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O53512

- AROG_MYCTU

UniProt

O53512 - AROG_MYCTU

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Protein
Phospho-2-dehydro-3-deoxyheptonate aldolase AroG
Gene
aroG, Rv2178c
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Binds 2 divalent cations per subunit. The enzyme is active with manganese, cobalt or cadmium ions.1 Publication

Enzyme regulationi

Feedback inhibited by tryptophan, tyrosine, phenylalanine and chorismate.1 Publication

Kineticsi

  1. KM=25 µM for D-erythrose 4-phosphate (E4P)1 Publication
  2. KM=37 µM for phosphoenolpyruvate (PEP)

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi87 – 871Divalent cations
Binding sitei126 – 1261Substrate
Binding sitei306 – 3061Substrate
Binding sitei337 – 3371Substrate
Metal bindingi369 – 3691Divalent cations
Metal bindingi411 – 4111Divalent cations
Metal bindingi441 – 4411Divalent cations

GO - Molecular functioni

  1. 3-deoxy-7-phosphoheptulonate synthase activity Source: MTBBASE
  2. manganese ion binding Source: MTBBASE
  3. protein binding Source: MTBBASE

GO - Biological processi

  1. aromatic amino acid family biosynthetic process Source: UniProtKB-KW
  2. chorismate biosynthetic process Source: Reactome
  3. growth Source: MTBBASE
  4. protein homooligomerization Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciMTBRV:RV2178C-MONOMER.
ReactomeiREACT_27268. Chorismate via Shikimate Pathway.
UniPathwayiUPA00053; UER00084.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:aroG
Ordered Locus Names:Rv2178c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001584: Chromosome

Organism-specific databases

TubercuListiRv2178c.

Subcellular locationi

GO - Cellular componenti

  1. cell wall Source: MTBBASE
  2. cytosol Source: Reactome
  3. plasma membrane Source: MTBBASE
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Phospho-2-dehydro-3-deoxyheptonate aldolase AroG
PRO_0000414909Add
BLAST

Proteomic databases

PRIDEiO53512.

Interactioni

Subunit structurei

Homodimer. Interacts with Rv0948c.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MT0975P647672EBI-5241825,EBI-5241850From a different organism.

Protein-protein interaction databases

IntActiO53512. 1 interaction.
MINTiMINT-7298545.
STRINGi83332.Rv2178c.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni1 – 33
Beta strandi4 – 85
Helixi20 – 3011
Helixi42 – 5211
Helixi61 – 7515
Beta strandi80 – 856
Helixi91 – 933
Helixi96 – 11722
Beta strandi121 – 1266
Beta strandi143 – 1453
Turni150 – 1523
Beta strandi155 – 1584
Helixi159 – 1624
Helixi168 – 18821
Turni189 – 1924
Helixi194 – 20714
Beta strandi208 – 2103
Helixi211 – 23020
Helixi236 – 2383
Beta strandi244 – 2485
Helixi252 – 2576
Beta strandi259 – 2613
Beta strandi266 – 2683
Beta strandi271 – 2733
Beta strandi277 – 2815
Turni283 – 2853
Helixi291 – 2988
Beta strandi303 – 3075
Helixi313 – 32311
Beta strandi331 – 3366
Turni340 – 3423
Helixi343 – 35614
Beta strandi362 – 3654
Turni367 – 3693
Beta strandi371 – 3744
Beta strandi380 – 3834
Helixi384 – 40118
Beta strandi407 – 4126
Beta strandi420 – 4223
Turni423 – 4264
Helixi431 – 4333
Beta strandi439 – 4413
Helixi446 – 46116

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliO53512.
SMRiO53512. Positions 1-462.

Miscellaneous databases

EvolutionaryTraceiO53512.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni283 – 2842Substrate binding

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000242917.
KOiK01626.
OMAiHFEMTGQ.
OrthoDBiEOG6H1Q0Q.
PhylomeDBiO53512.

Family and domain databases

InterProiIPR002480. DAHP_synth_2.
[Graphical view]
PANTHERiPTHR21337. PTHR21337. 1 hit.
PfamiPF01474. DAHP_synth_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01358. DAHP_synth_II. 1 hit.

Sequencei

Sequence statusi: Complete.

