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Protein

D-galactarolactone isomerase

Gene

Atu3138

Organism
Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the isomerization of D-galactaro-1,5-lactone to D-galactaro-1,4-lactone. This is a step in the oxidative degradation pathway of D-galacturonate, which allows A.tumefaciens to utilize D-galacturonate as a sole carbon source.1 Publication

Catalytic activityi

D-galactaro-1,5-lactone = D-galactaro-1,4-lactone.1 Publication

Cofactori

Note: Does not require a metal cofactor.1 Publication

Kineticsi

kcat is 440 sec(-1).
  1. KM=5.3 mM for D-galactaro-1,5-lactone1 Publication

    Pathwayi: D-galacturonate degradation via prokaryotic oxidative pathway

    This protein is involved in the pathway D-galacturonate degradation via prokaryotic oxidative pathway, which is part of Carbohydrate acid metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway D-galacturonate degradation via prokaryotic oxidative pathway and in Carbohydrate acid metabolism.

    GO - Molecular functioni

    Keywordsi

    Molecular functionIsomerase

    Enzyme and pathway databases

    BioCyciAGRO:ATU3138-MONOMER
    MetaCyc:MONOMER-19230
    UniPathwayiUPA01050

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-galactarolactone isomerase (EC:5.4.1.41 Publication)
    Short name:
    GLI
    Alternative name(s):
    Galactaro delta-lactone isomerase
    Gene namesi
    Ordered Locus Names:Atu3138
    OrganismiAgrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
    Taxonomic identifieri176299 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex
    Proteomesi
    • UP000000813 Componenti: Chromosome linear

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi240N → D: 28-fold decrease in enzymatic activity. Does not gain the ability to hydrolyze D-galactaro-1,5-lactone or D-galactaro-1,4-lactone. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004294321 – 292D-galactarolactone isomeraseAdd BLAST292

    Interactioni

    Protein-protein interaction databases

    STRINGi176299.Atu3138

    Structurei

    Secondary structure

    1292
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi22 – 26Combined sources5
    Beta strandi44 – 46Combined sources3
    Helixi50 – 60Combined sources11
    Beta strandi64 – 68Combined sources5
    Helixi71 – 73Combined sources3
    Helixi78 – 87Combined sources10
    Helixi88 – 90Combined sources3
    Beta strandi91 – 95Combined sources5
    Helixi103 – 111Combined sources9
    Beta strandi114 – 120Combined sources7
    Helixi129 – 131Combined sources3
    Helixi132 – 141Combined sources10
    Beta strandi145 – 149Combined sources5
    Helixi152 – 154Combined sources3
    Helixi155 – 163Combined sources9
    Beta strandi167 – 171Combined sources5
    Helixi173 – 176Combined sources4
    Helixi186 – 197Combined sources12
    Beta strandi200 – 204Combined sources5
    Helixi207 – 209Combined sources3
    Helixi218 – 230Combined sources13
    Helixi232 – 234Combined sources3
    Beta strandi235 – 237Combined sources3
    Helixi249 – 251Combined sources3
    Helixi255 – 263Combined sources9
    Beta strandi266 – 268Combined sources3
    Helixi269 – 276Combined sources8
    Helixi278 – 284Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4MUPX-ray1.60A/B/C1-292[»]
    ProteinModelPortaliA9CEQ7
    SMRiA9CEQ7
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105GAK Bacteria
    COG3618 LUCA
    HOGENOMiHOG000107488
    KOiK18982
    OMAiRIVWGTN

    Family and domain databases

    InterProiView protein in InterPro
    IPR006680 Amidohydro-rel
    IPR032466 Metal_Hydrolase
    PfamiView protein in Pfam
    PF04909 Amidohydro_2, 1 hit
    SUPFAMiSSF51556 SSF51556, 1 hit

    Sequencei

    Sequence statusi: Complete.

    A9CEQ7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSELVRKLSG TAPNPAFPRG AVDTQMHMYL PGYPALPGGP GLPPGALPGP
    60 70 80 90 100
    EDYRRLMQWL GIDRVIITQG NAHQRDNGNT LACVAEMGEA AHAVVIIDAT
    110 120 130 140 150
    TTEKDMEKLT AAGTVGARIM DLPGGAVNLS ELDAVDERAH AADWMVAVQF
    160 170 180 190 200
    DGNGLLDHLP RLQKIRSRWV FDHHGKFFKG IRTDGPEMAA LLKLIDRGNL
    210 220 230 240 250
    WFKFAGVYES SRKSWPYADV AAFSRVIAAH APERIVWGTN WPHNSVRETA
    260 270 280 290
    AYPDDARLAE LTLGWLPDEA ARHRALVENP EALFKLSPVK AT
    Length:292
    Mass (Da):31,983
    Last modified:January 15, 2008 - v1
    Checksum:i4596112829F94E4B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE007870 Genomic DNA Translation: AAK90248.1
    PIRiAD2942
    F98340
    RefSeqiNP_357463.1, NC_003063.2
    WP_010972788.1, NC_003063.2

    Genome annotation databases

    EnsemblBacteriaiAAK90248; AAK90248; Atu3138
    GeneIDi1140387
    KEGGiatu:Atu3138
    PATRICifig|176299.10.peg.2983

    Similar proteinsi

    Entry informationi

    Entry nameiGLI_AGRFC
    AccessioniPrimary (citable) accession number: A9CEQ7
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 11, 2014
    Last sequence update: January 15, 2008
    Last modified: July 5, 2017
    This is version 51 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

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