NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165;
DOI=10.1073/pnas.211433198; PubMed=11572948 [NCBI, ExPASy, EBI, Israel, Japan]
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.;
"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites.";
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165;
DOI=10.1038/nbt820; PubMed=12692562 [NCBI, ExPASy, EBI, Israel, Japan]
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.;
"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis.";
Nat. Biotechnol. 21:526-531(2003).

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

BA000030; BAC71154.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_824619.1; -.

3D structure databases

HSSP

P11586; 1A4I. [HSSP ENTRY / PDB]

SMR

Q82HR6; 3-281.

ModBase

Q82HR6.

Enzyme and pathway databases

BioCyc

SAVE227882:SAV3442-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

Q82HR6.

Genome annotation databases

GeneID

1210741; -.

GenomeReviews

BA000030_GR; SAV_3442.

KEGG

sma:SAV3442; -.

NMPDR

fig|227882.1.peg.3445; -.

Phylogenomic databases

HOGENOM

Q82HR6; -.

Genome annotation databases

CMR

Q82HR6; SAV_3442.

Other

ProtoNet

Q82HR6.

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`	`1 284`	`284`		`Bifunctional protein folD 2.`	`PRO_0000268526`

Sequence information

Length: 284 AA [This is the length of the unprocessed precursor]

Molecular weight: 29667 Da [This is the MW of the unprocessed precursor]

CRC64: 9F2DCABF45B4B89D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTAQILDGKA TAAAIKSDLT ARVAALKEKG VTPGLGTILV GDDPGSQKYV AGKHRDCAQV 

        70         80         90        100        110        120 
GIASIQRELP ATATQEEIEA AVRELNEDPA CTGYIVQLPL PKGIDENRIL ELMDPDKDAD 

       130        140        150        160        170        180 
GLHPMNLGRL VLNEPAPLPC TPNGVLTLLR RYGVEIKGAE VVVVGRGVTI GRPMPLLLTR 

       190        200        210        220        230        240 
RSENATVTQC HTGTRDLSSH LKRADIIVAA AGSAHLIRPE DVKPGAAVLD VGVSRSAEGK 

       250        260        270        280 
IVGDVHPGVA EVAGWISPNP GGVGPMTRAQ LLVNVVEAAE RSVG

Q82HR6 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