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Protein

L-talarate/galactarate dehydratase

Gene

STM3697

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the efficient dehydration of both L-talarate and galactarate to 5-keto-4-deoxy-D-glucarate. Also catalyzes the epimerization of L-talarate to galactarate; epimerization occurs in competition with dehydration. Is required for the utilization of L-talarate as a carbon source. Also functions in galactarate utilization. Is not active on other acid sugars.1 Publication

Catalytic activityi

L-altarate = 5-dehydro-4-deoxy-D-glucarate + H2O.1 Publication
Galactarate = (2R,3S)-2,3-dihydroxy-5-oxohexanedioate + H2O.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Kineticsi

kcat is 2.1 sec(-1) with L-talarate as substrate. kcat is 3.6 sec(-1) with galactarate as substrate.

  1. KM=230 µM for L-talarate1 Publication
  2. KM=330 µM for galactarate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei195 – 1951Substrate
    Active sitei197 – 1971Proton acceptor1 Publication
    Metal bindingi226 – 2261Magnesium
    Binding sitei228 – 2281Substrate
    Metal bindingi252 – 2521Magnesium
    Metal bindingi278 – 2781Magnesium
    Sitei301 – 3011Increases basicity of active site His
    Active sitei328 – 3281Proton donor/acceptor1 Publication
    Binding sitei348 – 3481Substrate

    GO - Molecular functioni

    • galactarate dehydratase activity Source: CACAO
    • L-altrarate dehydratase activity Source: CACAO
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    • cellular amino acid catabolic process Source: InterPro
    • galactarate catabolic process Source: CACAO
    • L-altrarate catabolic process Source: CACAO
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-3722-MONOMER.
    BRENDAi4.2.1.42. 5542.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-talarate/galactarate dehydratase (EC:4.2.1.1561 Publication, EC:4.2.1.421 Publication)
    Short name:
    TalrD/GalrD
    Gene namesi
    Ordered Locus Names:STM3697
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    Proteomesi
    • UP000001014 Componenti: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene lose the ability to grow on L-talarate as carbon source, and are impaired in the ability to utilize galactarate as carbon source.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi197 – 1971K → A: Loss of dehydration activity on both L-talarate and galactarate and loss of epimerization activity. 1 Publication
    Mutagenesisi328 – 3281H → N or A: Loss of dehydration activity on both L-talarate and galactarate and loss of epimerization activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 398398L-talarate/galactarate dehydratasePRO_0000429330Add
    BLAST

    Proteomic databases

    PaxDbiQ8ZL58.
    PRIDEiQ8ZL58.

    Interactioni

    Subunit structurei

    Homooctamer; tetramer of dimers.1 Publication

    Protein-protein interaction databases

    STRINGi99287.STM3697.

    Structurei

    Secondary structure

    1
    398
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 244Combined sources
    Beta strandi28 – 4417Combined sources
    Helixi47 – 504Combined sources
    Beta strandi57 – 6913Combined sources
    Beta strandi74 – 8310Combined sources
    Helixi86 – 9611Combined sources
    Helixi97 – 1004Combined sources
    Helixi108 – 11811Combined sources
    Helixi120 – 1223Combined sources
    Helixi127 – 14620Combined sources
    Helixi151 – 1555Combined sources
    Beta strandi160 – 1667Combined sources
    Helixi176 – 18813Combined sources
    Beta strandi194 – 1974Combined sources
    Helixi203 – 21715Combined sources
    Beta strandi219 – 2213Combined sources
    Beta strandi223 – 2264Combined sources
    Helixi233 – 24311Combined sources
    Helixi244 – 2463Combined sources
    Helixi260 – 26910Combined sources
    Beta strandi274 – 2763Combined sources
    Helixi283 – 2919Combined sources
    Beta strandi296 – 2983Combined sources
    Helixi302 – 3054Combined sources
    Helixi308 – 32013Combined sources
    Helixi331 – 3399Combined sources
    Beta strandi347 – 3493Combined sources
    Helixi354 – 3563Combined sources
    Beta strandi362 – 3643Combined sources
    Beta strandi367 – 3693Combined sources
    Beta strandi372 – 3754Combined sources
    Helixi382 – 3865Combined sources
    Beta strandi388 – 3958Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PP0X-ray2.20A/B/C1-398[»]
    2PP1X-ray2.20A/B/C/D/E/F1-398[»]
    2PP3X-ray2.20A/B/C1-398[»]
    ProteinModelPortaliQ8ZL58.
    SMRiQ8ZL58. Positions 4-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8ZL58.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni46 – 483Substrate binding
    Regioni82 – 832Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105DIA. Bacteria.
    COG4948. LUCA.
    HOGENOMiHOG000113759.
    OMAiPWVEHFD.
    OrthoDBiEOG6H4K4R.
    PhylomeDBiQ8ZL58.

