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UniProtKB - P0A955 (ALKH_ECOLI)

Entry version 118 (11 Dec 2019)
Sequence version 1 (19 Jul 2005)
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Protein

KHG/KDPG aldolase

Gene

eda

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

Annotation score:5 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

Involved in the degradation of glucose via the Entner-Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-Keto-3-deoxy-6-phosphogluconate (KDPG) to pyruvate and D-glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophilic aldehydes with si-facial selectivity. It accepts some nucleophiles other than pyruvate, including 2-oxobutanoate, phenylpyruvate, and fluorobutanoate. It has a preference for the S-configuration at C2 of the electrophile.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 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 80 sec(-1) for KDPG, 0.012 sec(-1) for pyruvate and 0.0004 sec(-1) for 2-oxobutyrate.
  1. KM=0.1 mM for KDPG2 Publications
  2. KM=9 mM for 2-oxobutyrate2 Publications
  3. KM=10 mM for pyruvate2 Publications

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: 2-dehydro-3-deoxy-D-gluconate degradation

    This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. 2-dehydro-3-deoxygluconokinase (kdgK)
    2. KHG/KDPG aldolase (eda)
    This subpathway is part of the pathway 2-dehydro-3-deoxy-D-gluconate 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-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate, the pathway 2-dehydro-3-deoxy-D-gluconate degradation and in Carbohydrate acid metabolism.

    Pathwayi: glyoxylate and dicarboxylate metabolism

    This protein is involved in the pathway glyoxylate and dicarboxylate metabolism, which is part of Carbohydrate metabolism.
    View all proteins of this organism that are known to be involved in the pathway glyoxylate and dicarboxylate metabolism and in Carbohydrate metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei45Proton acceptor1
    Active sitei491
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei49Substrate1 Publication1
    Binding sitei73Substrate1 Publication1
    Active sitei133Schiff-base intermediate with substrate1
    Binding sitei133Substrate (covalent)1 Publication1
    Binding sitei161Substrate1 Publication1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei161Plays a major role in determining the stereoselectivity1
    Binding sitei163Substrate; via amide nitrogen1 Publication1
    Binding sitei184Substrate1 Publication1

    <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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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, Multifunctional enzyme
    LigandSchiff base

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER
    ECOL316407:JW1839-MONOMER
    MetaCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		4.1.2.14 2026
    4.1.3.42 2026

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

    More...    UniPathwayi    		UPA00227
    UPA00856;UER00829

    <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_and_taxonomy_section">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:
    KHG/KDPG aldolase
    Including the following 2 domains:
    4-hydroxy-2-oxoglutarate aldolase (EC:4.1.3.16)
    Alternative name(s):
    2-keto-4-hydroxyglutarate aldolase
    Short name:
    KHG-aldolase
    2-dehydro-3-deoxy-phosphogluconate aldolase (EC:4.1.2.14)
    Alternative name(s):
    2-keto-3-deoxy-6-phosphogluconate aldolase
    Short name:
    KDPG-aldolase
    Phospho-2-dehydro-3-deoxygluconate aldolase
    Phospho-2-keto-3-deoxygluconate aldolase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:eda
    Synonyms:hga, kdgA
    Ordered Locus Names:b1850, JW1839
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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 provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation on QuickGO ...

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Cells lacking this gene lose KHG aldolase activity.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi45E → N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity. 2 Publications1
    Mutagenesisi133K → Q: Absence of aldolase activity. Shows a markedly altered substrate specificity relative to the wild-type, with an enhanced activity against pyridine carboxaldehyde, benzaldehyde, and alpha-ketobutyrate; when associated with k-161. 1 Publication1
    Mutagenesisi161T → K: Shows activity significantly greater than wild-type. Shows a markedly altered substrate specificity relative to the wild-type, with an enhanced activity against pyridine carboxaldehyde, benzaldehyde, and alpha-ketobutyrate; when associated with Q-133. 2 Publications1
    Mutagenesisi161T → V: Little stereoselectivity, accepting KDPG and KDPGal as substrate with roughly equal efficacy. It strongly diminishes the activity against KDPG and slightly increases activity against KDPGal. 2 Publications1
    Mutagenesisi168N → S: Shows activity significantly greater than wild-type. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...    DrugBanki    		DB04272 Citric acid

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002010371 – 213KHG/KDPG aldolaseAdd BLAST213

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		P0A955

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P0A955

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

    More...    PaxDbi    		P0A955

    PRoteomics IDEntifications database

    More...    PRIDEi    		P0A955

    2D gel databases

    Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

    More...    SWISS-2DPAGEi    		P0A955

    <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

    Constitutive, three-fold induction occurs for growth on gluconate and two-fold for growth on hexuronic acids.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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotrimer.

