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

AE015451; AAN67561.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_744097.1; -.

3D structure databases

HSSP

P11586; 1A4I. [HSSP ENTRY / PDB]

ModBase

Q88LI7.

Enzyme and pathway databases

BioCyc

PPUT160488:PP_1945-MON; -.

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; FALSE_NEG.
PS00767; THF_DHG_CYH_2; 1.

Genome annotation databases

GeneID

1043115; -.

GenomeReviews

AE015451_GR; PP_1945.

KEGG

ppu:PP_1945; -.

NMPDR

fig|160488.1.peg.1927; -.

TIGR

PP_1945; -.

Phylogenomic databases

HOGENOM

Q88LI7; -.

Other

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`	`1 291`	`291`		`Bifunctional protein folD 1.`	`PRO_0000268446`

Sequence information

Length: 291 AA [This is the length of the unprocessed precursor]

Molecular weight: 30531 Da [This is the MW of the unprocessed precursor]

CRC64: 84FB34A46E8EEDC4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTAQLIDGKA LAAQVRQEVE EGVAAFIADG WAAPGLAVVL VGCDAASQVY VENKIRQTEA 

        70         80         90        100        110        120 
VGMRSERFLL PADTDESQLL TLIEQLNNND AIHGILVQFP LPPQIDVSRV ISAIHPSKDV 

       130        140        150        160        170        180 
DGFNPLNVGR LAAGLEGGLT PCTPLGVMRL IRSVHPDIAG MGALVVGASN VVGRPLARLL 

       190        200        210        220        230        240 
LQADCTVSIA HIRTTDLARR CREADILVVA TGVPGLIRGD YIKPGATVID VGISRVRLPN 

       250        260        270        280        290 
GRDKLTGDVA FEEAVEVAGA ITPVPGGVGP MTIAYLLANT LQAARAAVRL R

Q88LI7 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