PROTEIN SEQUENCE.
STRAIN=A / var. Durans;
PubMed=1097435 [NCBI, ExPASy, EBI, Israel, Japan]
Peterson D.L., Gleisner J.M., Blakley R.L.;
"The structure of the mutant dihydrofolate reductase from Streptococcus faecium. Amino acid sequence of peptide CNBr 7 and complete sequence of the protein.";
J. Biol. Chem. 250:4945-4954(1975).

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

PIR

A00392; RDSODF.

3D structure databases

HSSP

P15093; 1VDR. [HSSP ENTRY / PDB]

ModBase

P00380.

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).
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

P00380.

Other

UniRef

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

Keywords

Direct protein sequencing; NADP; One-carbon metabolism; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 167`	`167`	`Dihydrofolate reductase.`	`PRO_0000186390`
`DOMAIN`	`1 162`	`162`	`DHFR.`

Sequence information

Length: 167 AA [This is the length of the unprocessed precursor]

Molecular weight: 19583 Da [This is the MW of the unprocessed precursor]

CRC64: E00C2CF3BC420585 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFISMWAQDK NGLIGKDGLL PWRLPNDMRF FREHTMDKIL VMGRKTYEGM GKLSLPYRHI 

        70         80         90        100        110        120 
IVLTTQKDFK VEKNAEVLHS IDELLAYAKD IPEDIYVSGG SRIFQALLPE TKIIWRTLID 

       130        140        150        160 
AEFEGDTFIG EIDFTSFELV EEHEGIVNQE NQYPHRFQKW QKMSKVV

P00380 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