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Protein

Glucarate dehydratase

Gene

gudD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the dehydration of glucarate to 5-keto-4-deoxy-D-glucarate (5-kdGluc). Also acts on L-idarate.

Catalytic activityi

D-glucarate = 5-dehydro-4-deoxy-D-glucarate + H2O.

Cofactori

Mg2+1 Publication

Kineticsi

  1. KM=16 µM for idarate1 Publication
  2. KM=60 µM for glucarate1 Publication

    Pathwayi: D-glucarate degradation

    This protein is involved in step 1 of the subpathway that synthesizes 2,5-dioxopentanoate from D-glucarate.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Glucarate dehydratase (gudD)
    2. no protein annotated in this organism
    This subpathway is part of the pathway D-glucarate degradation, which is itself part of Carbohydrate acid metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2,5-dioxopentanoate from D-glucarate, the pathway D-glucarate degradation and in Carbohydrate acid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei32Substrate1
    Binding sitei103Substrate1
    Binding sitei150Substrate1
    Binding sitei205Substrate1
    Active sitei207Proton acceptor1
    Metal bindingi235Magnesium1
    Metal bindingi266Magnesium1
    Metal bindingi289Magnesium1
    Binding sitei289Substrate1
    Active sitei339Proton acceptor1
    Binding sitei368Substrate1
    Binding sitei422Substrate1

    GO - Molecular functioni

    • glucarate dehydratase activity Source: UniProtKB
    • magnesium ion binding Source: UniProtKB

    GO - Biological processi

    • D-glucarate catabolic process Source: UniProtKB

    Keywordsi

    Molecular functionLyase
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:GLUCARDEHYDRA-MONOMER
    MetaCyc:GLUCARDEHYDRA-MONOMER
    BRENDAi4.2.1.40 2026
    SABIO-RKiP0AES2
    UniPathwayiUPA00564; UER00627

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucarate dehydratase (EC:4.2.1.40)
    Short name:
    GDH
    Short name:
    GlucD
    Gene namesi
    Name:gudD
    Synonyms:ygcX
    Ordered Locus Names:b2787, JW2758
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13167 gudD

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi150Y → F: Reduces activity 100-fold. 1 Publication1
    Mutagenesisi207K → Q: Reduces activity 1000-fold. 1 Publication1
    Mutagenesisi207K → R: Reduces activity 10000-fold. 1 Publication1
    Mutagenesisi339H → A: Loss of activity. 1 Publication1
    Mutagenesisi339H → N: Reduces activity 10000-fold. 1 Publication1
    Mutagenesisi339H → Q: Reduces activity 1000-fold. 1 Publication1
    Mutagenesisi366D → A or N: Reduces activity over 100-fold. 1 Publication1

    Chemistry databases

    DrugBankiDB03212 4-Deoxyglucarate
    DB03603 Glucarate
    DB02325 Isopropyl Alcohol
    DB03734 Xylarohydroxamate

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001712642 – 446Glucarate dehydrataseAdd BLAST445

    Proteomic databases

    PaxDbiP0AES2
    PRIDEiP0AES2

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi4262287, 12 interactors
    IntActiP0AES2, 3 interactors
    STRINGi316385.ECDH10B_2955

    Structurei

    Secondary structure

    1446
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi9 – 21Combined sources13
    Beta strandi25 – 27Combined sources3
    Beta strandi34 – 45Combined sources12
    Beta strandi50 – 56Combined sources7
    Helixi59 – 72Combined sources14
    Helixi77 – 79Combined sources3
    Helixi80 – 90Combined sources11
    Helixi92 – 95Combined sources4
    Turni96 – 99Combined sources4
    Beta strandi101 – 104Combined sources4
    Helixi109 – 128Combined sources20
    Beta strandi130 – 132Combined sources3
    Helixi133 – 135Combined sources3
    Beta strandi143 – 147Combined sources5
    Beta strandi149 – 152Combined sources4
    Helixi157 – 159Combined sources3
    Beta strandi160 – 162Combined sources3
    Helixi173 – 177Combined sources5
    Helixi185 – 199Combined sources15
    Beta strandi202 – 207Combined sources6
    Beta strandi209 – 211Combined sources3
    Helixi213 – 226Combined sources14
    Beta strandi230 – 235Combined sources6
    Helixi242 – 251Combined sources10
    Turni252 – 255Combined sources4
    Beta strandi256 – 261Combined sources6
    Helixi271 – 282Combined sources12
    Beta strandi286 – 291Combined sources6
    Helixi295 – 304Combined sources10
    Beta strandi308 – 311Combined sources4
    Helixi314 – 317Combined sources4
    Helixi319 – 331Combined sources13
    Helixi345 – 356Combined sources12
    Helixi369 – 372Combined sources4
    Turni373 – 375Combined sources3
    Beta strandi378 – 381Combined sources4
    Beta strandi389 – 391Combined sources3
    Beta strandi395 – 397Combined sources3
    Helixi404 – 416Combined sources13
    Helixi425 – 429Combined sources5