    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. 1 hit.
    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.
    PROSITEiPS00909. MR_MLE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8ZL58-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MALSANSDAV TYAKAANTRT AAETGDRIEW VKLSLAFLPL ATPVSDAKVL
    60 70 80 90 100
    TGRQKPLTEV AIIIAEIRSR DGFEGVGFSY SKRAGGQGIY AHAKEIADNL
    110 120 130 140 150
    LGEDPNDIDK IYTKLLWAGA SVGRSGMAVQ AISPIDIALW DMKAKRAGLP
    160 170 180 190 200
    LAKLLGAHRD SVQCYNTSGG FLHTPLDQVL KNVVISRENG IGGIKLKVGQ
    210 220 230 240 250
    PNCAEDIRRL TAVREALGDE FPLMVDANQQ WDRETAIRMG RKMEQFNLIW
    260 270 280 290 300
    IEEPLDAYDI EGHAQLAAAL DTPIATGEML TSFREHEQLI LGNASDFVQP
    310 320 330 340 350
    DAPRVGGISP FLKIMDLAAK HGRKLAPHFA MEVHLHLSAA YPLEPWLEHF
    360 370 380 390
    EWLNPLFNEQ LELRDGRMWI SDRHGLGFTL SEQARRWTQL TCEFGKRP
    Length:398
    Mass (Da):44,027
    Last modified:March 1, 2002 - v1
    Checksum:i3AE71E6203A1C900
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE006468 Genomic DNA. Translation: AAL22556.1.
    RefSeqiNP_462597.1. NC_003197.1.
    WP_001218249.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL22556; AAL22556; STM3697.
    GeneIDi1255221.
    KEGGistm:STM3697.
    PATRICi32386227. VBISalEnt20916_3910.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE006468 Genomic DNA. Translation: AAL22556.1.
    RefSeqiNP_462597.1. NC_003197.1.
    WP_001218249.1. NC_003197.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PP0X-ray2.20A/B/C1-398[»]
    2PP1X-ray2.20A/B/C/D/E/F1-398[»]
    2PP3X-ray2.20A/B/C1-398[»]
    ProteinModelPortaliQ8ZL58.
    SMRiQ8ZL58. Positions 4-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi99287.STM3697.

    Proteomic databases

    PaxDbiQ8ZL58.
    PRIDEiQ8ZL58.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL22556; AAL22556; STM3697.
    GeneIDi1255221.
    KEGGistm:STM3697.
    PATRICi32386227. VBISalEnt20916_3910.

    Phylogenomic databases

    eggNOGiENOG4105DIA. Bacteria.
    COG4948. LUCA.
    HOGENOMiHOG000113759.
    OMAiPWVEHFD.
    OrthoDBiEOG6H4K4R.
    PhylomeDBiQ8ZL58.

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-3722-MONOMER.
    BRENDAi4.2.1.42. 5542.

    Miscellaneous databases

    EvolutionaryTraceiQ8ZL58.

    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. 1 hit.
    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.
    PROSITEiPS00909. MR_MLE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    2. "Computation-facilitated assignment of the function in the enolase superfamily: a regiochemically distinct galactarate dehydratase from Oceanobacillus iheyensis."
      Rakus J.F., Kalyanaraman C., Fedorov A.A., Fedorov E.V., Mills-Groninger F.P., Toro R., Bonanno J., Bain K., Sauder J.M., Burley S.K., Almo S.C., Jacobson M.P., Gerlt J.A.
      Biochemistry 48:11546-11558(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REGIOCHEMISTRY OF THE REACTION.
      Strain: LT2 / SGSC1412 / ATCC 700720.
    3. "Evolution of enzymatic activities in the enolase superfamily: L-talarate/galactarate dehydratase from Salmonella typhimurium LT2."
      Yew W.S., Fedorov A.A., Fedorov E.V., Almo S.C., Gerlt J.A.
      Biochemistry 46:9564-9577(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-197 IN COMPLEXES WITH AN ANALOG OF THE ENOLATE INTERMEDIATE; L-GLUCARATE AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, SUBSTRATE SPECIFICITY, COFACTOR, DISRUPTION PHENOTYPE, SUBUNIT, REACTION MECHANISM, ACTIVE SITES, MUTAGENESIS OF LYS-197 AND HIS-328.
      Strain: LT2 / SGSC1412 / ATCC 700720.

    Entry informationi

    Entry nameiTAGAD_SALTY
    AccessioniPrimary (citable) accession number: Q8ZL58
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 11, 2014
    Last sequence update: March 1, 2002
    Last modified: January 20, 2016
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The enzyme product is the enantiomer of the product obtained in the galactarate dehydratase reaction catalyzed by OB2843; the enzymes thus differ in their regiochemistry of dehydration.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.