[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-36, FUNCTION, AND SUBUNIT. PubMed=1748668 [NCBI, ExPASy, EBI, Israel, Japan] D'Ari L., Rabinowitz J.C.; "Purification, characterization, cloning, and amino acid sequence of the bifunctional enzyme 5,10-methylenetetrahydrofolate dehydrogenase/5,10-methenyltetrahydrofolate cyclohydrolase from Escherichia coli."; J. Biol. Chem. 266:23953-23958(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; Yonetani Y., Sanpei G., Mizobuchi K.; "Cloning and nucleotide sequence analysis of a novel adenine-sensitive mutation of Escherichia coli strain K-12 W3110."; Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; "Sequence of minutes 4-25 of Escherichia coli."; Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]	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).
[5]	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).
[6]	X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS), AND SUBUNIT. PubMed=10386884 [NCBI, ExPASy, EBI, Israel, Japan] Shen B.W., Dyer D.H., Huang J.-Y., D'Ari L., Rabinowitz J., Stoddard B.L.; "The crystal structure of a bacterial, bifunctional 5,10 methylene-tetrahydrofolate dehydrogenase/cyclohydrolase."; Protein Sci. 8:1342-1349(1999).

Comments

FUNCTION: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. This enzyme is specific for NADP.
CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + NADP⁺ = 5,10-methenyltetrahydrofolate + NADPH.
CATALYTIC ACTIVITY: 5,10-methenyltetrahydrofolate + H₂O = 10-formyltetrahydrofolate.
PATHWAY: One-carbon metabolism; tetrahydrofolate pathway .
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase 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

M74789; AAA23803.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D10588; BAA01445.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U82664; AAB40282.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73631.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76306.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

H64784; JS0662.

RefSeq

AP_001176.1; -.
NP_415062.1; -.

3D structure databases

PDB

1B0A; X-ray; 2.56 A; A=1-288.

[ExPASy / RCSB / EBI]

PDBsum

1B0A; -.

ModBase

P24186.

Enzyme and pathway databases

BioCyc

EcoCyc:FOLD-MON; -.
MetaCyc:FOLD-MON; -.

Organism-specific databases

EchoBASE

EB0324; -.

EcoGene

EG10328; folD.

Ontologies

GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004477;	Molecular function: methenyltetrahydrofolate cyclohydrolase activity (inferred from electronic annotation from HAMAP).
GO:0004488;	Molecular function: methylenetetrahydrofolate dehydrogenase (NADP+) activity (inferred from electronic annotation from HAMAP).
GO:0009396;	Biological process: folic acid and derivative biosynthetic process (inferred from electronic annotation from InterPro).
GO:0000105;	Biological process: histidine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0009086;	Biological process: methionine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0006730;	Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006164;	Biological process: purine nucleotide biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01576; -; 1.
PBIL [Tree]

InterPro

IPR016040; NAD(P)-bd.
IPR000672; THF_DHase/CycOHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF00763; THF_DHG_CYH; 1.
PF02882; THF_DHG_CYH_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00085; THFDHDRGNASE.

ProDom

PD002300; THFDhg/Cyc_hydro; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00766; THF_DHG_CYH_1; 1.
PS00767; THF_DHG_CYH_2; 1.

ProtoNet

P24186.

Genome annotation databases

GeneID

945221; -.

GenomeReviews

U00096_GR; b0529.
AP009048_GR; JW0518.

KEGG

ecj:JW0518; -.
eco:b0529; -.

Phylogenomic databases

HOGENOM

P24186; -.

Genome annotation databases

CMR

P24186; b0529.

Other

UniRef

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

Keywords

3D-structure; Amino-acid biosynthesis; Complete proteome; Direct protein sequencing; Histidine biosynthesis; Hydrolase; Methionine biosynthesis; Multifunctional enzyme; NADP; One-carbon metabolism; Oxidoreductase; Purine biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 288`	`287`	`Bifunctional protein folD.`	`PRO_0000199306`
`CONFLICT`	`47 47`		`S -> L (in Ref. 3; AAB40282).`
`CONFLICT`	`200 200`		`V -> L (in Ref. 1; AAA23803).`
`HELIX`	`8 28`	`21`
`STRAND`	`35 42`	`8`
`HELIX`	`45 61`	`17`
`STRAND`	`68 70`	`3`
`HELIX`	`76 87`	`12`
`STRAND`	`94 97`	`4`
`HELIX`	`107 111`	`5`
`TURN`	`116 118`	`3`
`HELIX`	`125 132`	`8`
`HELIX`	`141 152`	`12`
`STRAND`	`161 165`	`5`
`TURN`	`169 171`	`3`
`HELIX`	`172 180`	`9`
`TURN`	`181 183`	`3`
`STRAND`	`185 189`	`5`
`HELIX`	`196 202`	`7`
`STRAND`	`204 208`	`5`
`TURN`	`218 220`	`3`
`STRAND`	`226 229`	`4`
`HELIX`	`246 252`	`7`
`STRAND`	`254 256`	`3`
`STRAND`	`259 263`	`5`
`HELIX`	`264 281`	`18`

Sequence information

Length: 288 AA [This is the length of the unprocessed precursor]

Molecular weight: 31044 Da [This is the MW of the unprocessed precursor]

CRC64: 028039D7C611085D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAKIIDGKT IAQQVRSEVA QKVQARIAAG LRAPGLAVVL VGSNPASQIY VASKRKACEE 

        70         80         90        100        110        120 
VGFVSRSYDL PETTSEAELL ELIDTLNADN TIDGILVQLP LPAGIDNVKV LERIHPDKDV 

       130        140        150        160        170        180 
DGFHPYNVGR LCQRAPRLRP CTPRGIVTLL ERYNIDTFGL NAVVIGASNI VGRPMSMELL 

       190        200        210        220        230        240 
LAGCTTTVTH RFTKNLRHHV ENADLLIVAV GKPGFIPGDW IKEGAIVIDV GINRLENGKV 

       250        260        270        280 
VGDVVFEDAA KRASYITPVP GGVGPMTVAT LIENTLQACV EYHDPQDE

P24186 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