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Protein

Glucarate dehydratase-related protein

Gene

gudX

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Does not seem to have an in-vivo activity on glucarate or idarate. Its real substrate is unknown.

Cofactori

Kineticsi

  1. KM=170 µM for idarate1 Publication
  2. KM=320 µM for glucarate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei31SubstrateBy similarity1
    Binding sitei104SubstrateBy similarity1
    Binding sitei149SubstrateBy similarity1
    Binding sitei204SubstrateBy similarity1
    Active sitei206Proton acceptorSequence analysis1
    Metal bindingi234MagnesiumSequence analysis1
    Metal bindingi265MagnesiumSequence analysis1
    Metal bindingi288MagnesiumSequence analysis1
    Binding sitei288SubstrateBy similarity1
    Active sitei338Proton acceptorSequence analysis1
    Binding sitei367SubstrateBy similarity1
    Binding sitei421SubstrateBy similarity1

    GO - Molecular functioni

    GO - Biological processi

    • cellular amino acid catabolic process Source: InterPro
    • cellular catabolic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:G7446-MONOMER.
    ECOL316407:JW2759-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucarate dehydratase-related protein (EC:4.2.1.-)
    Short name:
    GDH-RP
    Short name:
    GlucDRP
    Gene namesi
    Name:gudX
    Synonyms:ygcY
    Ordered Locus Names:b2788, JW2759
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13168. gudX.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001712661 – 446Glucarate dehydratase-related proteinAdd BLAST446

    Proteomic databases

    PaxDbiQ46915.
    PRIDEiQ46915.

    Interactioni

    Protein-protein interaction databases

    BioGridi4260899. 20 interactors.
    IntActiQ46915. 3 interactors.
    STRINGi511145.b2788.

    Structurei

    Secondary structure

    1446
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi8 – 20Combined sources13
    Beta strandi24 – 26Combined sources3
    Beta strandi33 – 44Combined sources12
    Beta strandi49 – 55Combined sources7
    Helixi58 – 66Combined sources9
    Helixi68 – 71Combined sources4
    Helixi76 – 78Combined sources3
    Helixi79 – 90Combined sources12
    Helixi92 – 99Combined sources8
    Helixi104 – 106Combined sources3
    Helixi107 – 127Combined sources21
    Helixi131 – 134Combined sources4
    Beta strandi142 – 146Combined sources5
    Beta strandi148 – 150Combined sources3
    Helixi156 – 158Combined sources3
    Beta strandi169 – 171Combined sources3
    Helixi173 – 176Combined sources4
    Helixi184 – 198Combined sources15
    Beta strandi201 – 206Combined sources6
    Beta strandi208 – 210Combined sources3
    Helixi212 – 225Combined sources14
    Beta strandi229 – 234Combined sources6
    Helixi241 – 247Combined sources7
    Turni248 – 250Combined sources3
    Turni252 – 254Combined sources3
    Beta strandi256 – 260Combined sources5
    Helixi270 – 281Combined sources12
    Beta strandi285 – 290Combined sources6
    Helixi294 – 302Combined sources9
    Beta strandi307 – 310Combined sources4
    Helixi313 – 316Combined sources4
    Helixi318 – 330Combined sources13
    Helixi344 – 355Combined sources12
    Helixi368 – 371Combined sources4
    Turni372 – 374Combined sources3
    Beta strandi378 – 380Combined sources3
    Beta strandi388 – 390Combined sources3
    Beta strandi394 – 396Combined sources3
    Helixi403 – 414Combined sources12
    Helixi424 – 430Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4GYPX-ray2.10C/D2-446[»]
    4IL0X-ray2.80A/B/C/D/E/F/G/H1-446[»]
    ProteinModelPortaliQ46915.
    SMRiQ46915.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni234 – 236Substrate bindingBy similarity3
    Regioni338 – 340Substrate bindingBy similarity3

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105EQX. Bacteria.
    COG4948. LUCA.
    HOGENOMiHOG000238021.
    InParanoidiQ46915.
    KOiK13918.
    OMAiREMNHAL.
    PhylomeDBiQ46915.