    3 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-558114,EBI-558114

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4259153, 29 interactors
    850724, 2 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-36196N

    Protein interaction database and analysis system

    More...    IntActi    		P0A955, 10 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b1850

    <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

    1213
    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    		P0A955

    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    		P0A955

    <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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni8 – 9Substrate binding2

    <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 KHG/KDPG aldolase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4108UHU Bacteria
    COG0800 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000233114

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0A955

    KEGG Orthology (KO)

    More...    KOi    		K01625

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P0A955

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd00452 KDPG_aldolase, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.20.20.70, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR000887 Aldlse_KDPG_KHG
    IPR013785 Aldolase_TIM
    IPR031337 KDPG/KHG_AS_1
    IPR031338 KDPG/KHG_AS_2

    The PANTHER Classification System

    More...    PANTHERi    		PTHR30246 PTHR30246, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01081 Aldolase, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR01182 eda, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00159 ALDOLASE_KDPG_KHG_1, 1 hit
    PS00160 ALDOLASE_KDPG_KHG_2, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    P0A955-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKNWKTSAES ILTTGPVVPV IVVKKLEHAV PMAKALVAGG VRVLEVTLRT 
            60         70         80         90        100
    ECAVDAIRAI AKEVPEAIVG AGTVLNPQQL AEVTEAGAQF AISPGLTEPL 
           110        120        130        140        150
    LKAATEGTIP LIPGISTVSE LMLGMDYGLK EFKFFPAEAN GGVKALQAIA 
           160        170        180        190        200
    GPFSQVRFCP TGGISPANYR DYLALKSVLC IGGSWLVPAD ALEAGDYDRI 
           210 
    TKLAREAVEG AKL
    Length:213
    Mass (Da):22,284
    Last modified:July 19, 2005 - v1
    <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:iCC8D51B50480D0B7
    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
    		X68871 Genomic DNA Translation: CAA48732.1
    M87458 Genomic DNA Translation: AAA23723.1
    L20897 Genomic DNA Translation: AAA23862.1
    X63694 Genomic DNA Translation: CAA45222.1
    U00096 Genomic DNA Translation: AAC74920.1
    AP009048 Genomic DNA Translation: BAA15658.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		B42986 ADECOG

    NCBI Reference Sequences

    More...    RefSeqi    		NP_416364.1, NC_000913.3
    WP_000800512.1, NZ_STEB01000009.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC74920; AAC74920; b1850
    BAA15658; BAA15658; BAA15658

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		946367

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW1839
    eco:b1850

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.399

    <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
    		X68871 Genomic DNA Translation: CAA48732.1
    M87458 Genomic DNA Translation: AAA23723.1
    L20897 Genomic DNA Translation: AAA23862.1
    X63694 Genomic DNA Translation: CAA45222.1
    U00096 Genomic DNA Translation: AAC74920.1
    AP009048 Genomic DNA Translation: BAA15658.1
    PIRiB42986 ADECOG
    RefSeqiNP_416364.1, NC_000913.3
    WP_000800512.1, NZ_STEB01000009.1

    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
    1EUAX-ray1.95A/B/C1-213[»]
    1EUNX-ray2.00A/B/C1-213[»]
    1FQ0X-ray2.10A/B/C1-213[»]
    1FWRX-ray2.70A/B/C1-213[»]
    1WAUX-ray2.80A1-213[»]
    1WBHX-ray1.55A/B/C1-213[»]
    2C0AX-ray1.55A/B/C1-213[»]
    SMRiP0A955
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4259153, 29 interactors
    850724, 2 interactors
    DIPiDIP-36196N
    IntActiP0A955, 10 interactors
    STRINGi511145.b1850

    Chemistry databases

    DrugBankiDB04272 Citric acid

    2D gel databases

    SWISS-2DPAGEiP0A955

    Proteomic databases

    EPDiP0A955
    jPOSTiP0A955
    PaxDbiP0A955
    PRIDEiP0A955

    Genome annotation databases

    EnsemblBacteriaiAAC74920; AAC74920; b1850
    BAA15658; BAA15658; BAA15658
    GeneIDi946367
    KEGGiecj:JW1839
    eco:b1850
    PATRICifig|1411691.4.peg.399

    Organism-specific databases

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

    More...    EchoBASEi    		EB0252

    Phylogenomic databases

    eggNOGiENOG4108UHU Bacteria
    COG0800 LUCA
    HOGENOMiHOG000233114
    InParanoidiP0A955
    KOiK01625
    PhylomeDBiP0A955

    Enzyme and pathway databases

    UniPathwayiUPA00227
    UPA00856;UER00829
    BioCyciEcoCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER
    ECOL316407:JW1839-MONOMER
    MetaCyc:KDPGALDOL-4OH2OXOGLUTARALDOL-MONOMER
    BRENDAi4.1.2.14 2026
    4.1.3.42 2026

    Miscellaneous databases

    EvolutionaryTraceiP0A955

    Protein Ontology

    More...    PROi    		PR:P0A955

    Family and domain databases

    CDDicd00452 KDPG_aldolase, 1 hit
    Gene3Di3.20.20.70, 1 hit
    InterProiView protein in InterPro
    IPR000887 Aldlse_KDPG_KHG
    IPR013785 Aldolase_TIM
    IPR031337 KDPG/KHG_AS_1
    IPR031338 KDPG/KHG_AS_2
    PANTHERiPTHR30246 PTHR30246, 1 hit
    PfamiView protein in Pfam
    PF01081 Aldolase, 1 hit
    TIGRFAMsiTIGR01182 eda, 1 hit
    PROSITEiView protein in PROSITE
    PS00159 ALDOLASE_KDPG_KHG_1, 1 hit
    PS00160 ALDOLASE_KDPG_KHG_2, 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 nameiALKH_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: P0A955
    Secondary accession number(s): P10177
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: December 11, 2019
    This is version 118 of the entry and version 1 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, Direct protein sequencing, 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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