Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 135 (02 Dec 2020)
Sequence version 2 (01 Nov 1995)
Previous versions | rss
Add a publicationFeedback
Protein

Galactarate dehydratase (L-threo-forming)

Gene

garD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the dehydration of galactarate to form 5-dehydro-4-deoxy-D-glucarate (5-KDG).UniRule annotation2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Fe2+1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 22 sec(-1).1 Publication
  1. KM=800 µM for galactarate1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: galactarate degradation

    This protein is involved in step 1 of the subpathway that synthesizes D-glycerate from galactarate.UniRule annotation1 Publication
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Galactarate dehydratase (L-threo-forming) (garD), Galactarate dehydratase (L-threo-forming) (garD)
    2. 5-keto-4-deoxy-D-glucarate aldolase (garL), 5-keto-4-deoxy-D-glucarate aldolase (garL)
    3. 2-hydroxy-3-oxopropionate reductase (garR), 2-hydroxy-3-oxopropionate reductase (garR)
    This subpathway is part of the pathway galactarate 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 D-glycerate from galactarate, the pathway galactarate degradation and in Carbohydrate acid metabolism.

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    • galactarate dehydratase activity Source: EcoCyc

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionLyase
    LigandIron, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:GALACTARDEHYDRA-MONOMER
    MetaCyc:GALACTARDEHYDRA-MONOMER

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00565;UER00629

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Galactarate dehydratase (L-threo-forming)1 PublicationUniRule annotation (EC:4.2.1.42UniRule annotation1 Publication)
    Short name:
    GalcD1 PublicationUniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:garD1 PublicationUniRule annotation
    Synonyms:yhaG
    Ordered Locus Names:b3128, JW3097
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001722851 – 523Galactarate dehydratase (L-threo-forming)Add BLAST523

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P39829

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P39829

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P39829

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Induced by galactarate, D-glucarate and D-glycerate.1 Publication

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    4259485, 24 interactors
    851954, 1 interactor

    Protein interaction database and analysis system

    More...
    IntActi
    P39829, 5 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b3128

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1523
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P39829

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P39829

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    Consists of three domains. The N-terminal SAF domain, which forms a beta-clip fold, is likely involved in the substrate recognition. It is connected by a long unstructured linker to the second domain, which serves as a dimerization interface between two monomers. The C-terminal domain represents the catalytic core of the protein and probably contains the metal binding site.1 Publication

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the UxaA family.UniRule annotationCurated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG2721, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_029189_0_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P39829

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P39829

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_02031, Galactar_dehydrat, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR007392, Gal/Altron_deHydtase_C
    IPR017654, GarD-like
    IPR032893, GarD_Enterobacteriaceae
    IPR013974, SAF

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF04295, GD_AH_C, 1 hit
    PF08666, SAF, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00858, SAF, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR03248, galactar-dH20, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    P39829-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MANIEIRQET PTAFYIKVHD TDNVAIIVND NGLKAGTRFP DGLELIEHIP
    60 70 80 90 100
    QGHKVALLDI PANGEIIRYG EVIGYAVRAI PRGSWIDESM VVLPEAPPLH
    110 120 130 140 150
    TLPLATKVPE PLPPLEGYTF EGYRNADGSV GTKNLLGITT SVHCVAGVVD
    160 170 180 190 200
    YVVKIIERDL LPKYPNVDGV VGLNHLYGCG VAINAPAAVV PIRTIHNISL
    210 220 230 240 250
    NPNFGGEVMV IGLGCEKLQP ERLLTGTDDV QAIPVESASI VSLQDEKHVG
    260 270 280 290 300
    FQSMVEDILQ IAERHLQKLN QRQRETCPAS ELVVGMQCGG SDAFSGVTAN
    310 320 330 340 350
    PAVGYASDLL VRCGATVMFS EVTEVRDAIH LLTPRAVNEE VGKRLLEEME
    360 370 380 390 400
    WYDNYLNMGK TDRSANPSPG NKKGGLANVV EKALGSIAKS GKSAIVEVLS
    410 420 430 440 450
    PGQRPTKRGL IYAATPASDF VCGTQQVASG ITVQVFTTGR GTPYGLMAVP
    460 470 480 490 500
    VIKMATRTEL ANRWFDLMDI NAGTIATGEE TIEEVGWKLF HFILDVASGK
    510 520
    KKTFSDQWGL HNQLAVFNPA PVT
    Length:523
    Mass (Da):56,402
    Last modified:November 1, 1995 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i919BCC8B49411BB0
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    U18997 Genomic DNA Translation: AAA57931.1
    U00096 Genomic DNA Translation: AAC76162.1
    AP009048 Genomic DNA Translation: BAE77175.1
    M30178 Genomic DNA No translation available.

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    D65102

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417597.1, NC_000913.3
    WP_001273753.1, NZ_CP014272.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC76162; AAC76162; b3128
    BAE77175; BAE77175; BAE77175

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    947641

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW3097
    eco:b3128

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.3603

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U18997 Genomic DNA Translation: AAA57931.1
    U00096 Genomic DNA Translation: AAC76162.1
    AP009048 Genomic DNA Translation: BAE77175.1
    M30178 Genomic DNA No translation available.
    PIRiD65102
    RefSeqiNP_417597.1, NC_000913.3
    WP_001273753.1, NZ_CP014272.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3LAZX-ray1.92A/B1-96[»]
    6U7LX-ray2.75A/B/C/D1-523[»]
    SMRiP39829
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4259485, 24 interactors
    851954, 1 interactor
    IntActiP39829, 5 interactors
    STRINGi511145.b3128

    Proteomic databases

    jPOSTiP39829
    PaxDbiP39829
    PRIDEiP39829

    Genome annotation databases

    EnsemblBacteriaiAAC76162; AAC76162; b3128
    BAE77175; BAE77175; BAE77175
    GeneIDi947641
    KEGGiecj:JW3097
    eco:b3128
    PATRICifig|1411691.4.peg.3603

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB2413

    Phylogenomic databases

    eggNOGiCOG2721, Bacteria
    HOGENOMiCLU_029189_0_0_6
    InParanoidiP39829
    PhylomeDBiP39829

    Enzyme and pathway databases

    UniPathwayiUPA00565;UER00629
    BioCyciEcoCyc:GALACTARDEHYDRA-MONOMER
    MetaCyc:GALACTARDEHYDRA-MONOMER

    Miscellaneous databases

    EvolutionaryTraceiP39829

    Protein Ontology

    More...
    PROi
    PR:P39829

    Family and domain databases

    HAMAPiMF_02031, Galactar_dehydrat, 1 hit
    InterProiView protein in InterPro
    IPR007392, Gal/Altron_deHydtase_C
    IPR017654, GarD-like
    IPR032893, GarD_Enterobacteriaceae
    IPR013974, SAF
    PfamiView protein in Pfam
    PF04295, GD_AH_C, 1 hit
    PF08666, SAF, 1 hit
    SMARTiView protein in SMART
    SM00858, SAF, 1 hit
    TIGRFAMsiTIGR03248, galactar-dH20, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGARD_ECOLI
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P39829
    Secondary accession number(s): Q2M981
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: November 1, 1995
    Last modified: December 2, 2020
    This is version 135 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, 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
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again