metabolism; tetrahydrofolate interconversion.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the methylenetetrahydrofolate reductase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Ligand	FAD Flavoprotein NAD NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate interconversion Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytosol Inferred from electronic annotation. Source: InterPro
Molecular_function	methylenetetrahydrofolate reductase (NADPH) activity Inferred from direct assay PubMed 9922232. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 296

296

5,10-methylenetetrahydrofolate reductase

PRO_0000190261

Secondary structure

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296

Helix Strand Turn

Details...

Helix

4 – 17

14

Turn

18 – 21

4

Beta strand

24 – 29

6

Helix

35 – 49

15

Beta strand

54 – 58

5

Helix

67 – 81

15

Beta strand

85 – 91

7

Helix

96 – 108

13

Beta strand

113 – 117

5

Beta strand

123 – 125

3

Helix

132 – 142

11

Beta strand

146 – 151

6

Helix

162 – 175

14

Beta strand

179 – 182

4

Helix

188 – 200

13

Beta strand

207 – 211

5

Helix

217 – 226

10

Helix

233 – 239

7

Helix

246 – 266

21

Beta strand

271 – 275

5

Helix

281 – 289

9

Sequences

	Sequence		Length	Mass (Da)
	P0AEZ1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: B702702D2BE9521E	FASTA	296	33,103
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of metF, the E. coli structural gene for 5-10 methylene tetrahydrofolate reductase and of its control region." Saint-Girons I., Duchange N., Zakin M.M., Park I., Margarita D., Ferrara P., Cohen G.N. Nucleic Acids Res. 11:6723-6732(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Plunkett G. III, Burland V., Daniels D.L., Blattner F.R. Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia." Guenther B.D., Sheppard C.A., Tran P., Rozen R., Matthews R.G., Ludwig M.L. Nat. Struct. Biol. 6:359-365(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V01502 Genomic DNA. Translation: CAA24747.1.
L19201 Genomic DNA. Translation: AAB03073.1.
U00096 Genomic DNA. Translation: AAC76923.1.
AP009048 Genomic DNA. Translation: BAE77369.1.

PIR

RDECMH. A00462.

RefSeq

NP_418376.1. NC_000913.2.
YP_491510.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B5T	X-ray	2.50	A/B/C	21-294	[»]
1ZP3	X-ray	1.85	A/B/C	1-296	[»]
1ZP4	X-ray	1.85	A/B/C	1-296	[»]
1ZPT	X-ray	1.95	A/B/C	1-296	[»]
1ZRQ	X-ray	2.20	A/B/C	1-296	[»]
2FMN	X-ray	2.05	A/B/C	1-296	[»]
2FMO	X-ray	2.25	A/B/C	1-296	[»]
3FST	X-ray	1.65	A/C/E	1-296	[»]
3FSU	X-ray	1.70	A/C/E	1-296	[»]

ProteinModelPortal

P0AEZ1.

SMR

P0AEZ1. Positions 21-295.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0AEZ1. 4 interactions.

STRING

511145.b3941.

Proteomic databases

PaxDb

P0AEZ1.

PRIDE

P0AEZ1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76923; AAC76923; b3941.
BAE77369; BAE77369; BAE77369.

GeneID

12934069.
948432.

KEGG

ecj:Y75_p3246.
eco:b3941.

PATRIC

32123403. VBIEscCol129921_4062.

Organism-specific databases

EchoBASE

EB0580.

EcoGene

EG10585. metF.

Phylogenomic databases

eggNOG

COG0685.

HOGENOM

HOG000246232.

KO

K00297.

OMA

SITQMFF.

ProtClustDB

PRK09432.

Enzyme and pathway databases

BioCyc

EcoCyc:METHYLENETHFREDUCT-MONOMER.
ECOL316407:JW3913-MONOMER.
MetaCyc:METHYLENETHFREDUCT-MONOMER.

UniPathway

UPA00193.

Gene expression databases

Genevestigator

P0AEZ1.

Family and domain databases

InterPro

IPR003171. Mehydrof_redctse.
IPR004620. MTHF_reductase_bac.
[Graphical view]

Pfam

PF02219. MTHFR. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00676. fadh2. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0AEZ1.

Entry information

Entry name

METF_ECOLI

Accession

Primary (citable) accession number: P0AEZ1
Secondary accession number(s): P00394, Q2M8N7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program