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Q04KK5 (Q04KK5_STRP2) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 59. Feed History...

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

Names and origin

Protein namesRecommended name:
UDP-N-acetylglucosamine 1-carboxyvinyltransferase HAMAP-Rule MF_00111

EC=2.5.1.7 HAMAP-Rule MF_00111
Alternative name(s):
Enoylpyruvate transferase HAMAP-Rule MF_00111
UDP-N-acetylglucosamine enolpyruvyl transferase HAMAP-Rule MF_00111
Gene names
Name:murA-1 EMBL ABJ54180.1
Synonyms:murA HAMAP-Rule MF_00111
Ordered Locus Names:SPD_0967 EMBL ABJ54180.1
OrganismStreptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) [Complete proteome] [HAMAP] EMBL ABJ54180.1
Taxonomic identifier373153 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine By similarity. SAAS SAAS005750 HAMAP-Rule MF_00111

Catalytic activity

Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine. SAAS SAAS005750 HAMAP-Rule MF_00111

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00111

Subcellular location

Cytoplasm By similarity SAAS SAAS005750 HAMAP-Rule MF_00111.

Sequence similarities

Belongs to the EPSP synthase family. MurA subfamily. HAMAP-Rule MF_00111

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1161Proton donor By similarity HAMAP-Rule MF_00111

Amino acid modifications

Modified residue11612-(S-cysteinyl)pyruvic acid O-phosphothioketal By similarity HAMAP-Rule MF_00111

Sequences

Sequence LengthMass (Da)Tools
Q04KK5 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 5717D819B16DF8E3

FASTA41945,025
        10         20         30         40         50         60 
MRKIVINGGL PLQGEITISG AKNSVVALIP AIILADDVVT LDCVPDISDV ASLVEIMELM 

        70         80         90        100        110        120 
GATVKRYDDV LEIDPRGVQN IPMPYGKINS LRASYYFYGS LLGRFGEATV GLPGGCDLGP 

       130        140        150        160        170        180 
RPIDLHLKAF EAMGATASYE GDNMKLSAKD TGLHGASIYM DTVSVGATIN TMIAAVKANG 

       190        200        210        220        230        240 
RTIIENAARE PEIIDVATLL NNMGAHIRGA GTNIIIIDGV ERLHGTRHQV IPDRIEAGTY 

       250        260        270        280        290        300 
ISLAAAVGKG IRINNVLYEH LEGFIAKLEE MGVRMTVSED SIFVEEQSNL KAINIKTAPY 

       310        320        330        340        350        360 
PGFATDLQQP LTPLLLRANG RGTIVDTIYE KRVNHVFELA KMDADISTTN GHILYTGGRD 

       370        380        390        400        410 
LRGASVKATD LRAGAALVIA GLMAEGKTEI TNIEFILRGY SDIIEKLRNL GADIRLVED 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus pneumoniae and comparison with that of unencapsulated laboratory strain R6."
Lanie J.A., Ng W.L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.
J. Bacteriol. 189:38-51(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D39 / NCTC 7466.
[2]"Heteroresistance to fosfomycin is predominant in Streptococcus pneumoniae and depends on the murA1 gene."
Engel H., Gutierrez-Fernandez J., Fluckiger C., Martinez-Ripoll M., Muhlemann K., Hermoso J.A., Hilty M., Hathaway L.J.
Antimicrob. Agents Chemother. 57:2801-2808(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000410 Genomic DNA. Translation: ABJ54180.1.
RefSeqYP_816443.1. NC_008533.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZH3X-ray2.90A1-419[»]
ProteinModelPortalQ04KK5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING373153.SPD_0967.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ54180; ABJ54180; SPD_0967.
GeneID4441381.
KEGGspd:SPD_0967.
PATRIC19683096. VBIStrPne27904_1083.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0766.
HOGENOMHOG000075602.
KOK00790.
OMAGATIWRE.
OrthoDBEOG68M4GK.

Enzyme and pathway databases

BioCycSPNE373153:GIX6-967-MONOMER.
UniPathwayUPA00219.

Family and domain databases

Gene3D3.65.10.10. 2 hits.
HAMAPMF_00111. MurA.
InterProIPR001986. Enolpyruvate_Tfrase_dom.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR005750. UDP_GlcNAc_COvinyl_MurA.
[Graphical view]
PANTHERPTHR21090:SF4. PTHR21090:SF4. 1 hit.
PfamPF00275. EPSP_synthase. 1 hit.
[Graphical view]
SUPFAMSSF55205. SSF55205. 1 hit.
TIGRFAMsTIGR01072. murA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ04KK5_STRP2
AccessionPrimary (citable) accession number: Q04KK5
Entry history
Integrated into UniProtKB/TrEMBL: November 14, 2006
Last sequence update: November 14, 2006
Last modified: June 11, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)