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UniProtKB - P51015 (HOA4_PARXL)

Entry version 112 (07 Apr 2021)
Sequence version 2 (19 Sep 2006)
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Protein

4-hydroxy-2-oxovalerate aldolase 4

Gene

bphI

Organism
Paraburkholderia xenovorans (strain LB400)
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 retro-aldol cleavage of both 4-hydroxy-2-oxopentanoate (HOPA) and 4-hydroxy-2-oxohexanoate (HOHA) to pyruvate and acetaldehyde or propanaldehyde, respectively. The aldehydes produced by this reaction are directly channeled from BphI to the dehydrogenase BphJ, ensuring that these toxic aldehydes are sequestered from cellular components. Is involved in the meta-cleavage pathway for the degradation of polychlorinated biphenyls (PCBs). Appears to be stereospecific since it can cleave (4S)-4-hydroxy-2-oxopentanoate but not the (4R) isomer. Also exhibits a secondary oxaloacetate decarboxylase activity. Finally, is also able to catalyze the reverse reaction, albeit much less efficiently, i.e. the condensation of aldehyde acceptors of two to three carbons in length with pyruvate. This aldol addition reaction is stereospecific; the condensation of acetaldehyde and pyruvate with BphI produces only the (4S)-4-hydroxy-2-oxopentanoate isomer. Aldehyde channeling in the BphI-BphJ complex can occur in reverse, from the dehydrogenase to the aldolase active sites, and the BphJ reductive deacylation reaction increases 4-fold when BphI is catalyzing the aldol addition reaction. Therefore, the BphI-BphJ enzyme complex exhibits unique bidirectionality in substrate channeling and allosteric activation.2 Publications

Miscellaneous

The aldol addition reaction proceeds via a compulsory order mechanism, with pyruvate binding first.

<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

Mn2+1 Publication, Cd2+1 Publication, Co2+1 PublicationNote: Divalent metal cation. Has the highest activity with Mn2+ as cofactor. Can also use Cd2+ at low concentrations (0.01-0.1 mM) or Co2+, although with less efficiency. Mg2+ and Ni2+ are very poor metal cofactors.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Competitively inhibited by oxalate. Also inhibited by high concentrations of Cd2+ (1 mM) in vitro. Appears to be allosterically activated by aldehyde turnover occurring in BphJ, partly via NADH.

<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 is similar when using 4-hydroxy-2-oxopentanoate or 4-hydroxy-2-oxohexanoate as substrate, but is 10-fold lower with 4-hydroxy-2-oxoheptanoate. It is also 25-fold higher when NADH is present than the value obtained without nucleotides. Moreover, the catalytic efficiency is similar when using acetaldehyde or propanaldehyde as substrate in the aldol addition reaction.
  1. KM=89 µM for (4S)-4-hydroxy-2-oxopentanoate (in the presence of NADH at pH 8 and 25 degrees Celsius)3 Publications
  2. KM=0.22 mM for racemic 4-hydroxy-2-oxopentanoate (in the presence of NADH at pH 8 and 25 degrees Celsius)3 Publications
  3. KM=1.12 mM for racemic 4-hydroxy-2-oxopentanoate (in the absence of NADH at pH 8 and 25 degrees Celsius)3 Publications
  4. KM=0.18 mM for racemic 4-hydroxy-2-oxohexanoate (in the presence of NADH at pH 8 and 25 degrees Celsius)3 Publications
  5. KM=0.35 mM for racemic 4-hydroxy-2-oxoheptanoate (in the presence of NADH at pH 8 and 25 degrees Celsius)3 Publications
  6. KM=64.28 mM for acetaldehyde (in the absence of NADH at pH 8 and 25 degrees Celsius)3 Publications
  7. KM=135.9 mM for propanaldehyde (in the absence of NADH at pH 8 and 25 degrees Celsius)3 Publications
  8. KM=13.0 mM for pyruvate (at pH 8 and 25 degrees Celsius)3 Publications

    pH dependencei

    Activity increases from pH 6.5 to 9.1 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: polychlorinated biphenyl degradation

    This protein is involved in the pathway polychlorinated biphenyl degradation, which is part of Xenobiotic degradation.
    View all proteins of this organism that are known to be involved in the pathway polychlorinated biphenyl degradation and in Xenobiotic degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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>Sitei16Transition state stabilizerUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi17ManganeseUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei20Proton acceptorUniRule annotation1
    Sitei87Important for aldehyde specificity, and governs stereochemical control1
    Sitei89Important for aldehyde specificity; governs substrate alkyl chain length1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei170SubstrateUniRule annotation1
    Metal bindingi199Manganese; via tele nitrogenUniRule annotation1
    Binding sitei199SubstrateUniRule annotation1
    Metal bindingi201Manganese; via tele nitrogenUniRule annotation1
    Binding sitei290SubstrateUniRule annotation1
    Sitei290Governs stereochemical control1