    3D structure databases

    ProteinModelPortaliP0AES2
    SMRiP0AES2
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AES2

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni235 – 237Substrate binding3
    Regioni339 – 341Substrate binding3

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105EQX Bacteria
    COG4948 LUCA
    HOGENOMiHOG000238021
    InParanoidiP0AES2
    KOiK01706
    OMAiRVAQMCN
    PhylomeDBiP0AES2

    Family and domain databases

    CDDicd03323 D-glucarate_dehydratase, 1 hit
    Gene3Di3.20.20.120, 1 hit
    3.30.390.10, 2 hits
    InterProiView protein in InterPro
    IPR036849 Enolase-like_C_sf
    IPR029017 Enolase-like_N
    IPR034390 Enolase-like_superfamily
    IPR029065 Enolase_C-like
    IPR017653 Glucarate_dehydratase
    IPR034598 GlucD-like
    IPR013342 Mandelate_racemase_C
    PfamiView protein in Pfam
    PF13378 MR_MLE_C, 1 hit
    SFLDiSFLDG00055 glucarate_dehydratase, 1 hit
    SFLDS00001 Enolase, 1 hit
    SMARTiView protein in SMART
    SM00922 MR_MLE, 1 hit
    SUPFAMiSSF51604 SSF51604, 1 hit
    TIGRFAMsiTIGR03247 glucar-dehydr, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0AES2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSSQFTTPVV TEMQVIPVAG HDSMLMNLSG AHAPFFTRNI VIIKDNSGHT
    60 70 80 90 100
    GVGEIPGGEK IRKTLEDAIP LVVGKTLGEY KNVLTLVRNT FADRDAGGRG
    110 120 130 140 150
    LQTFDLRTTI HVVTGIEAAM LDLLGQHLGV NVASLLGDGQ QRSEVEMLGY
    160 170 180 190 200
    LFFVGNRKAT PLPYQSQPDD SCDWYRLRHE EAMTPDAVVR LAEAAYEKYG
    210 220 230 240 250
    FNDFKLKGGV LAGEEEAESI VALAQRFPQA RITLDPNGAW SLNEAIKIGK
    260 270 280 290 300
    YLKGSLAYAE DPCGAEQGFS GREVMAEFRR ATGLPTATNM IATDWRQMGH
    310 320 330 340 350
    TLSLQSVDIP LADPHFWTMQ GSVRVAQMCH EFGLTWGSHS NNHFDISLAM
    360 370 380 390 400
    FTHVAAAAPG KITAIDTHWI WQEGNQRLTK EPFEIKGGLV QVPEKPGLGV
    410 420 430 440
    EIDMDQVMKA HELYQKHGLG ARDDAMGMQY LIPGWTFDNK RPCMVR
    Length:446
    Mass (Da):49,141
    Last modified:January 23, 2007 - v2
    Checksum:iDFB07C9CA33F542C
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti310 – 313PLAD → RWRI in AAB40437 (PubMed:9278503).Curated4

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA Translation: AAC75829.1
    U29581 Genomic DNA Translation: AAB40437.1
    AP009048 Genomic DNA Translation: BAA16572.2
    PIRiG65060
    RefSeqiNP_417267.1, NC_000913.3
    WP_000098255.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC75829; AAC75829; b2787
    BAA16572; BAA16572; BAA16572
    GeneIDi947258
    KEGGiecj:JW2758
    eco:b2787
    PATRICifig|1411691.4.peg.3947

    Similar proteinsi

    Entry informationi

    Entry nameiGUDD_ECOLI
    AccessioniPrimary (citable) accession number: P0AES2
    Secondary accession number(s): P76637, P78217, Q46914
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: January 23, 2007
    Last modified: March 28, 2018
    This is version 102 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    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

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