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Q5UQG3 (DRTS_MIMIV) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional dihydrofolate reductase-thymidylate synthase

Short name=DHFR-TS

Including the following 2 domains:

  1. Dihydrofolate reductase
    EC=1.5.1.3
  2. Thymidylate synthase
    EC=2.1.1.45
Gene names
Ordered Locus Names:MIMI_R497
OrganismAcanthamoeba polyphaga mimivirus (APMV) [Reference proteome]
Taxonomic identifier212035 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageMimiviridaeMimivirus
Virus hostAcanthamoeba polyphaga (Amoeba) [TaxID: 5757]

Protein attributes

Sequence length563 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP By similarity. HAMAP-Rule MF_00008

Catalytic activity

5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH. HAMAP-Rule MF_00008

5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. HAMAP-Rule MF_00008

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1. HAMAP-Rule MF_00008

Sequence similarities

In the N-terminal section; belongs to the dihydrofolate reductase family.

In the C-terminal section; belongs to the thymidylate synthase family.

Contains 1 DHFR (dihydrofolate reductase) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 563563Bifunctional dihydrofolate reductase-thymidylate synthase HAMAP-Rule MF_00008
PRO_0000186360

Regions

Domain3 – 195193DHFR
Nucleotide binding117 – 1248NADP By similarity
Nucleotide binding464 – 4685dUMP By similarity
Nucleotide binding504 – 5063dUMP By similarity
Region275 – 563289Thymidylate synthase By similarity

Sites

Active site4351 By similarity
Binding site2921dUMP By similarity
Binding site4361dUMP By similarity
Binding site4741dUMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5UQG3 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 590F4EAE5A11625B

FASTA56365,063
        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 

« Hide

References

[1]"The 1.2-megabase genome sequence of Mimivirus."
Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H., La Scola B., Susan M., Claverie J.-M.
Science 306:1344-1350(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Rowbotham-Bradford.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY653733 Genomic DNA. Translation: AAV50762.1.
RefSeqYP_003987009.1. NC_014649.1.

3D structure databases

ProteinModelPortalQ5UQG3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9925127.

Enzyme and pathway databases

UniPathwayUPA00077; UER00158.

Family and domain databases

Gene3D3.30.572.10. 1 hit.
3.40.430.10. 1 hit.
HAMAPMF_00008. Thymidy_synth_bact.
InterProIPR024072. DHFR-like_dom.
IPR001796. DHFR_dom.
IPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]
PfamPF00186. DHFR_1. 1 hit.
PF00303. Thymidylat_synt. 1 hit.
[Graphical view]
PRINTSPR00108. THYMDSNTHASE.
SUPFAMSSF53597. SSF53597. 1 hit.
SSF55831. SSF55831. 1 hit.
TIGRFAMsTIGR03284. thym_sym. 1 hit.
PROSITEPS51330. DHFR_2. 1 hit.
PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDRTS_MIMIV
AccessionPrimary (citable) accession number: Q5UQG3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: December 7, 2004
Last modified: February 19, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways