NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43049 / DSM 3752 / JCM 8966;
DOI=10.1101/gr.2700304; PubMed=15520287 [NCBI, ExPASy, EBI, Israel, Japan]
Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V.;
"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.";
Genome Res. 14:2221-2234(2004).

Comments

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

AY596297; AAV45963.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_135669.1; -.

3D structure databases

ModBase

Q5V3D9.

Enzyme and pathway databases

BioCyc

HMAR272569:RRNAC0996-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).
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; FALSE_NEG.

Genome annotation databases

GeneID

3129858; -.

GenomeReviews

AY596297_GR; rrnAC0996.

KEGG

hma:rrnAC0996; -.

NMPDR

fig|272569.1.peg.933; -.

Phylogenomic databases

HOGENOM

Q5V3D9; -.

Genome annotation databases

CMR

Q5V3D9; rrnAC0996.

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`	`1 297`	`297`		`Bifunctional protein folD 1.`	`PRO_0000268578`

Sequence information

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

Molecular weight: 31569 Da [This is the MW of the unprocessed precursor]

CRC64: D9CDC2DC8D980743 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTEIIDGNAV AQSIRDDLVA SIDRLADAGH RPSLATVLMS EDPASETYVS MKQDDCEEVG 

        70         80         90        100        110        120 
IEAIDIDIDS DADAAELYDT IEDLNADEDV NGILVQMPVP DHVEDRSVLR AIDPMKDVDG 

       130        140        150        160        170        180 
FHPENVGRLV AGDARYKPCT PHGIQKLIES AGVDTEGKDA VVVGRSDIVG KPMANLLIQK 

       190        200        210        220        230        240 
APGGNATTTV CHSRTENLAE RTRNADILVA AAGVPEMIDG KMIQEGATVI DVGINRVDAD 

       250        260        270        280        290 
TEKGYELVGD VEYESAKEVA GAITPVPGGV GPMTRAMLLY NTVKATGLQH DIDVDLP

Q5V3D9 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