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O53512

- AROG_MYCTU

UniProt

O53512 - AROG_MYCTU

Protein

Phospho-2-dehydro-3-deoxyheptonate aldolase AroG

Gene

aroG

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    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)1 Publication

    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

    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

    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
    MT0975P647672EBI-5241825,EBI-5241850From a different organism.

    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 – 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.
    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.
    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

    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: October 1, 2014
    This is version 89 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