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Protein

Phospho-2-dehydro-3-deoxyheptonate aldolase AroG

Gene

aroG

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: 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

Mn2+1 Publication, Co2+1 Publication, Cd2+1 PublicationNote: 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)1 Publication

    Pathway:ichorismate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.
    Proteins known to be involved in the 7 steps of the subpathway in this organism are:
    1. Phospho-2-dehydro-3-deoxyheptonate aldolase AroG (aroG)
    2. 3-dehydroquinate synthase (LH57_13905), 3-dehydroquinate synthase (aroB)
    3. 3-dehydroquinate dehydratase (aroQ)
    4. no protein annotated in this organism
    5. Shikimate kinase (aroK)
    6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
    7. Chorismate synthase (aroC)
    This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate biosynthesis.

    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

    • 3-deoxy-7-phosphoheptulonate synthase activity Source: MTBBASE
    • manganese ion binding Source: MTBBASE

    GO - Biological processi

    • aromatic amino acid family biosynthetic process Source: UniProtKB-KW
    • chorismate biosynthetic process Source: Reactome
    • growth Source: MTBBASE
    • 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.
    BRENDAi2.5.1.54. 3445.
    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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    ProteomesiUP000001584 Componenti: Chromosome

    Organism-specific databases

    TubercuListiRv2178c.

    Subcellular locationi

    GO - Cellular componenti

    • cell wall Source: MTBBASE
    • cytosol Source: Reactome
    • plasma membrane Source: MTBBASE
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 462462Phospho-2-dehydro-3-deoxyheptonate aldolase AroGPRO_0000414909Add
    BLAST

    Proteomic databases

    PRIDEiO53512.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with Rv0948c.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Rv0948cP9WIC12EBI-5241825,EBI-5241850

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    462
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni1 – 33Combined sources
    Beta strandi4 – 85Combined sources
    Helixi20 – 3011Combined sources
    Helixi42 – 5211Combined sources
    Helixi61 – 7515Combined sources
    Beta strandi80 – 856Combined sources
    Helixi91 – 933Combined sources
    Helixi96 – 11722Combined sources
    Beta strandi121 – 1266Combined sources
    Beta strandi143 – 1453Combined sources
    Turni150 – 1523Combined sources
    Beta strandi155 – 1584Combined sources
    Helixi159 – 1624Combined sources
    Helixi168 – 18821Combined sources
    Turni189 – 1924Combined sources
    Helixi194 – 20714Combined sources
    Beta strandi208 – 2103Combined sources
    Helixi211 – 23020Combined sources
    Helixi236 – 2383Combined sources
    Beta strandi244 – 2485Combined sources
    Helixi252 – 2576Combined sources
    Beta strandi259 – 2613Combined sources
    Beta strandi265 – 2684Combined sources
    Beta strandi271 – 2733Combined sources
    Beta strandi277 – 2815Combined sources
    Turni283 – 2853Combined sources
    Helixi291 – 2988Combined sources
    Beta strandi303 – 3075Combined sources
    Helixi313 – 32311Combined sources
    Beta strandi331 – 3366Combined sources
    Turni340 – 3423Combined sources
    Helixi343 – 35614Combined sources
    Beta strandi362 – 3654Combined sources
    Turni367 – 3693Combined sources
    Beta strandi371 – 3744Combined sources
    Beta strandi380 – 3834Combined sources
    Helixi384 – 40118Combined sources
    Beta strandi407 – 4126Combined sources
    Beta strandi420 – 4223Combined sources
    Turni423 – 4264Combined sources
    Helixi431 – 4333Combined sources
    Beta strandi439 – 4413Combined sources
    Helixi446 – 46116Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO53512.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the class-II DAHP synthase family.Curated

    Phylogenomic databases

    HOGENOMiHOG000242917.
    InParanoidiO53512.
    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

            10         20         30         40         50
    MNWTVDIPID QLPSLPPLPT DLRTRLDAAL AKPAAQQPTW PADQALAMRT
    60 70 80 90 100
    VLESVPPVTV PSEIVRLQEQ LAQVAKGEAF LLQGGDCAET FMDNTEPHIR
    110 120 130 140 150
    GNVRALLQMA VVLTYGASMP VVKVARIAGQ YAKPRSADID ALGLRSYRGD
    160 170 180 190 200
    MINGFAPDAA AREHDPSRLV RAYANASAAM NLVRALTSSG LASLHLVHDW
    210 220 230 240 250
    NREFVRTSPA GARYEALATE IDRGLRFMSA CGVADRNLQT AEIYASHEAL
    260 270 280 290 300
    VLDYERAMLR LSDGDDGEPQ LFDLSAHTVW IGERTRQIDG AHIAFAQVIA
    310 320 330 340 350
    NPVGVKLGPN MTPELAVEYV ERLDPHNKPG RLTLVSRMGN HKVRDLLPPI
    360 370 380 390 400
    VEKVQATGHQ VIWQCDPMHG NTHESSTGFK TRHFDRIVDE VQGFFEVHRA
    410 420 430 440 450
    LGTHPGGIHV EITGENVTEC LGGAQDISET DLAGRYETAC DPRLNTQQSL
    460
    ELAFLVAEML RD
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA. Translation: CCP44955.1.
    PIRiD70936.
    RefSeqiNP_216694.1. NC_000962.3.
    WP_003911784.1. NZ_KK339370.1.

    Genome annotation databases

    EnsemblBacteriaiCCP44955; CCP44955; Rv2178c.
    GeneIDi888309.
    KEGGimtu:Rv2178c.
    mtv:RVBD_2178c.
    PATRICi18153402. VBIMycTub87468_2429.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL123456 Genomic DNA. Translation: CCP44955.1.
    PIRiD70936.
    RefSeqiNP_216694.1. NC_000962.3.
    WP_003911784.1. NZ_KK339370.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

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

    Proteomic databases

    PRIDEiO53512.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCCP44955; CCP44955; Rv2178c.
    GeneIDi888309.
    KEGGimtu:Rv2178c.
    mtv:RVBD_2178c.
    PATRICi18153402. VBIMycTub87468_2429.

    Organism-specific databases

    TubercuListiRv2178c.

    Phylogenomic databases

    HOGENOMiHOG000242917.
    InParanoidiO53512.
    KOiK01626.
    OMAiHFEMTGQ.
    OrthoDBiEOG6H1Q0Q.
    PhylomeDBiO53512.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00084.
    BioCyciMTBRV:RV2178C-MONOMER.
    BRENDAi2.5.1.54. 3445.
    ReactomeiREACT_27268. Chorismate via Shikimate Pathway.

    Miscellaneous databases

    EvolutionaryTraceiO53512.
    PROiO53512.

    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.
    ProtoNetiSearch...

    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: July 22, 2015
    This is version 98 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.