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UniProtKB - P0AB71 (ALF_ECOLI)

Protein

Fructose-bisphosphate aldolase class 2

Gene

fbaA

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

Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.1 Publication

<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 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

Zn2+Note: Binds 2 Zn2+ ions per subunit. One is catalytic and the other provides a structural contribution.

<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

The catalytic efficiency measured with fructose-1,6-bisphosphate as substrate is 1440-fold higher than that with tagatose-1,6-bisphosphate.
  1. KM=0.17 mM for fructose-1,6-bisphosphate1 Publication
  2. KM=0.35 mM for tagatose-1,6-bisphosphate1 Publication

    <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: glycolysis

    This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. Glucose-6-phosphate isomerase (pgi)
    3. ATP-dependent 6-phosphofructokinase isozyme 2 (pfkB), ATP-dependent 6-phosphofructokinase isozyme 1 (pfkA)
    4. Fructose-bisphosphate aldolase class 2 (fbaA)
    This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sitei62Glyceraldehyde 3-phosphateCurated1
    <p>This subsection of the ‘Function’ 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 sitei110Proton donor1 Publication1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi111Zinc 1; catalytic3 Publications1
    Metal bindingi145Zinc 23 Publications1
    Metal bindingi175Zinc 23 Publications1
    Metal bindingi227Zinc 1; catalytic3 Publications1
    Binding sitei228Dihydroxyacetone phosphate; via amide nitrogen1
    Metal bindingi265Zinc 1; catalytic3 Publications1

    <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

    • fructose-bisphosphate aldolase activity Source: EcoCyc
    • identical protein binding Source: IntAct
    • zinc ion binding Source: EcoliWiki
    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    • gluconeogenesis Source: GO_Central
    • glycolytic process Source: EcoCyc
    View the 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
    Biological processGlycolysis
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:FRUCTBISALD-CLASSII-MONOMER
    MetaCyc:FRUCTBISALD-CLASSII-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		4.1.2.13 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P0AB71

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

    More...    UniPathwayi
    UPA00109;UER00183

    <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:
    Fructose-bisphosphate aldolase class 2 (EC:4.1.2.13)
    Short name:
    FBP aldolase
    Short name:
    FBPA
    Alternative name(s):
    Fructose-1,6-bisphosphate aldolase
    Fructose-bisphosphate aldolase class II
    <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:fbaA
    Synonyms:fba, fda
    Ordered Locus Names:b2925, JW2892
    <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

    Organism-specific databases

    Escherichia coli strain K12 genome database

    More...    EcoGenei    		EG10282 fbaA

    <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

    View the complete GO annotation on QuickGO ...

    <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

    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>Mutagenesisi36N → A: 1.5% of wild-type activity. 5-fold decrease in FBP affinity. 1 Publication1
    Mutagenesisi60Q → A: 81% of wild-type activity. 1.3-fold decrease in FBP affinity. 1 Publication1
    Mutagenesisi62S → A: 8% of wild-type activity. 16-fold decrease in FBP affinity. 1 Publication1
    Mutagenesisi62S → T: 60% of wild-type activity. 2.5-fold decrease in FBP affinity. 1 Publication1
    Mutagenesisi108H → A: Loss of activity. 1 Publication1
    Mutagenesisi111H → A: Loss of activity. 1 Publication1
    Mutagenesisi112C → A: Partial loss of activity. 1 Publication1
    Mutagenesisi326K → A: 6% of wild-type activity. 2.2-fold decrease in FBP affinity. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL4912

    Drug and drug target database

    More...    DrugBanki    		DB03026 Phosphoglycolohydroxamic 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved3 Publications
    <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_00001787132 – 359Fructose-bisphosphate aldolase class 2Add BLAST358

