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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

    Pathwayi: chorismate 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 (LH57_11870), Phospho-2-dehydro-3-deoxyheptonate aldolase AroG (aroG)
    2. 3-dehydroquinate synthase (aroB), 3-dehydroquinate synthase (aroB)
    3. 3-dehydroquinate dehydratase (aroQ), 3-dehydroquinate dehydratase (aroQ)
    4. no protein annotated in this organism
    5. Shikimate kinase (aroK), Shikimate kinase (aroK)
    6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA), 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
    7. Chorismate synthase (aroC), 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)DescriptionActionsGraphical viewLength
    Metal bindingi87Divalent cations1
    Binding sitei126Substrate1
    Binding sitei306Substrate1
    Binding sitei337Substrate1
    Metal bindingi369Divalent cations1
    Metal bindingi411Divalent cations1
    Metal bindingi441Divalent cations1

    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
    • cellular amino acid 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

    BioCyciMTBH37RV:G185E-6388-MONOMER.
    BRENDAi2.5.1.54. 3445.
    ReactomeiR-MTU-964903. 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
    Proteomesi
    • UP000001584 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)DescriptionActionsGraphical viewLength
    ChainiPRO_00004149091 – 462Phospho-2-dehydro-3-deoxyheptonate aldolase AroGAdd BLAST462

    Proteomic databases

    PaxDbiO53512.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with Rv0948c.1 Publication

    Binary interactionsi

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

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1462
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni1 – 3Combined sources3
    Beta strandi4 – 8Combined sources5
    Helixi20 – 30Combined sources11
    Helixi42 – 52Combined sources11
    Helixi61 – 75Combined sources15
    Beta strandi80 – 85Combined sources6
    Helixi91 – 93Combined sources3
    Helixi96 – 117Combined sources22
    Beta strandi121 – 126Combined sources6
    Beta strandi143 – 145Combined sources3
    Turni150 – 152Combined sources3
    Beta strandi155 – 158Combined sources4
    Helixi159 – 162Combined sources4
    Helixi168 – 188Combined sources21
    Turni189 – 192Combined sources4
    Helixi194 – 207Combined sources14
    Beta strandi208 – 210Combined sources3
    Helixi211 – 230Combined sources20
    Helixi236 – 238Combined sources3
    Beta strandi244 – 248Combined sources5
    Helixi252 – 257Combined sources6
    Beta strandi259 – 261Combined sources3
    Beta strandi265 – 268Combined sources4
    Beta strandi271 – 273Combined sources3
    Beta strandi277 – 281Combined sources5
    Turni283 – 285Combined sources3
    Helixi291 – 298Combined sources8
    Beta strandi303 – 307Combined sources5
    Helixi313 – 323Combined sources11
    Beta strandi331 – 336Combined sources6
    Turni340 – 342Combined sources3
    Helixi343 – 356Combined sources14
    Beta strandi362 – 365Combined sources4
    Turni367 – 369Combined sources3
    Beta strandi371 – 374Combined sources4
    Beta strandi380 – 383Combined sources4
    Helixi384 – 401Combined sources18
    Beta strandi407 – 412Combined sources6
    Beta strandi420 – 422Combined sources3
    Turni423 – 426Combined sources4
    Helixi431 – 433Combined sources3
    Beta strandi439 – 441Combined sources3
    Helixi446 – 461Combined sources16

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    5CKVX-ray2.79A/B1-462[»]
    5CKXX-ray2.70A/B1-462[»]
    5E2LX-ray2.50A/B1-462[»]
    5E40X-ray2.05A/B1-462[»]
    5E4NX-ray2.05A/B1-462[»]
    5E5GX-ray1.95A/B1-462[»]
    5E7ZX-ray2.40A/B1-462[»]
    5EX4X-ray2.25A/B1-462[»]
    ProteinModelPortaliO53512.
    SMRiO53512.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO53512.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni283 – 284Substrate binding2

    Sequence similaritiesi

    Belongs to the class-II DAHP synthase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105C7V. Bacteria.
    COG3200. LUCA.
    HOGENOMiHOG000242917.
    InParanoidiO53512.
    KOiK01626.
    OMAiGGVHFEM.
    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.
    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
    PDB 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[»]
    5CKVX-ray2.79A/B1-462[»]
    5CKXX-ray2.70A/B1-462[»]
    5E2LX-ray2.50A/B1-462[»]
    5E40X-ray2.05A/B1-462[»]
    5E4NX-ray2.05A/B1-462[»]
    5E5GX-ray1.95A/B1-462[»]
    5E7ZX-ray2.40A/B1-462[»]
    5EX4X-ray2.25A/B1-462[»]
    ProteinModelPortaliO53512.
    SMRiO53512.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

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

    Proteomic databases

    PaxDbiO53512.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    TubercuListiRv2178c.

    Phylogenomic databases

    eggNOGiENOG4105C7V. Bacteria.
    COG3200. LUCA.
    HOGENOMiHOG000242917.
    InParanoidiO53512.
    KOiK01626.
    OMAiGGVHFEM.
    PhylomeDBiO53512.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00084.
    BioCyciMTBH37RV:G185E-6388-MONOMER.
    BRENDAi2.5.1.54. 3445.
    ReactomeiR-MTU-964903. 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...

    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: November 2, 2016
    This is version 107 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

    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 one 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.