[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PLASMID=pLMO27; TRANSPOSON=Tn5086; PubMed=8383666 [NCBI, ExPASy, EBI, Israel, Japan] Sundstroem L., Swedberg G., Skoeld O.; "Characterization of transposon Tn5086, carrying the site-specifically inserted gene dhfrVII mediating trimethoprim resistance."; J. Bacteriol. 175:1796-1805(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PLASMID=IncP-beta R751; TRANSPOSON=Tn5090; PubMed=8195081 [NCBI, ExPASy, EBI, Israel, Japan] Raadstroem P., Skoeld O., Swedberg G., Flensburg J., Roy P.H., Sundstroem L.; "Transposon Tn5090 of plasmid R751, which carries an integron, is related to Tn7, Mu, and the retroelements."; J. Bacteriol. 176:3257-3268(1994).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PLASMID=pDGO100; STRAIN=VA292; DOI=10.1006/plas.1996.0008; PubMed=8693029 [NCBI, ExPASy, EBI, Israel, Japan] Burnside J.M., Groot Obbink D.J.; "Plasmid pDGO100 contains a second integron with the trimethoprim resistance gene dfrA7 as the inserted cassette."; Plasmid 35:67-70(1996).

Comments

CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP⁺ = 7,8-dihydrofolate + NADPH.
PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1 .
SUBUNIT: Homodimer (By similarity).
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

X58425; CAA41326.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U31119; AAB18756.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A47087; A47087.

3D structure databases

HSSP

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

ModBase

P27422.

Ontologies

GO:0004146;	Molecular function: dihydrofolate reductase activity (inferred from electronic annotation from InterPro).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0006545;	Biological process: glycine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0009165;	Biological process: nucleotide biosynthetic process (inferred from electronic annotation from InterPro).
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:0046677;	Biological process: response to antibiotic (inferred from electronic annotation from UniProtKB-KW).
GO:0031427;	Biological process: response to methotrexate (inferred from electronic annotation from UniProtKB-KW).
GO:0032196;	Biological process: transposition (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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).

ProtoNet

P27422.

Other

UniRef

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

Keywords

Antibiotic resistance; Methotrexate resistance; NADP; One-carbon metabolism; Oxidoreductase; Plasmid; Transposable element; Trimethoprim resistance.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 157`	`157`	`Dihydrofolate reductase type 7.`	`PRO_0000186424`
`DOMAIN`	`2 156`	`155`	`DHFR.`

Sequence information

Length: 157 AA [This is the length of the unprocessed precursor]

Molecular weight: 17594 Da [This is the MW of the unprocessed precursor]

CRC64: A7791CC9C7E029DE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKISLISATS ENGVIGNGPD IPWSAKGEQL LFKALTYNQW LLVGRKTFDS MGVLPNRKYA 

        70         80         90        100        110        120 
VVSRKGISSS NENVLVFPSI EIALQELSKI TDHLYVSGGG QIYNSLIEKA DIIHLSTVHV 

       130        140        150 
EVEGDINFPK IPENFNLVFE QFFLSNINYT YQIWKKG

P27422 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