    <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 functionAllosteric enzyme, Lyase
    Biological processAromatic hydrocarbons catabolism
    LigandCadmium, Cobalt, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		BXEN266265:BXE_RS42265-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		4.1.3.39, 9987
    4.1.3.43, 7691

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P51015

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

    More...    UniPathwayi    		UPA01002

    <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:
    4-hydroxy-2-oxovalerate aldolase 4UniRule annotation (EC:4.1.3.39UniRule annotation1 Publication)
    Short name:
    HOA 4UniRule annotation
    Alternative name(s):
    4-hydroxy-2-keto-pentanoic acid aldolase 4UniRule annotation
    4-hydroxy-2-oxohexanoate aldolase (EC:4.1.3.431 Publication)
    4-hydroxy-2-oxopentanoate aldolase 4UniRule 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:bphI
    Ordered Locus Names:Bxeno_C1121
    ORF Names:Bxe_C1187
    <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>OrganismiParaburkholderia xenovorans (strain LB400)
    <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 identifieri266265 [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 lineageiBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Paraburkholderia ›
    <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
    • UP000001817 <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 3

    <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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi16R → A: Loss of aldol cleavage activity. 1 Publication1
    Mutagenesisi16R → K: 4000-fold decrease in the catalytic efficiency of the aldol cleavage reaction. 1 Publication1
    Mutagenesisi20H → A or S: 100-fold decrease in the catalytic efficiency of the aldol cleavage reaction. Dramatic reduction in acetaldehyde and propanaldehyde channeling efficiency by more than 70%. 2 Publications1
    Mutagenesisi87L → A: 32-fold reduction in the catalytic efficiency with acetaldehyde as substrate of the aldol addition reaction, but no change in the catalytic efficiency using propanaldehyde; thus, exhibits a 40-fold preference for propanaldehyde over acetaldehyde. 2 Publications1
    Mutagenesisi87L → N or W: Loss of aldolase activity (with either enantiomer of HOPA), but retains some decarboxylase activity for the smaller oxaloacetate substrate. In the retro-aldol cleavage reaction, is inactive toward 4(S)-HOPA but is active toward 4(R)-HOPA, albeit with a great reduction in catalytic efficiency, and in the aldol addition reaction, produces also exclusively the 4(R)-enantiomer; when associated with F-290. 2 Publications1
    Mutagenesisi89L → A: As the wild-type enzyme, exhibits similar catalytic efficiency with acetaldehyde or propanaldehyde as substrate in the aldol addition reaction but displays higher catalytic efficiency with longer aldehydes (50-fold increase using pentaldehyde). Shows a reduction in aldehyde channeling efficiency by 30%. 2 Publications1
    Mutagenesisi290Y → F: Loss of stereochemical control as the mutant is able to catalyze the aldol cleavage of substrates with both R and S configurations at C4 with similar kinetic parameters. 3.5-fold decrease in the catalytic efficiency of the aldol cleavage reaction. Reduction in aldehyde channeling efficiency by more than 30%. In the retro-aldol cleavage reaction, is inactive toward 4(S)-HOPA but is active toward 4(R)-HOPA, albeit with a great reduction in catalytic efficiency, and in the aldol addition reaction, produces also exclusively the 4(R)-enantiomer; when associated with N-87 or W-87. 3 Publications1
    Mutagenesisi290Y → S: Loss of stereochemical control as the mutant is able to catalyze the aldol cleavage of substrates with both R and S configurations at C4 with similar kinetic parameters. 3.5-fold decrease in the catalytic efficiency of the aldol cleavage reaction. 3 Publications1
    Mutagenesisi322G → A: Displays a reduction in aldehyde channeling efficiency of about 20%. 1 Publication1
    Mutagenesisi322G → F or L: Unable to channel either acetaldehyde or propanaldehyde. 1 Publication1
    Mutagenesisi323G → A: Able to channel butyraldehyde (with less efficiency than wild-type) but not its isomer isobutyraldehyde. 1 Publication1
    Mutagenesisi323G → F: Unable to channel either acetaldehyde or propanaldehyde. 1 Publication1
    Mutagenesisi323G → L: Able to channel acetaldehyde but not the larger propanaldehyde. 1 Publication1

    <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_00000649781 – 3464-hydroxy-2-oxovalerate aldolase 4Add BLAST346

    <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

    Heterotetramer composed of two BphI (aldolase) and two BphJ (dehydrogenase).

