NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
"Complete sequence of Geobacter metallireducens GS-15.";
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.

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

CP000148; ABB31400.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_384125.1; -.

3D structure databases

ModBase

Q39WH4.

Enzyme and pathway databases

BioCyc

GMET269799:GMET_1162-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; 1.
PS00767; THF_DHG_CYH_2; 1.

Genome annotation databases

GeneID

3740389; -.

GenomeReviews

CP000148_GR; Gmet_1162.

KEGG

gme:Gmet_1162; -.

NMPDR

fig|269799.3.peg.1730; -.

Phylogenomic databases

HOGENOM

Q39WH4; -.

Genome annotation databases

CMR

Q39WH4; Gmet_1162.

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`	`1 285`	`285`		`Bifunctional protein folD 2.`	`PRO_0000268359`

Sequence information

Length: 285 AA [This is the length of the unprocessed precursor]

Molecular weight: 30179 Da [This is the MW of the unprocessed precursor]

CRC64: 5CE21B382B24171F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTIIDGKAI AAKLRAEIAT EVKILKEKGI IPGLATVLVG EDPASEVYVR MKGNACQELG 

        70         80         90        100        110        120 
MHSVKHTLPA TTTEAELLAL VARLNSDPTI HGILVQLPLP KQINSDTILE AISPVKDVDG 

       130        140        150        160        170        180 
FHPYNVGRLM VGKPTFQPCT PYGVMVMLRE AGVDLAGKEV VVVGRSNIVG KPVALMCLQQ 

       190        200        210        220        230        240 
HATVTICHSK TRDLPSKVKE ADVVIAAVGV PEMIKGEWIK EGAVVIDVGV NRVGEKKLVG 

       250        260        270        280 
DVEFAAASQR ASAITPVPGG VGPMTITMLL YNTLEAAKKT GEGNR

Q39WH4 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