O53512-1 [UniParc]FASTAAdd to Basket

« Hide

MNWTVDIPID QLPSLPPLPT DLRTRLDAAL AKPAAQQPTW PADQALAMRT    50
VLESVPPVTV PSEIVRLQEQ LAQVAKGEAF LLQGGDCAET FMDNTEPHIR 100
GNVRALLQMA VVLTYGASMP VVKVARIAGQ YAKPRSADID ALGLRSYRGD 150
MINGFAPDAA AREHDPSRLV RAYANASAAM NLVRALTSSG LASLHLVHDW 200
NREFVRTSPA GARYEALATE IDRGLRFMSA CGVADRNLQT AEIYASHEAL 250
VLDYERAMLR LSDGDDGEPQ LFDLSAHTVW IGERTRQIDG AHIAFAQVIA 300
NPVGVKLGPN MTPELAVEYV ERLDPHNKPG RLTLVSRMGN HKVRDLLPPI 350
VEKVQATGHQ VIWQCDPMHG NTHESSTGFK TRHFDRIVDE VQGFFEVHRA 400
LGTHPGGIHV EITGENVTEC LGGAQDISET DLAGRYETAC DPRLNTQQSL 450
ELAFLVAEML RD 462
Length:462
Mass (Da):50,641
Last modified:June 1, 1998 - v1
Checksum:i1BE844FAEF21C4C5
GO

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL123456 Genomic DNA. Translation: CCP44955.1.
PIRiD70936.
RefSeqiNP_216694.1. NC_000962.3.
YP_006515597.1. NC_018143.2.

Genome annotation databases

EnsemblBacteriaiCCP44955; CCP44955; Rv2178c.
GeneIDi13318866.
888309.
KEGGimtu:Rv2178c.
mtv:RVBD_2178c.
PATRICi18153402. VBIMycTub87468_2429.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL123456 Genomic DNA. Translation: CCP44955.1 .
PIRi D70936.
RefSeqi NP_216694.1. NC_000962.3.
YP_006515597.1. NC_018143.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2B7O X-ray 2.30 A/B 1-462 [» ]
2W19 X-ray 2.15 A/B 1-462 [» ]
2W1A X-ray 2.35 A/B 1-462 [» ]
2YPO X-ray 2.00 A/B 1-462 [» ]
2YPP X-ray 2.30 A/B 1-462 [» ]
2YPQ X-ray 2.76 A/B 1-462 [» ]
3KGF X-ray 2.00 A/B 1-462 [» ]
3NUD X-ray 3.00 A/B 1-462 [» ]
3NUE X-ray 2.50 A/B 1-462 [» ]
3NV8 X-ray 2.25 A/B 1-462 [» ]
3PFP X-ray 2.35 A/B 1-462 [» ]
3RZI X-ray 1.95 A/B 1-462 [» ]
ProteinModelPortali O53512.
SMRi O53512. Positions 1-462.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O53512. 1 interaction.
MINTi MINT-7298545.
STRINGi 83332.Rv2178c.

Proteomic databases

PRIDEi O53512.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CCP44955 ; CCP44955 ; Rv2178c .
GeneIDi 13318866.
888309.
KEGGi mtu:Rv2178c.
mtv:RVBD_2178c.
PATRICi 18153402. VBIMycTub87468_2429.

Organism-specific databases

TubercuListi Rv2178c.

Phylogenomic databases

HOGENOMi HOG000242917.
KOi K01626.
OMAi HFEMTGQ.
OrthoDBi EOG6H1Q0Q.
PhylomeDBi O53512.

Enzyme and pathway databases

UniPathwayi UPA00053 ; UER00084 .
BioCyci MTBRV:RV2178C-MONOMER.
Reactomei REACT_27268. Chorismate via Shikimate Pathway.

Miscellaneous databases

EvolutionaryTracei O53512.

Family and domain databases

InterProi IPR002480. DAHP_synth_2.
[Graphical view ]
PANTHERi PTHR21337. PTHR21337. 1 hit.
Pfami PF01474. DAHP_synth_2. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01358. DAHP_synth_II. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. 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).

Entry informationi

Entry nameiAROG_MYCTU
AccessioniPrimary (citable) accession number: O53512
Secondary accession number(s): L0T926
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: June 1, 1998
Last modified: September 3, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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