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei9N6-acetyllysine; alternate1 Publication1
    Modified residuei9N6-malonyllysine; alternate1 Publication1
    Modified residuei9N6-succinyllysine; alternate1 Publication1
    Modified residuei72N6-succinyllysine1 Publication1
    Modified residuei115N6-succinyllysine1 Publication1
    Modified residuei231N6-succinyllysine1 Publication1
    Modified residuei251N6-succinyllysine1 Publication1
    Modified residuei319N6-succinyllysine1 Publication1
    Modified residuei326N6-succinyllysine1 Publication1
    Modified residuei348N6-succinyllysine1 Publication1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		P0AB71

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

    More...    PaxDbi    		P0AB71

    PRoteomics IDEntifications database

    More...    PRIDEi    		P0AB71

    2D gel databases

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

    More...    SWISS-2DPAGEi    		P0AB71

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P0AB71

    <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

    Homodimer.4 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

    GO - Molecular functioni

    View the complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		4262069, 20 interactors
    851736, 1 interactor

    Database of interacting proteins

    More...    DIPi    		DIP-31872N

    Protein interaction database and analysis system

    More...    IntActi    		P0AB71, 7 interactors

    STRING: functional protein association networks

    More...    STRINGi    		316385.ECDH10B_3100

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P0AB71

    <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

    1359
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		P0AB71

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

    More...    SMRi    		P0AB71

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P0AB71

    <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>Regioni266 – 268Dihydroxyacetone phosphate binding3
    Regioni287 – 290Dihydroxyacetone phosphate binding4

    <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 class II fructose-bisphosphate aldolase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4105D2N Bacteria
    COG0191 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000227794

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0AB71

    KEGG Orthology (KO)

    More...    KOi    		K01624

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P0AB71

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd00946 FBP_aldolase_IIA, 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
    IPR013785 Aldolase_TIM
    IPR000771 FBA_II
    IPR006411 Fruct_bisP_bact

    The PANTHER Classification System

    More...    PANTHERi    		PTHR30559 PTHR30559, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01116 F_bP_aldolase, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF001359 F_bP_aldolase_II, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR00167 cbbA, 1 hit
    TIGR01520 FruBisAldo_II_A, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00602 ALDOLASE_CLASS_II_1, 1 hit
    PS00806 ALDOLASE_CLASS_II_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>.<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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P0AB71-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSKIFDFVKP GVITGDDVQK VFQVAKENNF ALPAVNCVGT DSINAVLETA 
            60         70         80         90        100
    AKVKAPVIVQ FSNGGASFIA GKGVKSDVPQ GAAILGAISG AHHVHQMAEH 
           110        120        130        140        150
    YGVPVILHTD HCAKKLLPWI DGLLDAGEKH FAATGKPLFS SHMIDLSEES 
           160        170        180        190        200
    LQENIEICSK YLERMSKIGM TLEIELGCTG GEEDGVDNSH MDASALYTQP 
           210        220        230        240        250
    EDVDYAYTEL SKISPRFTIA ASFGNVHGVY KPGNVVLTPT ILRDSQEYVS 
           260        270        280        290        300
    KKHNLPHNSL NFVFHGGSGS TAQEIKDSVS YGVVKMNIDT DTQWATWEGV 
           310        320        330        340        350
    LNYYKANEAY LQGQLGNPKG EDQPNKKYYD PRVWLRAGQT SMIARLEKAF 

    QELNAIDVL
    Length:359
    Mass (Da):39,147
    Last modified:January 23, 2007 - 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:i7A076D9EA62FBEC4
    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
    		X14436 Genomic DNA Translation: CAA32605.1
    U28377 Genomic DNA Translation: AAA69092.1
    U00096 Genomic DNA Translation: AAC75962.1
    AP009048 Genomic DNA Translation: BAE76989.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		S02177 ADEC2A

    NCBI Reference Sequences

    More...    RefSeqi    		NP_417400.1, NC_000913.3
    WP_000034372.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC75962; AAC75962; b2925
    BAE76989; BAE76989; BAE76989

