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P22487 (AROA_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Rv3227, MT3324
ORF Names:MTCY20B11.02
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length450 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. Ref.2

Subcellular location

Cytoplasm Probable HAMAP MF_00210.

Sequence similarities

Belongs to the EPSP synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4504503-phosphoshikimate 1-carboxyvinyltransferase HAMAP MF_00210
PRO_0000088273

Secondary structure

1 ........................................................................... 450
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22487 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 27BB86F9412A07D5

FASTA45046,426
        10         20         30         40         50         60 
MKTWPAPTAP TPVRATVTVP GSKSQTNRAL VLAALAAAQG RGASTISGAL RSRDTELMLD 

        70         80         90        100        110        120 
ALQTLGLRVD GVGSELTVSG RIEPGPGARV DCGLAGTVLR FVPPLAALGS VPVTFDGDQQ 

       130        140        150        160        170        180 
ARGRPIAPLL DALRELGVAV DGTGLPFRVR GNGSLAGGTV AIDASASSQF VSGLLLSAAS 

       190        200        210        220        230        240 
FTDGLTVQHT GSSLPSAPHI AMTAAMLRQA GVDIDDSTPN RWQVRPGPVA ARRWDIEPDL 

       250        260        270        280        290        300 
TNAVAFLSAA VVSGGTVRIT GWPRVSVQPA DHILAILRQL NAVVIHADSS LEVRGPTGYD 

       310        320        330        340        350        360 
GFDVDLRAVG ELTPSVAALA ALASPGSVSR LSGIAHLRGH ETDRLAALST EINRLGGTCR 

       370        380        390        400        410        420 
ETPDGLVITA TPLRPGIWRA YADHRMAMAG AIIGLRVAGV EVDDIAATTK TLPEFPRLWA 

       430        440        450 
EMVGPGQGWG YPQPRSGQRA RRATGQGSGG

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the aroA gene from Mycobacterium tuberculosis."
Garbe T., Jones C., Charles I.G., Dougan G., Young D.
J. Bacteriol. 172:6774-6782(1990) [PubMed: 2123856] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Cloning and overexpression in soluble form of functional shikimate kinase and 5-enolpyruvylshikimate 3-phosphate synthase enzymes from Mycobacterium tuberculosis."
Oliveira J.S., Pinto C.A., Basso L.A., Santos D.S.
Protein Expr. Purif. 22:430-435(2001) [PubMed: 11483005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT.
[3]"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: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[4]"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: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X52269 Genomic DNA. Translation: CAA36510.1.
M62708 Genomic DNA. Translation: AAA25356.1.
BX842582 Genomic DNA. Translation: CAB08328.1.
AE000516 Genomic DNA. Translation: AAK47667.1.
PIRE70590.
RefSeqNP_217744.1. NC_000962.2.
NP_337853.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BJBX-ray1.80A1-450[»]
2O0BX-ray1.15A1-450[»]
2O0DX-ray1.60A1-450[»]
2O0EX-ray1.81A1-450[»]
2O0XX-ray1.96A1-450[»]
2O0ZX-ray2.00A1-450[»]
2O15X-ray1.95A1-450[»]
ProteinModelPortalP22487.
SMRP22487. Positions 1-424.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000003249; EBMYCP00000003249; EBMYCG00000003247.
EBMYCT00000068984; EBMYCP00000067043; EBMYCG00000068979.
GeneID888753.
922813.
GenomeReviewsGene locus MT3324 in contig AE000516_GR.
Gene locus Rv3227 in contig AL123456_GR.
KEGGmtc:MT3324.
mtu:Rv3227.
PATRIC18129068. VBIMycTub22151_3630.
TIGRMT3324.

Organism-specific databases

TubercuListRv3227.

Phylogenomic databases

GeneTreeEBGT00050000016231.
HOGENOMHBG646626.
OMAHRMATAG.
PhylomeDBP22487.
ProtClustDBPRK02427.

Enzyme and pathway databases

ReactomeREACT_27295. Mycobacterium tuberculosis biological processes.

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_MYCTU
AccessionPrimary (citable) accession number: P22487
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: January 25, 2012
This is version 101 of the entry and version 1 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

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