FUNCTION: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate (By similarity).
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 (By similarity).
SIMILARITY: Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

Copyright

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Cross-references

Sequence databases

EMBL

CP000699; ABQ68423.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001262561.1; -.

3D structure databases

ModBase

A5V807.

Ontologies

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).
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; FALSE_NEG.
PS00767; THF_DHG_CYH_2; 1.

BLOCKS

A5V807.

Genome annotation databases

GeneID

5197607; -.

GenomeReviews

CP000699_GR; Swit_2064.

KEGG

swi:Swit_2064; -.

NMPDR

fig|392499.4.peg.2303; -.

CMR

A5V807; Swit_2064.

Other

ProtoNet

A5V807.

UniRef

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

Keywords

Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; Hydrolase; Methionine biosynthesis; Multifunctional enzyme; NADP; One-carbon metabolism; Oxidoreductase; Purine biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 297`	`297`		`Bifunctional protein folD 2.`	`PRO_0000340600`

Sequence information

Length: 297 AA [This is the length of the unprocessed precursor]

Molecular weight: 30943 Da [This is the MW of the unprocessed precursor]

CRC64: 08CA8ECBA19B597A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAPSHAAHDS AATAHRIDGR AIARSLDERT AAAVRAIVAR DGAPPGLAVV LVGNDPASEV 

        70         80         90        100        110        120 
YVGRKIEACR RVGILSFEHR LPAQTTQDAL LTLIARLNAD PTIHGILVQV PLPSHIDDGM 

       130        140        150        160        170        180 
VLSAIDPAKD VDGFHPVNVG RLSTGTGGLV PCTPLGVMML LDSVIDDMKG MDAVVIGKSN 

       190        200        210        220        230        240 
IVGKPIAMLL LEREATVTVT HIETRGLPDI VRKADIIVAA AGAPRLVKGY WVKEGAVIID 

       250        260        270        280        290 
VGITRLPGEG GKTRLVGDVA FDEVQHARAV TPVPGGVGPM TIACLLANTV KAAEMRG

A5V807 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