    1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...    STRINGi    		266265.Bxe_C1187

    <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

    3D structure databases

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

    More...    SMRi    		P51015

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini8 – 260Pyruvate carboxyltransferaseUniRule annotationAdd BLAST253

    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>Regioni16 – 17Substrate bindingUniRule annotation2

    <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 4-hydroxy-2-oxovalerate aldolase family.UniRule annotationCurated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG0119, Bacteria

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		YVGGQED

    Database of Orthologous Groups

    More...    OrthoDBi    		840579at2

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd07943, DRE_TIM_HOA, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.20.20.70, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_01656, HOA, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR017629, 4OH_2_O-val_aldolase
    IPR013785, Aldolase_TIM
    IPR012425, DmpG_comm
    IPR035685, DRE_TIM_HOA
    IPR000891, PYR_CT

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF07836, DmpG_comm, 1 hit
    PF00682, HMGL-like, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR03217, 4OH_2_O_val_ald, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS50991, PYR_CT, 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.

    P51015-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKLEGKKVTV HDMTLRDGMH PKRHQMTLEQ MKSIACGLDA AGIPLIEVTH 
            60         70         80         90        100
    GDGLGGSSVN YGFPAHSDEE YLGAVIPLMK QAKVSALLLP GIGTVEHLKM 
           110        120        130        140        150
    AKDLGVNTIR VATHCTEADV SEQHITQSRK LGLDTVGFLM MAHMASPEKL 
           160        170        180        190        200
    VSQALLMQGY GANCIYVTDS AGYMLPDDVK ARLSAVRAAL KPETELGFHG 
           210        220        230        240        250
    HHNLAMGVAN SIAAIEAGAT RIDAAAAGLG AGAGNTPMEV FIAVCARMGI 
           260        270        280        290        300
    ETGVDVFKIQ DVAEDLVVPI MDHVIRIDRD SLTLGYAGVY SSFLLFAKRA 
           310        320        330        340 
    SAKYGVPARD ILVELGRRGM VGGQEDMIED TAMTMARERG LTLTAA
    Length:346
    Mass (Da):36,798
    Last modified:September 19, 2006 - 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:iBD4A951D513C97CE
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti263A → S in CAA54036 (PubMed:8026764).Curated1
    Sequence conflicti302A → E in CAA54036 (PubMed:8026764).Curated1

    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
    		X76500 Genomic DNA Translation: CAA54036.1
    CP000272 Genomic DNA Translation: ABE37049.1

    NCBI Reference Sequences

    More...    RefSeqi    		WP_003450974.1, NZ_CP008761.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		ABE37049; ABE37049; Bxe_C1187

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		bxb:DR64_8618
    bxe:Bxe_C1187

    <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
    		X76500 Genomic DNA Translation: CAA54036.1
    CP000272 Genomic DNA Translation: ABE37049.1
    RefSeqiWP_003450974.1, NZ_CP008761.1

    3D structure databases

    SMRiP51015
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi266265.Bxe_C1187

    Genome annotation databases

    EnsemblBacteriaiABE37049; ABE37049; Bxe_C1187
    KEGGibxb:DR64_8618
    bxe:Bxe_C1187

    Phylogenomic databases

    eggNOGiCOG0119, Bacteria
    OMAiYVGGQED
    OrthoDBi840579at2

    Enzyme and pathway databases

    UniPathwayiUPA01002
    BioCyciBXEN266265:BXE_RS42265-MONOMER
    BRENDAi4.1.3.39, 9987
    4.1.3.43, 7691
    SABIO-RKiP51015

    Family and domain databases

    CDDicd07943, DRE_TIM_HOA, 1 hit
    Gene3Di3.20.20.70, 1 hit
    HAMAPiMF_01656, HOA, 1 hit
    InterProiView protein in InterPro
    IPR017629, 4OH_2_O-val_aldolase
    IPR013785, Aldolase_TIM
    IPR012425, DmpG_comm
    IPR035685, DRE_TIM_HOA
    IPR000891, PYR_CT
    PfamiView protein in Pfam
    PF07836, DmpG_comm, 1 hit
    PF00682, HMGL-like, 1 hit
    TIGRFAMsiTIGR03217, 4OH_2_O_val_ald, 1 hit
    PROSITEiView protein in PROSITE
    PS50991, PYR_CT, 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 nameiHOA4_PARXL
    <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: P51015
    Secondary accession number(s): Q13FU0
    <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: October 1, 1996
    Last sequence update: September 19, 2006
    Last modified: April 7, 2021
    This is version 112 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

    Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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