NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
DOI=10.1016/0167-4781(94)00251-W; PubMed=7742362 [NCBI, ExPASy, EBI, Israel, Japan]
Wang M., Ratnam S., Freisheim J.H.;
"Cloning, nucleotide sequence and expression of the bifunctional dihydrofolate reductase-thymidylate synthase from Glycine max.";
Biochim. Biophys. Acta 1261:325-336(1995).

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

S78087; AAB34317.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S55683; S55683.

UniGene

Gma.483

3D structure databases

HSSP

P04818; 1HW4. [HSSP ENTRY / PDB]

ModBase

P51820.

Ontologies

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).

Other

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 530`	`530`	`Bifunctional dihydrofolate reductase-thymidylate synthase.`	`PRO_0000186359`
`DOMAIN`	`26 203`	`178`	`DHFR.`
`REGION`	`206 530`	`325`	`Thymidylate synthase.`
`ACT_SITE`	`412 412`		`By similarity.`

Sequence information

Length: 530 AA [This is the length of the unprocessed precursor]

Molecular weight: 59745 Da [This is the MW of the unprocessed precursor]

CRC64: AFD710709FD5D820 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPSDSSVISN GHSNGSVNPL PNLQRTYQVV VAATQDWGIG KDGKLPWRLP TDLKFFKEIT 

        70         80         90        100        110        120 
MKTSEPGKKN AIVMGRKTWE SIPLEYRPLS GRLNVVLTRS GSFDIATAEN VVICGSMSSA 

       130        140        150        160        170        180 
LELLAASPYS LSIEKVFVIG GGQIFREALN VPGCEAIHLT EIQSSIECDT FMPPVDFTIF 

       190        200        210        220        230        240 
RPWYSSFPKV ENNIRYSFTT YVRVRSSAAE SAGQNIDPLL DNNSESMKFE VKDFSFLPKM 

       250        260        270        280        290        300 
ISERHEEYLY LKLVQDIIAE GTTKGDRTGT GTLSKFGCQM RFNLRGNFPL LTTKKVFWRG 

       310        320        330        340        350        360 
VVEELLWFIS GSTNAKVLQE KGIHIWDGNA SREYLDGVGL TEREEGDLGP VYGFQWRHFG 

       370        380        390        400        410        420 
ARYTDMHHDY SGQGFDQLLD VINKIKRNPD DRRIILSAWN PVDLKLMALP PCHMFAQFYV 

       430        440        450        460        470        480 
AHGELSCQMY QRSADMGLGI PFNIASYALL TCMIAHVCDL IPGDFIHVIG DAHIYRNHVR 

       490        500        510        520        530 
PLQEQLHNQP KPFPTLKINP KKKDIDSFVA ADFKLIGYDP HQKIDMKLSV

P51820 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