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P66930 (THYX_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Thymidylate synthase ThyX

Short name=TS
Short name=TSase
EC=2.1.1.148
Gene names
Name:thyX
Ordered Locus Names:Rv2754c, MT2824
ORF Names:MTV002.19c
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate By similarity. HAMAP-Rule MF_01408

Catalytic activity

5,10-methylenetetrahydrofolate + dUMP + NADPH = dTMP + tetrahydrofolate + NADP+. HAMAP-Rule MF_01408

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homotetramer By similarity.

Miscellaneous

Was identified as a high-confidence drug target. HAMAP-Rule MF_01408

Sequence similarities

Belongs to the thymidylate synthase ThyX family.

Contains 1 thyX (flavin-dependent thymidylate synthase) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 250250Thymidylate synthase ThyX HAMAP-Rule MF_01408
PRO_0000175570

Regions

Domain7 – 233227ThyX
Motif95 – 10511ThyX motif HAMAP-Rule MF_01408

Secondary structure

....................................... 250
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P66930 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 7BACFA59B5DA7294

FASTA25027,591
        10         20         30         40         50         60 
MAETAPLRVQ LIAKTDFLAP PDVPWTTDAD GGPALVEFAG RACYQSWSKP NPKTATNAGY 

        70         80         90        100        110        120 
LRHIIDVGHF SVLEHASVSF YITGISRSCT HELIRHRHFS YSQLSQRYVP EKDSRVVVPP 

       130        140        150        160        170        180 
GMEDDADLRH ILTEAADAAR ATYSELLAKL EAKFADQPNA ILRRKQARQA ARAVLPNATE 

       190        200        210        220        230        240 
TRIVVTGNYR AWRHFIAMRA SEHADVEIRR LAIECLRQLA AVAPAVFADF EVTTLADGTE 

       250 
VATSPLATEA 

« Hide

References

[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842580 Genomic DNA. Translation: CAA15550.1.
AE000516 Genomic DNA. Translation: AAK47143.1.
AL123456 Genomic DNA. Translation: CCP45553.1.
PIRA70880.
RefSeqNP_217270.1. NC_000962.3.
NP_337329.1. NC_002755.2.
YP_006516199.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AF6X-ray2.01A/B/C/D/E/F/G/H1-250[»]
2GQ2X-ray2.10A/B/C/D1-250[»]
3GWCX-ray1.90A/B/C/D/E/F/G/H1-250[»]
3HZGX-ray2.45A/B/C/D1-250[»]
ProteinModelPortalP66930.
SMRP66930. Positions 3-247.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv2754c.

Proteomic databases

PRIDEP66930.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK47143; AAK47143; MT2824.
GeneID13319482.
887766.
925465.
KEGGmtc:MT2824.
mtu:Rv2754c.
mtv:RVBD_2754c.
PATRIC18127962. VBIMycTub22151_3080.

Organism-specific databases

TubercuListRv2754c.

Phylogenomic databases

eggNOGCOG1351.
HOGENOMHOG000047391.
KOK03465.
OMASRSLTHE.
ProtClustDBPRK00847.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15770.

Family and domain databases

HAMAPMF_01408. ThyX.
InterProIPR003669. Thymidylate_synthase_ThyX.
[Graphical view]
PfamPF02511. Thy1. 1 hit.
[Graphical view]
SUPFAMSSF69796. Thy1. 1 hit.
TIGRFAMsTIGR02170. thyX. 1 hit.
PROSITEPS51331. THYX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP66930.
ChEMBLCHEMBL1795161.
EvolutionaryTraceP66930.

Entry information

Entry nameTHYX_MYCTU
AccessionPrimary (citable) accession number: P66930
Secondary accession number(s): L0TD90, O33296
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families