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P0A552 (DUT_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Deoxyuridine 5'-triphosphate nucleotidohydrolase

Short name=dUTPase
EC=3.6.1.23
Alternative name(s):
dUTP pyrophosphatase
Gene names
Name:dut
Ordered Locus Names:Rv2697c, MT2771
ORF Names:MTCY05A6.18c
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length154 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. HAMAP-Rule MF_00116

Catalytic activity

dUTP + H2O = dUMP + diphosphate. HAMAP-Rule MF_00116

Cofactor

Magnesium.

Pathway

Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. HAMAP-Rule MF_00116

Subunit structure

Homotrimer. Ref.4

Miscellaneous

Each trimer binds three substrate molecules. The ligands are bound between subunits, and for each substrate molecule, residues from adjacent subunits contribute to the binding interactions. HAMAP-Rule MF_00116

Sequence similarities

Belongs to the dUTPase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 154154Deoxyuridine 5'-triphosphate nucleotidohydrolase HAMAP-Rule MF_00116
PRO_0000182884

Regions

Region64 – 663Substrate binding HAMAP-Rule MF_00116
Region81 – 833Substrate binding HAMAP-Rule MF_00116

Sites

Binding site771Substrate
Binding site911Substrate; via amide nitrogen and carbonyl oxygen

Secondary structure

................................. 154
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A552 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 836D5E6420EF455B

FASTA15415,803
        10         20         30         40         50         60 
MSTTLAIVRL DPGLPLPSRA HDGDAGVDLY SAEDVELAPG RRALVRTGVA VAVPFGMVGL 

        70         80         90        100        110        120 
VHPRSGLATR VGLSIVNSPG TIDAGYRGEI KVALINLDPA APIVVHRGDR IAQLLVQRVE 

       130        140        150 
LVELVEVSSF DEAGLASTSR GDGGHGSSGG HASL 

« Hide

References

« Hide 'large scale' 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]"Crystal structure of dUTPase from Mycobacterium tuberculosis."
Sawaya M.R., Chan S., Segelke B.W., Lekin T., Heike K., Cho U.S., Naranjo C., Perry L.J., Yeates T.O., Eisenberg D.
Submitted (SEP-2002) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
[4]"Crystal structure of the Mycobacterium tuberculosis dUTPase: insights into the catalytic mechanism."
Chan S., Segelke B., Lekin T., Krupka H., Cho U.S., Kim M.-Y., So M., Kim C.-Y., Naranjo C.M., Rogers Y.C., Park M.S., Waldo G.S., Pashkov I., Cascio D., Perry J.L., Sawaya M.R.
J. Mol. Biol. 341:503-517(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH MAGNESIUM ION AND SUBSTRATE ANALOG, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000516 Genomic DNA. Translation: AAK47086.1.
AL123456 Genomic DNA. Translation: CCP45495.1.
PIRD70530.
RefSeqNP_217213.1. NC_000962.3.
NP_337272.1. NC_002755.2.
YP_006516141.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MQ7X-ray1.95A1-154[»]
1SIXX-ray1.30A1-154[»]
1SJNX-ray1.80A/B/C1-154[»]
1SLHX-ray3.00A/B/C1-154[»]
1SM8X-ray2.90A/B/C1-154[»]
1SMCX-ray2.10A/B/C1-154[»]
1SNFX-ray1.85A/B/C1-154[»]
2PY4X-ray1.49A1-154[»]
3H6DX-ray1.80A1-154[»]
3HZAX-ray1.20A1-154[»]
3I93X-ray1.80A1-138[»]
3LOJX-ray1.25A1-154[»]
ProteinModelPortalP0A552.
SMRP0A552. Positions 1-138.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv2697c.

Proteomic databases

PRIDEP0A552.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK47086; AAK47086; MT2771.
GeneID13319424.
887290.
925523.
KEGGmtc:MT2771.
mtu:Rv2697c.
PATRIC18127836. VBIMycTub22151_3017.

Organism-specific databases

TubercuListRv2697c.

Phylogenomic databases

eggNOGCOG0756.
HOGENOMHOG000028966.
KOK01520.
OMAKVCLINH.
ProtClustDBPRK00601.

Enzyme and pathway databases

UniPathwayUPA00610; UER00666.

Family and domain databases

HAMAPMF_00116. dUTPase_bact.
InterProIPR008180. dUTP_pyroPase.
IPR008181. dUTP_pyroPase_sf.
[Graphical view]
PANTHERPTHR11241. PTHR11241. 1 hit.
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00576. dut. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A552.

Entry information

Entry nameDUT_MYCTU
AccessionPrimary (citable) accession number: P0A552
Secondary accession number(s): L0TAD4, O07199
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 29, 2013
This is version 60 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families