[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Heart ventricle; NIH - Mammalian Gene Collection (MGC) project; Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
[2]	PROTEIN SEQUENCE OF 2-187. TISSUE=Liver; DOI=10.1021/bi00257a006; PubMed=7115669 [NCBI, ExPASy, EBI, Israel, Japan] Lai P.-H., Pan Y.-C.E., Gleisner J.M., Peterson D.L., Williams K.R., Blakley R.L.; "Structure of dihydrofolate reductase: primary sequence of the bovine liver enzyme."; Biochemistry 21:3284-3294(1982).

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

BC114162; AAI14163.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A00388; RDBOD.

NP_001071351.1; -.

3D structure databases

HSSP

P00374; 1DHF. [HSSP ENTRY / PDB]

SMR

P00376; 2-187.

ModBase

P00376.

Family and domain databases

InterPro

IPR001796; DHFR_reg.
Graphical view of domain structure.

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

P00376.

Genome annotation databases

Ensembl

ENSBTAG00000007681; Bos taurus. [Contig view]

GeneID

508809; -.

KEGG

bta:508809; -.

Phylogenomic databases

HOVERGEN

P00376; -.

Other

ProtoNet

P00376.

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`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 187`	`186`	`Dihydrofolate reductase.`	`PRO_0000186361`
`DOMAIN`	`4 185`	`182`	`DHFR.`
`CONFLICT`	`22 22`		`D -> N (in Ref. 1; AAI14163).`
`CONFLICT`	`102 102`		`E -> Q (in Ref. 2; AA sequence).`

Sequence information

Length: 187 AA [This is the length of the unprocessed precursor]

Molecular weight: 21604 Da [This is the MW of the unprocessed precursor]

CRC64: 0727DD855C8A7CD8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVRPLNCIVA VSQNMGIGKN GDLPWPPLRN EFQYFQRMTT VSSVEGKQNL VIMGRKTWFS 

        70         80         90        100        110        120 
IPEKNRPLKD RINIVLSREL KEPPKGAHFL AKSLDDALEL IEDPELTNKV DVVWIVGGSS 

       130        140        150        160        170        180 
VYKEAMNKPG HVRLFVTRIM QEFESDAFFP EIDFEKYKLL PEYPGVPLDV QEEKGIKYKF 


EVYEKNN

P00376 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