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		947415

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW2892
    eco:b2925

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.3807

    <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
    		X14436 Genomic DNA Translation: CAA32605.1
    U28377 Genomic DNA Translation: AAA69092.1
    U00096 Genomic DNA Translation: AAC75962.1
    AP009048 Genomic DNA Translation: BAE76989.1
    PIRiS02177 ADEC2A
    RefSeqiNP_417400.1, NC_000913.3
    WP_000034372.1, NZ_LN832404.1

    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
    1B57X-ray2.00A/B2-359[»]
    1DOSX-ray1.67A/B2-359[»]
    1GYNX-ray2.00A2-359[»]
    1ZENX-ray2.50A2-359[»]
    5GK3X-ray1.80A/B1-359[»]
    5GK4X-ray2.00A/B1-359[»]
    5GK5X-ray1.90A/B/C/D/E/F/G/H1-359[»]
    5GK6X-ray1.80A/B1-359[»]
    5GK7X-ray1.80A/B1-359[»]
    5GK8X-ray2.00A/B1-359[»]
    5VJDX-ray1.70A/B2-359[»]
    5VJEX-ray1.65A/B2-359[»]
    ProteinModelPortaliP0AB71
    SMRiP0AB71
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262069, 20 interactors
    851736, 1 interactor
    DIPiDIP-31872N
    IntActiP0AB71, 7 interactors
    STRINGi316385.ECDH10B_3100

    Chemistry databases

    BindingDBiP0AB71
    ChEMBLiCHEMBL4912
    DrugBankiDB03026 Phosphoglycolohydroxamic Acid

    PTM databases

    iPTMnetiP0AB71

    2D gel databases

    SWISS-2DPAGEiP0AB71

    Proteomic databases

    EPDiP0AB71
    PaxDbiP0AB71
    PRIDEiP0AB71

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75962; AAC75962; b2925
    BAE76989; BAE76989; BAE76989
    GeneIDi947415
    KEGGiecj:JW2892
    eco:b2925
    PATRICifig|1411691.4.peg.3807

    Organism-specific databases

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

    More...    EchoBASEi    		EB0278
    EcoGeneiEG10282 fbaA

    Phylogenomic databases

    eggNOGiENOG4105D2N Bacteria
    COG0191 LUCA
    HOGENOMiHOG000227794
    InParanoidiP0AB71
    KOiK01624
    PhylomeDBiP0AB71

    Enzyme and pathway databases

    UniPathwayi
    UPA00109;UER00183

    BioCyciEcoCyc:FRUCTBISALD-CLASSII-MONOMER
    MetaCyc:FRUCTBISALD-CLASSII-MONOMER
    BRENDAi4.1.2.13 2026
    SABIO-RKiP0AB71

    Miscellaneous databases

    EvolutionaryTraceiP0AB71

    Protein Ontology

    More...    PROi    		PR:P0AB71

    Family and domain databases

    CDDicd00946 FBP_aldolase_IIA, 1 hit
    Gene3Di3.20.20.70, 1 hit
    InterProiView protein in InterPro
    IPR013785 Aldolase_TIM
    IPR000771 FBA_II
    IPR006411 Fruct_bisP_bact
    PANTHERiPTHR30559 PTHR30559, 1 hit
    PfamiView protein in Pfam
    PF01116 F_bP_aldolase, 1 hit
    PIRSFiPIRSF001359 F_bP_aldolase_II, 1 hit
    TIGRFAMsiTIGR00167 cbbA, 1 hit
    TIGR01520 FruBisAldo_II_A, 1 hit
    PROSITEiView protein in PROSITE
    PS00602 ALDOLASE_CLASS_II_1, 1 hit
    PS00806 ALDOLASE_CLASS_II_2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		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 nameiALF_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: P0AB71
    Secondary accession number(s): P11604, Q2M9R7
    <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: November 8, 2005
    Last sequence update: January 23, 2007
    Last modified: December 5, 2018
    This is version 114 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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