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    InterProiIPR029065. Enolase_C-like.
    IPR029017. Enolase_N-like.
    IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
    IPR013342. Mandelate_racemase_C.
    IPR013341. Mandelate_racemase_N_dom.
    IPR001354. MR/MLE/MAL.
    [Graphical view]
    PANTHERiPTHR13794. PTHR13794. 2 hits.
    PfamiPF13378. MR_MLE_C. 1 hit.
    PF02746. MR_MLE_N. 1 hit.
    [Graphical view]
    SMARTiSM00922. MR_MLE. 1 hit.
    [Graphical view]
    SUPFAMiSSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    PROSITEiPS00908. MR_MLE_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q46915-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MATQSSPVIT DMKVIPVAGH DSMLLNIGGA HNAYFTRNIV VLTDNAGHTG
    60 70 80 90 100
    IGEAPGGDVI YQTLVDAIPM VLGQEVARLN KVVQQVHKGN QAADFDTFGK
    110 120 130 140 150
    GAWTFELRVN AVAALEAALL DLLGKALNVP VCELLGPGKQ REAITVLGYL
    160 170 180 190 200
    FYIGDRTKTD LPYVENTPGN HEWYQLRHQK AMNSEAVVRL AEASQDRYGF
    210 220 230 240 250
    KDFKLKGGVL PGEQEIDTVR ALKKRFPDAR ITVDPNGAWL LDEAISLCKG
    260 270 280 290 300
    LNDVLTYAED PCGAEQGFSG REVMAEFRRA TGLPVATNMI ATNWREMGHA
    310 320 330 340 350
    VMLNAVDIPL ADPHFWTLSG AVRVAQLCDD WGLTWGCHSN NHFDISLAMF
    360 370 380 390 400
    THVGAAAPGN PTAIDTHWIW QEGDCRLTQN PLEIKNGKIA VPDAPGLGVE
    410 420 430 440
    LDWEQVQKAH EAYKRLPGGA RNDAGPMQYL IPGWTFDRKR PVFGRH
    Length:446
    Mass (Da):48,850
    Last modified:November 1, 1996 - v1
    Checksum:i9010C7FAAE4FBE49
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U29581 Genomic DNA. Translation: AAB40438.1.
    U00096 Genomic DNA. Translation: AAC75830.1.
    AP009048 Genomic DNA. Translation: BAE76860.1.
    PIRiH65060.
    RefSeqiNP_417268.1. NC_000913.3.
    WP_000235391.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75830; AAC75830; b2788.
    BAE76860; BAE76860; BAE76860.
    GeneIDi947261.
    KEGGiecj:JW2759.
    eco:b2788.
    PATRICi32120992. VBIEscCol129921_2888.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U29581 Genomic DNA. Translation: AAB40438.1.
    U00096 Genomic DNA. Translation: AAC75830.1.
    AP009048 Genomic DNA. Translation: BAE76860.1.
    PIRiH65060.
    RefSeqiNP_417268.1. NC_000913.3.
    WP_000235391.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4GYPX-ray2.10C/D2-446[»]
    4IL0X-ray2.80A/B/C/D/E/F/G/H1-446[»]
    ProteinModelPortaliQ46915.
    SMRiQ46915.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260899. 20 interactors.
    IntActiQ46915. 3 interactors.
    STRINGi511145.b2788.

    Proteomic databases

    PaxDbiQ46915.
    PRIDEiQ46915.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75830; AAC75830; b2788.
    BAE76860; BAE76860; BAE76860.
    GeneIDi947261.
    KEGGiecj:JW2759.
    eco:b2788.
    PATRICi32120992. VBIEscCol129921_2888.

    Organism-specific databases

    EchoBASEiEB2960.
    EcoGeneiEG13168. gudX.

    Phylogenomic databases

    eggNOGiENOG4105EQX. Bacteria.
    COG4948. LUCA.
    HOGENOMiHOG000238021.
    InParanoidiQ46915.
    KOiK13918.
    OMAiREMNHAL.
    PhylomeDBiQ46915.

    Enzyme and pathway databases

    BioCyciEcoCyc:G7446-MONOMER.
    ECOL316407:JW2759-MONOMER.

    Miscellaneous databases

    PROiQ46915.

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    InterProiIPR029065. Enolase_C-like.
    IPR029017. Enolase_N-like.
    IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
    IPR013342. Mandelate_racemase_C.
    IPR013341. Mandelate_racemase_N_dom.
    IPR001354. MR/MLE/MAL.
    [Graphical view]
    PANTHERiPTHR13794. PTHR13794. 2 hits.
    PfamiPF13378. MR_MLE_C. 1 hit.
    PF02746. MR_MLE_N. 1 hit.
    [Graphical view]
    SMARTiSM00922. MR_MLE. 1 hit.
    [Graphical view]
    SUPFAMiSSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    PROSITEiPS00908. MR_MLE_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGUDX_ECOLI
    AccessioniPrimary (citable) accession number: Q46915
    Secondary accession number(s): Q2MA46
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: November 2, 2016
    This is version 108 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, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.