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

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

Cross-references

Sequence databases

EMBL

CP000359; ABF45001.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_604170.1; -.

3D structure databases

ModBase

Q1J0I3.

Enzyme and pathway databases

BioCyc

DGEO319795:DGEO_0699-MON; -.

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; 1.
PS00767; THF_DHG_CYH_2; 1.

BLOCKS

Q1J0I3.

Genome annotation databases

GeneID

4058281; -.

GenomeReviews

CP000359_GR; Dgeo_0699.

KEGG

dge:Dgeo_0699; -.

NMPDR

fig|68909.1.peg.1000; -.

Phylogenomic databases

HOGENOM

Q1J0I3; -.

Genome annotation databases

CMR

Q1J0I3; Dgeo_0699.

Other

ProtoNet

Q1J0I3.

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`	`1 289`	`289`		`Bifunctional protein folD 2.`	`PRO_0000268333`

Sequence information

Length: 289 AA [This is the length of the unprocessed precursor]

Molecular weight: 30103 Da [This is the MW of the unprocessed precursor]

CRC64: 49218ECB6C2F4DFF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTARLLRGGP AADALLAEAT ARAARLPAPP QLVMLRLGED PASVSYVRGK DRKAREVGLK 

        70         80         90        100        110        120 
STVYALPETT SQAELLDLIA RLNADDTVNG ILVQLPLPLH IQEQAVLHAI DPRKDVDGFH 

       130        140        150        160        170        180 
PLNVGELWAG RPALRPCTPA GILYLLDHYG IPVAGQRAVV VGRSSIVGRP LAGLLLHRDA 

       190        200        210        220        230        240 
TVTVAHSRTP DLGAVTREAD LLCVAVGRPH LITPDMVRPG ATVVDVGINR VLGEGGGKAQ 

       250        260        270        280 
LTGDVAPEVA QVAGAITPVP GGVGPMTIAQ LLANTVLAAE LQAKGRAAR

Q1J0I3 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