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Q1B9Y5 (Q1B9Y5_MYCSS) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 54. Feed History...

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

Protein names
EC=3.6.1.23 EMBL ABG08299.1
Gene names
Ordered Locus Names:Mmcs_2191
OrganismMycobacterium sp. (strain MCS) [Complete proteome] [HAMAP]
Taxonomic identifier164756 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length139 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. SAAS SAAS008181

Catalytic activity

dUTP + H2O = dUMP + diphosphate. SAAS SAAS008181

Cofactor

Magnesium By similarity. SAAS SAAS008181

Sequences

Sequence LengthMass (Da)Tools
Q1B9Y5 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 96C4D6ECC532B0E2

FASTA13914,406
        10         20         30         40         50         60 
MPARAHDGDA GVDLFSARDV ELAPGQRELV PTGIAVAIPH GMVGLVHPRS GLAARVGLSI 

        70         80         90        100        110        120 
VNSPGTIDAG YRGEIKVSLI NLDPHAPIVI RRGDRIAQLL VQRVELPELV EVTSFDEAGL 

       130 
AETTRGEGGH GSSGGHASL 

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References

[1]"Complete sequence of chromosome of Mycobacterium sp. MCS."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000384 Genomic DNA. Translation: ABG08299.1.
RefSeqYP_639355.1. NC_008146.1.

3D structure databases

ProteinModelPortalQ1B9Y5.
SMRQ1B9Y5. Positions 1-129.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1B9Y5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000061139; EBMYCP00000059306; EBMYCG00000061134.
GeneID4111024.
GenomeReviewsGene locus Mmcs_2191 in contig CP000384_GR.
KEGGmmc:Mmcs_2191.
PATRIC18114580. VBIMycSp106721_2243.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0756.
GeneTreeEBGT00050000017683.
HOGENOMHBG436079.
OMAKIAQMVI.
ProtClustDBPRK00601.

Family and domain databases

InterProIPR008180. dUTP_pyroPase.
IPR008181. dUTP_pyroPase_sf.
[Graphical view]
KOK01520.
PANTHERPTHR11241. PTHR11241. 1 hit.
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00576. Dut. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ1B9Y5_MYCSS
AccessionPrimary (citable) accession number: Q1B9Y5
Entry history
Integrated into UniProtKB/TrEMBL: July 11, 2006
Last sequence update: July 11, 2006
Last modified: December 14, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)