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

CP000386; ABG05437.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_645249.1; -.

3D structure databases

ModBase

Q1AT41.

Enzyme and pathway databases

BioCyc

RXYL266117:RXYL_2517-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; FALSE_NEG.
PS00767; THF_DHG_CYH_2; FALSE_NEG.

BLOCKS

Q1AT41.

Genome annotation databases

GeneID

4117102; -.

GenomeReviews

CP000386_GR; Rxyl_2517.

KEGG

rxy:Rxyl_2517; -.

NMPDR

fig|266117.6.peg.2194; -.

Phylogenomic databases

HOGENOM

Q1AT41; -.

Genome annotation databases

CMR

Q1AT41; Rxyl_2517.

Other

ProtoNet

Q1AT41.

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`	`1 318`	`318`		`Bifunctional protein folD 3.`	`PRO_0000268487`

Sequence information

Length: 318 AA [This is the length of the unprocessed precursor]

Molecular weight: 33254 Da [This is the MW of the unprocessed precursor]

CRC64: 746A5C5140AD8322 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGARVIDGRP IAGELKKRVA SEVEGLAARG VRPGLATVLV GEDYAARAYE RRVGGLAAEL 

        70         80         90        100        110        120 
GCRYVCERLP REAEEADVLA VVGKLNADPR VSGILVLRPL PGHISEPAVF SALDPLKDIE 

       130        140        150        160        170        180 
AVHPVNAGLL ALGRPRYVPS TPAACFYLLD RYLERSGRPP EEFYPRSTVV VVGRSNNVGK 

       190        200        210        220        230        240 
PAVSLGFARG AAVISCDANA YRAGRLREHT LKADALIVAA GVAGLIDESY VREGVIAVDV 

       250        260        270        280        290        300 
GINPVADPGG SGRTLLVGDL DFGSVARKAE ALTPVPGGVG PITDVWLLKN TVAAGRGLAS 

       310 
QAKARCLLRG SHAHSSLI

Q1AT41 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