[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1023/A:1006324328355; PubMed=10737138 [NCBI, ExPASy, EBI, Israel, Japan] Cox K.M., Robertson D., Fites R.C.; "Mapping and expression of a bifunctional thymidylate synthase, dihydrofolate reductase gene from maize."; Plant Mol. Biol. 41:733-739(1999).

Comments

CATALYTIC ACTIVITY: 5,6,7,8-tetrahydrofolate + NADP⁺ = 7,8-dihydrofolate + NADPH.
CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.
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: In the N-terminal section; belongs to the dihydrofolate reductase family.
SIMILARITY: In the C-terminal section; belongs to the thymidylate synthase 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

AF073488; AAC26003.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

T01684; T01684.

NP_001104916.1; -.

3D structure databases

HSSP

P13100; 1CI7. [HSSP ENTRY / PDB]

ModBase

O81395.

Organism-specific databases

Gramene

O81395; -.

Ontologies

GO:0004146;	Molecular function: dihydrofolate reductase activity (inferred from electronic annotation from InterPro).
GO:0004799;	Molecular function: thymidylate synthase activity (inferred from electronic annotation from InterPro).
GO:0006231;	Biological process: dTMP biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006545;	Biological process: glycine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006730;	Biological process: one-carbon compound metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR012262; DHFR-TS.
IPR001796; DHFR_reg.
IPR000398; Thymidylat_synth_C.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.572.10; Thymidylat_synth_C; 1.

PANTHER

PTHR11549:SF2; Thymidylat_synth_C; 1.

Pfam

PF00186; DHFR_1; 1.
PF00303; Thymidylat_synt; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000389; DHFR-TS; 1.

PRINTS

PR00070; DHFR.
PR00108; THYMDSNTHASE.

ProDom

PD001180; Thymidylat_synth; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR03284; thym_sym; 1.

PROSITE

PS00075; DHFR_1; 1.
PS51330; DHFR_2; 1.
PS00091; THYMIDYLATE_SYNTHASE; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

541707; -.

Other

ProtoNet

O81395.

UniRef

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

Keywords

Methyltransferase; Multifunctional enzyme; NADP; Nucleotide biosynthesis; One-carbon metabolism; Oxidoreductase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 521`	`521`	`Bifunctional dihydrofolate reductase-thymidylate synthase.`	`PRO_0000186358`
`DOMAIN`	`17 194`	`178`	`DHFR.`
`REGION`	`197 521`	`325`	`Thymidylate synthase.`
`ACT_SITE`	`403 403`		`By similarity.`

Sequence information

Length: 521 AA [This is the length of the unprocessed precursor]

Molecular weight: 58966 Da [This is the MW of the unprocessed precursor]

CRC64: 81266F8652625F06 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVLANGDS QGRPQRNYQV VVAGTRDMGI GKDGVLPWKL PGDLKFFKEL TLTTSDPVKK 

        70         80         90        100        110        120 
NAVIMGRKTW ESIPVKSRPL PGRLNVILTR SGSFDFATVE NVVICGSMES ALELLASTPY 

       130        140        150        160        170        180 
CLSIEKVFVI GGGQVLREYL KGPACEAIHL TDIQSSIECD TFIPPVDFSV FQPWYSSFPV 

       190        200        210        220        230        240 
IESNIRHSFV SFVRVRKSVA ETHESNGKES TEVDTKNDKF ETENFSFLPK MVYDRHEEYQ 

       250        260        270        280        290        300 
YLNLVEDIIR SGAQKNDRTG TGTLSKFGCQ MRFNLRKNFP LLTTKRVFWR GVVEELLWFI 

       310        320        330        340        350        360 
SGSTNAKVLQ EKGIHIWDGN ASREYLNSVG LAHREEGDLG PIYGFQWRHF GAEYTDMHAD 

       370        380        390        400        410        420 
YTGKGFDQLM DVIDKIKNDP EDRRIILSAW NPSDLKKMAL PPCHMFAQFY VENGELSCQM 

       430        440        450        460        470        480 
YQRSADMGLG VPFNIASYSL LTYMIAQVCD LSPGDFVHVI GDAHVYRNHV RALEEQIQKM 

       490        500        510        520 
PKPFPILKIN PSKKDIDSFM ASDFKLVGYD PHQKIEMKMA V

O81395 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