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Q9S400 (AROA_STRPN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. 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:
3-phosphoshikimate 1-carboxyvinyltransferase

EC=2.5.1.19
Alternative name(s):
5-enolpyruvylshikimate-3-phosphate synthase
Short name=EPSP synthase
Short name=EPSPS
Gene names
Name:aroA
Ordered Locus Names:SP_1371
OrganismStreptococcus pneumoniae [Complete proteome] [HAMAP]
Taxonomic identifier1313 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. HAMAP MF_00210

Pathway

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. HAMAP MF_00210

Subunit structure

Monomer By similarity. HAMAP MF_00210

Subcellular location

Cytoplasm Probable HAMAP MF_00210.

Sequence similarities

Belongs to the EPSP synthase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Aromatic amino acid biosynthesis
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processaromatic amino acid family biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-phosphoshikimate 1-carboxyvinyltransferase activity

Inferred from electronic annotation. Source: EC

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4274273-phosphoshikimate 1-carboxyvinyltransferase HAMAP MF_00210
PRO_0000088304

Experimental info

Sequence conflict131S → I in AAD45819. Ref.1
Sequence conflict711I → V in AAD45819. Ref.1
Sequence conflict2011K → Q in AAD45819. Ref.1
Sequence conflict3031G → C in AAD45819. Ref.1

Secondary structure

................................................................................ 427
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9S400 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: 45CE6F4D0D1C7B70

FASTA42745,766
        10         20         30         40         50         60 
MKLKTNIRHL HGSIRVPGDK SISHRSIIFG SLAEGETKVY DILRGEDVLS TMQVFRDLGV 

        70         80         90        100        110        120 
EIEDKDGVIT IQGVGMAGLK APQNALNMGN SGTSIRLISG VLAGADFEVE MFGDDSLSKR 

       130        140        150        160        170        180 
PMDRVTLPLK KMGVSISGQT ERDLPPLRLK GTKNLRPIHY ELPIASAQVK SALMFAALQA 

       190        200        210        220        230        240 
KGESVIIEKE YTRNHTEDML KQFGGHLSVD GKKITVQGPQ KLTGQKVVVP GDISSAAFWL 

       250        260        270        280        290        300 
VAGLIAPNSR LVLQNVGINE TRTGIIDVIR AMGGKLEITE IDPVAKSATL IVESSDLKGT 

       310        320        330        340        350        360 
EIGGALIPRL IDELPIIALL ATQAQGVTVI KDAEELKVKE TDRIQVVADA LNSMGADITP 

       370        380        390        400        410        420 
TADGMIIKGK SALHGARVNT FGDHRIGMMT AIAALLVADG EVELDRAEAI NTSYPSFFDD 


LESLIHG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF169483 Genomic DNA. Translation: AAD45819.1.
AE005672 Genomic DNA. Translation: AAK75469.1.
PIRD95159.
RefSeqNP_345829.1. NC_003028.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RF4X-ray2.20A/B/C/D1-427[»]
1RF5X-ray2.30A/B/C/D1-427[»]
1RF6X-ray1.90A/B/C/D1-427[»]
ProteinModelPortalQ9S400.
SMRQ9S400. Positions 1-427.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9S400. 3 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000025448; EBSTRP00000024540; EBSTRG00000025448.
GeneID931459.
GenomeReviewsGene locus SP_1371 in contig AE005672_GR.
KEGGspn:SP_1371.
PATRIC19707147. VBIStrPne105772_1416.
TIGRSP_1371.

Phylogenomic databases

GeneTreeEBGT00050000028044.
HOGENOMHBG646626.
OMALECANIS.
ProtClustDBPRK02427.

Enzyme and pathway databases

BioCycSPNE170187-1:SP_1371-MONOMER.
BRENDA2.5.1.19. 5946.

Family and domain databases

HAMAPMF_00210. EPSP_synth.
[Tree]
InterProIPR001986. Enolpyruvate_Tfrase_dom.
IPR006264. EPSP_synthase.
IPR023193. EPSP_synthase_CS.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
[Graphical view]
Gene3DG3DSA:3.65.10.10. EPSP_synthase. 2 hits.
KOK00800.
PfamPF00275. EPSP_synthase. 1 hit.
[Graphical view]
PIRSFPIRSF000505. EPSPS. 1 hit.
SUPFAMSSF55205. RNA3'_cycl/enolpyr_transf_A/B. 1 hit.
TIGRFAMsTIGR01356. AroA. 1 hit.
PROSITEPS00104. EPSP_SYNTHASE_1. 1 hit.
PS00885. EPSP_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAROA_STRPN
AccessionPrimary (citable) accession number: Q9S400
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 26, 2001
Last modified: January 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

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