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Entry version 121 (07 Apr 2021)
Sequence version 1 (01 Feb 1997)
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Protein

Aldo/keto reductase slr0942

Gene

slr0942

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
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

Aldo/keto reductase with broad substrate spectrum. Catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols. Highest enzymatic efficiency is observed with 4-oxonon-2-enal (4-ONE) and 4-hydroxynon-2-enal (4-HNE), that are lipid peroxidation products, and 9,10-phenanthrenequinone (9,10-PQ), a photoproduct of phenanthrene that is one of the most prevalent polycyclic aromatic hydrocarbons in the environment. Is also active on sugar-derived reactive carbonyls such as methylglyoxal (MG), glyoxal and 3-deoxyglucosone (3-DG), and on other lipid-derived carbonyls such as acrolein. May be involved in the detoxification of the toxic lipid peroxidation products 4-ONE and 4-HNE besides many other exo- and endogenic reactive carbonyl compounds (RCs) that may lead to photoinhibition or other cell damages.2 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 <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

Curcumin non-competitively inhibits the enzyme with respect to furfural. To a lesser extent, enzyme activity is also inhibited by indomethacin, coumarate, coumarin, and alrestatin.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 351 min(-1) with methylglyoxal as substrate. kcat is 1049 min(-1) with glyoxal as substrate. kcat is 226 min(-1) with 3-deoxyglucosone as substrate. kcat is 1078 min(-1) with acrolein as substrate. kcat is 1.75 sec(-1) with hexanal as substrate. kcat is 1.17 sec(-1) with 4-pyridinecarboxaldehyde as substrate. kcat is 0.3 sec(-1) with 4-nitrobenzaldehyde as substrate. kcat is 2.23 sec(-1) with 9,10-phenanthrenequinone as substrate. kcat is 4.06 sec(-1) with 2,3-pentanedione as substrate. kcat is 2.63 sec(-1) with 4-oxonon-2-enal as substrate. kcat is 1.57 sec(-1) with 4-hydroxynon-2-enal as substrate. kcat is 8.52 sec(-1) with furfural as substrate.2 Publications
  1. KM=96 µM for methylglyoxal1 Publication
  2. KM=10.8 mM for glyoxal1 Publication
  3. KM=520 µM for 3-deoxyglucosone1 Publication
  4. KM=1.7 mM for acrolein1 Publication
  5. KM=94 µM for hexanal1 Publication
  6. KM=94 µM for 4-pyridinecarboxaldehyde1 Publication
  7. KM=46 µM for 4-nitrobenzaldehyde1 Publication
  8. KM=5 µM for 9,10-phenanthrenequinone1 Publication
  9. KM=4.7 µM for 4-oxonon-2-enal1 Publication
  10. KM=59.5 µM for 4-hydroxynon-2-enal1 Publication
  11. KM=890 µM for furfural1 Publication
  12. KM=8.5 µM for NADPH1 Publication

    pH dependencei

    Optimum pH is 5 for the reduction of methylglyoxal.1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius for the reduction of methylglyoxal.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei57Proton donorBy similarity1
    <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>Sitei86Lowers pKa of active site TyrBy similarity1
    <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 sitei119SubstrateBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi18 – 27NADPSequence analysis10
    Nucleotide bindingi216 – 280NADPBy similarityAdd BLAST65

    <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

    <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 functionOxidoreductase
    LigandNADP

    <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:
    Aldo/keto reductase slr09422 Publications (EC:1.1.1.1842 Publications)
    Short name:
    AKR2 Publications
    Alternative name(s):
    AKR3G11 Publication
    <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
    Ordered Locus Names:slr0942Imported
    <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>OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
    <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 identifieri1111708 [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 lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystisunclassified Synechocystis
    <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
    • UP000001425 <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

    <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

    <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_00004317281 – 327Aldo/keto reductase slr0942Add BLAST327

    Proteomic databases

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

    More...
    PaxDbi
    P74308

    <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

    Monomer.

    1 Publication

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    P74308, 10 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    1148.1653489

    <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
    P74308

    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

    <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 aldo/keto reductase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0656, Bacteria

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P74308

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    WATYNTR

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P74308

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd19123, AKR_AKR3G1, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.20.20.100, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR020471, AKR
    IPR044496, AKR3G
    IPR018170, Aldo/ket_reductase_CS
    IPR023210, NADP_OxRdtase_dom
    IPR036812, NADP_OxRdtase_dom_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00248, Aldo_ket_red, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000097, AKR, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00069, ALDKETRDTASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51430, SSF51430, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00798, ALDOKETO_REDUCTASE_1, 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.

    P74308-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MQSFNRINSM KYFPLSNGEQ IPALGLGTWK SSPQVVGQAV EQALDLGYRH
    60 70 80 90 100
    LDCAAIYGNE AEIGATLANA FTKGVVKREE LWITSKLWSN AHHPDAVLPA
    110 120 130 140 150
    LEKTLQDLGL DYLDLYLIHW PVVIQPDVGF PESGDQLLPF TPASLEGTWQ
    160 170 180 190 200
    ALEKAVDLGL CHHIGVSNFS LKKLEMVLSM ARIPPAVNQV ELHPYLQQSD
    210 220 230 240 250
    LLTFANSQNI LLTAYSPLGS GDRPAAFQQA AEPKLLTDPV INGIAAEQGC
    260 270 280 290 300
    SAAQVLLAWA IQRGTVTIPK SVNPERLEQN LRAADITLTD SEMAKIALLD
    310 320
    RHYRYVSGDF WTMPGSPYTL QNLWDEI
    Length:327
    Mass (Da):36,014
    Last modified:February 1, 1997 - 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:i4B9415E098A8892D
    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
    BA000022 Genomic DNA Translation: BAA18402.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S76143

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    BAA18402; BAA18402; BAA18402

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    syn:slr0942

    <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
    BA000022 Genomic DNA Translation: BAA18402.1
    PIRiS76143

    3D structure databases

    SMRiP74308
    ModBaseiSearch...

    Protein-protein interaction databases

    IntActiP74308, 10 interactors
    STRINGi1148.1653489

    Proteomic databases

    PaxDbiP74308

    Genome annotation databases

    EnsemblBacteriaiBAA18402; BAA18402; BAA18402
    KEGGisyn:slr0942

    Phylogenomic databases

    eggNOGiCOG0656, Bacteria
    InParanoidiP74308
    OMAiWATYNTR
    PhylomeDBiP74308

    Family and domain databases

    CDDicd19123, AKR_AKR3G1, 1 hit
    Gene3Di3.20.20.100, 1 hit
    InterProiView protein in InterPro
    IPR020471, AKR
    IPR044496, AKR3G
    IPR018170, Aldo/ket_reductase_CS
    IPR023210, NADP_OxRdtase_dom
    IPR036812, NADP_OxRdtase_dom_sf
    PfamiView protein in Pfam
    PF00248, Aldo_ket_red, 1 hit
    PIRSFiPIRSF000097, AKR, 1 hit
    PRINTSiPR00069, ALDKETRDTASE
    SUPFAMiSSF51430, SSF51430, 1 hit
    PROSITEiView protein in PROSITE
    PS00798, ALDOKETO_REDUCTASE_1, 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 nameiAKR_SYNY3
    <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: P74308
    <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 4, 2015
    Last sequence update: February 1, 1997
    Last modified: April 7, 2021
    This is version 121 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

    Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
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