[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=51-MG/7; PubMed=7574597 [NCBI, ExPASy, EBI, Israel, Japan] Leszczynska K., Bolhuis A., Leenhouts K., Venema G., Ceglowski P.; "Cloning and molecular analysis of the dihydrofolate reductase gene from Lactococcus lactis."; Appl. Environ. Microbiol. 61:561-566(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=IL1403; DOI=10.1101/gr.GR-1697R; PubMed=11337471 [NCBI, ExPASy, EBI, Israel, Japan] Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A.; "The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403."; Genome Res. 11:731-753(2001).

Comments

CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP⁺ = 7,8-dihydrofolate + NADPH.
PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1 .
MISCELLANEOUS: The reaction catalyzed by this enzyme represents an essential step for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.
SIMILARITY: Belongs to the dihydrofolate reductase family.
SIMILARITY: Contains 1 DHFR (dihydrofolate reductase) domain.

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

X60681; CAA43094.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE006347; AAK05248.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

F86768; F86768.
S47467; S47467.

RefSeq

NP_267306.1; -.

3D structure databases

HSSP

P00379; 1DHI. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

Q59487.

Enzyme and pathway databases

BioCyc

LLAC272623:L162872-MON; -.

Family and domain databases

InterPro

IPR012259; DHFR.
IPR001796; DHFR_reg.
Graphical view of domain structure.

PANTHER

PTHR11549:SF1; DHFR; 1.

Pfam

PF00186; DHFR_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00070; DHFR.

PROSITE

PS00075; DHFR_1; 1.
PS51330; DHFR_2; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q59487.

Genome annotation databases

1114791; -.

AE005176_GR; LL1150.

lla:L162872; -.

fig|272623.1.peg.1183; -.

Phylogenomic databases

HOGENOM

Q59487; -.

Genome annotation databases

CMR

Q59487; LL1150.

Other

ProtoNet

Q59487.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; NADP; One-carbon metabolism; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 168`	`168`	`Dihydrofolate reductase.`	`PRO_0000186394`
`DOMAIN`	`1 164`	`164`	`DHFR.`
`CONFLICT`	`11 11`		`A -> Q (in Ref. 1; CAA43094).`
`CONFLICT`	`29 29`		`Q -> K (in Ref. 1; CAA43094).`
`CONFLICT`	`72 72`		`D -> E (in Ref. 1; CAA43094).`
`CONFLICT`	`90 90`		`H -> Y (in Ref. 1; CAA43094).`
`CONFLICT`	`93 93`		`N -> D (in Ref. 1; CAA43094).`
`CONFLICT`	`125 125`		`K -> Q (in Ref. 1; CAA43094).`
`CONFLICT`	`132 133`		`ST -> TH (in Ref. 1; CAA43094).`
`CONFLICT`	`138 138`		`R -> K (in Ref. 1; CAA43094).`
`CONFLICT`	`141 141`		`L -> V (in Ref. 1; CAA43094).`
`CONFLICT`	`145 145`		`K -> I (in Ref. 1; CAA43094).`
`CONFLICT`	`154 154`		`S -> A (in Ref. 1; CAA43094).`

Sequence information

Length: 168 AA [This is the length of the unprocessed precursor]

Molecular weight: 19729 Da [This is the MW of the unprocessed precursor]

CRC64: 0BB4D97167F247F4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIIGIWAEDE AGLIGEADKM PWSLPAEQQH FKETTMNQVI LMGRKTFEGM NKRVLPGRIS 

        70         80         90        100        110        120 
IILTRDETYQ SDNEKVLIMH SPKEVLDWYH KQNKDLFITG GAEILALFES ELELLYRTVV 

       130        140        150        160 
HEKFKGDTYF PSTFDFGRFK LVSEKFHDKD ERNSYTFTIK KYEKVKQP

Q59487 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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