Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O53512 (AROG_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. 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:
Phospho-2-dehydro-3-deoxyheptonate aldolase AroG

EC=2.5.1.54
Alternative name(s):
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
DAHP synthase
Phospho-2-keto-3-deoxyheptonate aldolase
Gene names
Name:aroG
Ordered Locus Names:Rv2178c
OrganismMycobacterium tuberculosis (strain ATCC 25618 / H37Rv) [Reference proteome] [HAMAP]
Taxonomic identifier83332 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate. Ref.3

Catalytic activity

Phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate.

Cofactor

Binds 2 divalent cations per subunit. The enzyme is active with manganese, cobalt or cadmium ions. Ref.3

Enzyme regulation

Feedback inhibited by tryptophan, tyrosine, phenylalanine and chorismate. Ref.3

Pathway

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.

Subunit structure

Homodimer. Interacts with Rv0948c. Ref.3

Sequence similarities

Belongs to the class-II DAHP synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=25 µM for D-erythrose 4-phosphate (E4P) Ref.3

KM=37 µM for phosphoenolpyruvate (PEP)

Mass spectrometry

Molecular mass is 51827 Da from positions 1 - 462. Determined by MALDI. Ref.4

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Phospho-2-dehydro-3-deoxyheptonate aldolase AroG
PRO_0000414909

Regions

Region283 – 2842Substrate binding

Sites

Metal binding871Divalent cations
Metal binding3691Divalent cations
Metal binding4111Divalent cations
Metal binding4411Divalent cations
Binding site1261Substrate
Binding site3061Substrate
Binding site3371Substrate

Secondary structure

.............................................................................. 462
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O53512 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 1BE844FAEF21C4C5

FASTA46250,641
        10         20         30         40         50         60 
MNWTVDIPID QLPSLPPLPT DLRTRLDAAL AKPAAQQPTW PADQALAMRT VLESVPPVTV 

        70         80         90        100        110        120 
PSEIVRLQEQ LAQVAKGEAF LLQGGDCAET FMDNTEPHIR GNVRALLQMA VVLTYGASMP 

       130        140        150        160        170        180 
VVKVARIAGQ YAKPRSADID ALGLRSYRGD MINGFAPDAA AREHDPSRLV RAYANASAAM 

       190        200        210        220        230        240 
NLVRALTSSG LASLHLVHDW NREFVRTSPA GARYEALATE IDRGLRFMSA CGVADRNLQT 

       250        260        270        280        290        300 
AEIYASHEAL VLDYERAMLR LSDGDDGEPQ LFDLSAHTVW IGERTRQIDG AHIAFAQVIA 

       310        320        330        340        350        360 
NPVGVKLGPN MTPELAVEYV ERLDPHNKPG RLTLVSRMGN HKVRDLLPPI VEKVQATGHQ 

       370        380        390        400        410        420 
VIWQCDPMHG NTHESSTGFK TRHFDRIVDE VQGFFEVHRA LGTHPGGIHV EITGENVTEC 

       430        440        450        460 
LGGAQDISET DLAGRYETAC DPRLNTQQSL ELAFLVAEML RD 

« 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]"Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry."
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M., Kumar P. expand/collapse author list , Chaerkady R., Ramachandran S., Dash D., Pandey A.
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ATCC 25618 / H37Rv.
[3]"The structure of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase from Mycobacterium tuberculosis reveals a common catalytic scaffold and ancestry for type I and type II enzymes."
Webby C.J., Baker H.M., Lott J.S., Baker E.N., Parker E.J.
J. Mol. Biol. 354:927-939(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MANGANESE IONS, FUNCTION AS A DAHP SYNTHASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR, SUBUNIT.
Strain: ATCC 25618 / H37Rv.
[4]"Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner."
Sasso S., Okvist M., Roderer K., Gamper M., Codoni G., Krengel U., Kast P.
EMBO J. 28:2128-2142(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), MASS SPECTROMETRY.
Strain: ATCC 25618 / H37Rv.
[5]"Synergistic inhibition of the first enzyme of the shikimate pathway by combinations of aromatic amino acids."
Webby C.J., Jiao W., Hutton R.D., Baker H.M., Baker E.N., Jameson G.B., Parker E.J.
Submitted (OCT-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
[6]"Synergistic allostery of the first enzyme of the shikimate pathway reveals a sophisticated regulatory network for the control of a branched biosynthetic pathway."
Webby C.J., Jiao W., Hutton R.D., Baker H.M., Baker E.N., Jameson G.B., Parker E.J.
Submitted (JUL-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS).
[7]"Potent inhibitors of a shikimate pathway enzyme from mycobacterium tuberculosis combining mechanism- and modeling based design."
Reichau S., Jiao W., Walker S.R., Hutton R.D., Parker E.J.
Submitted (OCT-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL123456 Genomic DNA. Translation: CCP44955.1.
PIRD70936.
RefSeqNP_216694.1. NC_000962.3.
YP_006515597.1. NC_018143.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B7OX-ray2.30A/B1-462[»]
2W19X-ray2.15A/B1-462[»]
2W1AX-ray2.35A/B1-462[»]
2YPOX-ray2.00A/B1-462[»]
2YPPX-ray2.30A/B1-462[»]
2YPQX-ray2.76A/B1-462[»]
3KGFX-ray2.00A/B1-462[»]
3NUDX-ray3.00A/B1-462[»]
3NUEX-ray2.50A/B1-462[»]
3NV8X-ray2.25A/B1-462[»]
3PFPX-ray2.35A/B1-462[»]
3RZIX-ray1.95A/B1-462[»]
ProteinModelPortalO53512.
SMRO53512. Positions 1-462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-7298545.
STRING83332.Rv2178c.

Proteomic databases

PRIDEO53512.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCP44955; CCP44955; Rv2178c.
GeneID888309.
KEGGmtu:Rv2178c.
mtv:RVBD_2178c.
PATRIC18153402. VBIMycTub87468_2429.

Organism-specific databases

TubercuListRv2178c.

Phylogenomic databases

HOGENOMHOG000242917.
KOK01626.
OMAHFEMTGQ.
OrthoDBEOG6H1Q0Q.
PhylomeDBO53512.

Enzyme and pathway databases

BioCycMTBRV:RV2178C-MONOMER.
ReactomeREACT_27295. Mycobacterium tuberculosis biological processes.
UniPathwayUPA00053; UER00084.

Family and domain databases

InterProIPR002480. DAHP_synth_2.
[Graphical view]
PANTHERPTHR21337. PTHR21337. 1 hit.
PfamPF01474. DAHP_synth_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR01358. DAHP_synth_II. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO53512.

Entry information

Entry nameAROG_MYCTU
AccessionPrimary (citable) accession number: O53512
Secondary accession number(s): L0T926
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names