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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-Experimental evidence at protein leveli

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

Catalytic activityi

R-CHOH-R' + NADP+ = R-CO-R' + NADPH.2 Publications

Enzyme 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

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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei57 – 571Proton donorBy similarity
    Sitei86 – 861Lowers pKa of active site TyrBy similarity
    Binding sitei119 – 1191SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 2710NADPSequence analysis
    Nucleotide bindingi216 – 28065NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    • aldo-keto reductase (NADP) activity Source: UniProtKB
    • carbonyl reductase (NADPH) activity Source: UniProtKB-EC
    • NADPH binding Source: UniProtKB

    GO - Biological processi

    • oxidation-reduction process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldo/keto reductase slr09422 Publications (EC:1.1.1.1842 Publications)
    Short name:
    AKR2 Publications
    Alternative name(s):
    AKR3G11 Publication
    Gene namesi
    Ordered Locus Names:slr0942Imported
    OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
    Taxonomic identifieri1111708 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
    Proteomesi
    • UP000001425 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 327327Aldo/keto reductase slr0942PRO_0000431728Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    IntActiP74308. 10 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP74308.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    HOGENOMiHOG000250272.
    InParanoidiP74308.
    KOiK00002.
    OMAiQKLRTDH.
    PhylomeDBiP74308.

    Family and domain databases

    CDDicd06660. Aldo_ket_red. 1 hit.
    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    [Graphical view]

    Sequencei

    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
    Checksum:i4B9415E098A8892D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000022 Genomic DNA. Translation: BAA18402.1.
    PIRiS76143.

    Genome annotation databases

    EnsemblBacteriaiBAA18402; BAA18402; BAA18402.
    KEGGisyn:slr0942.
    PATRICi23840926. VBISynSp132158_2017.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000022 Genomic DNA. Translation: BAA18402.1.
    PIRiS76143.

    3D structure databases

    ProteinModelPortaliP74308.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP74308. 10 interactions.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAA18402; BAA18402; BAA18402.
    KEGGisyn:slr0942.
    PATRICi23840926. VBISynSp132158_2017.

    Phylogenomic databases

    HOGENOMiHOG000250272.
    InParanoidiP74308.
    KOiK00002.
    OMAiQKLRTDH.
    PhylomeDBiP74308.

    Family and domain databases

    CDDicd06660. Aldo_ket_red. 1 hit.
    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAKR_SYNY3
    AccessioniPrimary (citable) accession number: P74308
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 4, 2015
    Last sequence update: February 1, 1997
    Last modified: September 7, 2016
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Synechocystis PCC 6803
      Synechocystis (strain PCC 6803): entries and gene names

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.