NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Rowbotham-Bradford;
DOI=10.1126/science.1101485; PubMed=15486256 [NCBI, ExPASy, EBI, Israel, Japan]
Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H., La Scola B., Susan M., Claverie J.-M.;
"The 1.2-megabase genome sequence of Mimivirus.";
Science 306:1344-1350(2004).

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

AY653733; AAV50762.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_142851.1; -.

3D structure databases

ModBase

Q5UQG3.

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 UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

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.

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

ProtoNet

Q5UQG3.

Genome annotation databases

GeneID

3162308; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 563`	`563`	`Bifunctional dihydrofolate reductase-thymidylate synthase.`	`PRO_0000186360`
`DOMAIN`	`3 195`	`193`	`DHFR.`
`REGION`	`275 563`	`289`	`Thymidylate synthase (By similarity).`
`ACT_SITE`	`435 435`		`By similarity.`

Sequence information

Length: 563 AA [This is the length of the unprocessed precursor]

Molecular weight: 65063 Da [This is the MW of the unprocessed precursor]

CRC64: 590F4EAE5A11625B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKFNIIAAI NNDSIIGVKE YGTFSMPWPY LKDDMNHFRK ITTDTGSIES GVNAIIVGFN 

        70         80         90        100        110        120 
TWQTLPSSYR NIRSRFNIVI SRDDETDGQF HKYVKTFDEA IEFASSLTNL NEIFVIGGGV 

       130        140        150        160        170        180 
IYDLALKHKL LDKLYLTHVG SNYPIDDNVE KVVHFPLTWS KIEKMCDSNF LELDSEISKH 

       190        200        210        220        230        240 
DIGKNILLRF QEYSVKKELY WAIEYLKKNT SLDNKGIIGD KGATGSKGYS LEQHDYYSTE 

       250        260        270        280        290        300 
YFWNFYEFIT RKVFDLFNSS NEISIPSEEC PENQYIELVK TIMEKGIVKQ TRNSITKSIF 

       310        320        330        340        350        360 
GYQLKYDLSK GYPIQTIKRS YPKAIFEELM WMIRGQTDVS ILQKKGVHVW DKNSSKDFLS 

       370        380        390        400        410        420 
KYNLPYEEGD IGPGYGFQMR YWGAEYTDCK TSYQGQGIDQ LNKCIESIQN NPHDRRIMIN 

       430        440        450        460        470        480 
LWNCSDLDKM ALAPCHFCYM FGVDLYEVPT TSGKKGRLNC HLVQRSWDVL LGWNTTTAAL 

       490        500        510        520        530        540 
LTYLIANHCD LDPGILVHSI SDAHIYQSHI DSGAISQLLQ RKCRKFPNLV IRNKKEKIDD 

       550        560 
YEFDDLIIEN YYPCPSISAE MIA

Q5UQG3 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