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Q57843

- ADHS_METJA

UniProt

Q57843 - ADHS_METJA

Protein

2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase

Gene

aroA'

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. Can also catalyze the cleavage of fructose-1,6-bisphosphate (FBP) to glyceraldehyde-3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).2 PublicationsUniRule annotation

    Catalytic activityi

    L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + 2,3-dioxopropylaldehyde phosphate.1 PublicationUniRule annotation

    Enzyme regulationi

    Inhibited by NaBH4 in the presence of FBP.1 Publication

    Kineticsi

    1. KM=430 µM for fructose-1,6-bisphosphate (at pH 7 and 50 degrees Celsius)1 Publication

    Vmax=33 nmol/min/mg enzyme for the FBP aldolase activity (at pH 7 and 50 degrees Celsius)1 Publication

    Temperature dependencei

    Optimum temperature is not reached at 100 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei33 – 331Proton acceptorCurated
    Active sitei153 – 1531Proton donorCurated
    Active sitei184 – 1841Schiff-base intermediate with substrate

    GO - Molecular functioni

    1. hydro-lyase activity Source: InterPro
    2. transferase activity, transferring aldehyde or ketonic groups Source: UniProtKB-HAMAP

    GO - Biological processi

    1. aromatic amino acid family biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14592.
    SABIO-RKQ57843.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthaseUniRule annotation (EC:2.2.1.10UniRule annotation)
    Short name:
    ADH synthaseUniRule annotation
    Short name:
    ADHSUniRule annotation
    Short name:
    ADTH synthaseUniRule annotation
    Alternative name(s):
    Transaldolase-like ADHS
    Gene namesi
    Name:aroA'UniRule annotation
    Ordered Locus Names:MJ0400
    OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
    Taxonomic identifieri243232 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
    ProteomesiUP000000805: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2732732-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthasePRO_0000138957Add
    BLAST

    Interactioni

    Subunit structurei

    Homodecamer.1 PublicationUniRule annotation

    Protein-protein interaction databases

    STRINGi243232.MJ0400.

    Structurei

    Secondary structure

    1
    273
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni3 – 64
    Helixi10 – 167
    Turni17 – 193
    Turni22 – 243
    Beta strandi27 – 315
    Helixi34 – 385
    Beta strandi44 – 463
    Helixi47 – 5711
    Beta strandi60 – 645
    Helixi66 – 705
    Beta strandi75 – 773
    Beta strandi81 – 855
    Beta strandi93 – 953
    Helixi105 – 1106
    Beta strandi114 – 1229
    Helixi127 – 14418
    Beta strandi148 – 1547
    Helixi165 – 17713
    Beta strandi181 – 1855
    Helixi191 – 20010
    Beta strandi205 – 2084
    Helixi216 – 22914
    Beta strandi232 – 2354
    Helixi238 – 2414
    Beta strandi243 – 2453
    Helixi246 – 25914
    Helixi263 – 2675

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QJGX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-273[»]
    2QJHX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-273[»]
    2QJIX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-273[»]
    ProteinModelPortaliQ57843.
    SMRiQ57843. Positions 1-272.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ57843.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni33 – 375DKFP binding
    Regioni153 – 1553DKFP binding
    Regioni209 – 2102DKFP binding
    Regioni237 – 2382DKFP binding

    Sequence similaritiesi

    Belongs to the DeoC/FbaB aldolase family. ADHS subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1830.
    KOiK16306.
    OMAiGNPYNAT.
    PhylomeDBiQ57843.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00960. ADH_synthase.
    InterProiIPR010210. ADH_synthase.
    IPR013785. Aldolase_TIM.
    IPR002915. DeoC/FbaB/lacD_aldolase.
    [Graphical view]
    PfamiPF01791. DeoC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038992. Aldolase_Ia. 1 hit.
    TIGRFAMsiTIGR01949. AroFGH_arch. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q57843-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELFKDIKNL GKLVRLERIF NRESEKTVIV PMDHGVSNGP IKGLIDIRKT    50
    VNDVAEGGAN AVLLHKGIVR HGHRGYGKDV GLIIHLSGGT AISPNPLKKV 100
    IVTTVEEAIR MGADAVSIHV NVGSDEDWEA YRDLGMIAET CEYWGMPLIA 150
    MMYPRGKHIQ NERDPELVAH AARLGAELGA DIVKTSYTGD IDSFRDVVKG 200
    CPAPVVVAGG PKTNTDEEFL QMIKDAMEAG AAGVAVGRNI FQHDDVVGIT 250
    RAVCKIVHEN ADVEEALKEI RKK 273
    Length:273
    Mass (Da):29,675
    Last modified:November 1, 1996 - v1
    Checksum:i06DDA2E51E8275E6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77117 Genomic DNA. Translation: AAB98389.1.
    PIRiH64349.
    RefSeqiNP_247374.1. NC_000909.1.
    WP_010869899.1. NC_000909.1.

    Genome annotation databases

    EnsemblBacteriaiAAB98389; AAB98389; MJ_0400.
    GeneIDi1451260.
    KEGGimja:MJ_0400.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77117 Genomic DNA. Translation: AAB98389.1 .
    PIRi H64349.
    RefSeqi NP_247374.1. NC_000909.1.
    WP_010869899.1. NC_000909.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QJG X-ray 2.60 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 1-273 [» ]
    2QJH X-ray 2.60 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 1-273 [» ]
    2QJI X-ray 2.80 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 1-273 [» ]
    ProteinModelPortali Q57843.
    SMRi Q57843. Positions 1-272.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243232.MJ0400.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB98389 ; AAB98389 ; MJ_0400 .
    GeneIDi 1451260.
    KEGGi mja:MJ_0400.

    Phylogenomic databases

    eggNOGi COG1830.
    KOi K16306.
    OMAi GNPYNAT.
    PhylomeDBi Q57843.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-14592.
    SABIO-RK Q57843.

    Miscellaneous databases

    EvolutionaryTracei Q57843.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_00960. ADH_synthase.
    InterProi IPR010210. ADH_synthase.
    IPR013785. Aldolase_TIM.
    IPR002915. DeoC/FbaB/lacD_aldolase.
    [Graphical view ]
    Pfami PF01791. DeoC. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038992. Aldolase_Ia. 1 hit.
    TIGRFAMsi TIGR01949. AroFGH_arch. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
    2. "L-aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii."
      White R.H.
      Biochemistry 43:7618-7627(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN ADH SYNTHASE.
    3. "MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity."
      Samland A.K., Wang M., Sprenger G.A.
      FEMS Microbiol. Lett. 281:36-41(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A FBP ALDOLASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    4. "Structure of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, a catalyst in the archaeal pathway for the biosynthesis of aromatic amino acids."
      Morar M., White R.H., Ealick S.E.
      Biochemistry 46:10562-10571(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, REACTION MECHANISM, SUBUNIT.

    Entry informationi

    Entry nameiADHS_METJA
    AccessioniPrimary (citable) accession number: Q57843
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 83 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. Methanococcus jannaschii
      Methanococcus jannaschii: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3