Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aldo-keto reductase IolS

Gene

iolS

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In vitro, is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose and methylglyoxal in the presence of NADPH, albeit with poor efficiency. Shows only trace activity with benzaldehyde and butyraldehyde. Is unable to oxidize myo-inositol with either NADP+ or NAD+ as a cosubstrate and also does not use glucose, 2-pyridine carboxyaldehyde, fructose, xylose and succinyl semialdehyde as a substrate (PubMed:12554958, PubMed:15019785). The physiological function of this enzyme is not clear (PubMed:15019785). Does not seem to be necessary for inositol catabolism (PubMed:9226270).3 Publications

Miscellaneous

The 3D-structure shows a unique architecture for an AKR active site, which may explain the low catalytic power.1 Publication

Kineticsi

kcat is 2.07 sec(-1) with DL-glyceraldehyde as substrate. kcat is 2.97 sec(-1) with D-erythrose as substrate.1 Publication
  1. KM=271 mM for DL-glyceraldehyde1 Publication
  2. KM=207 mM for D-erythrose1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei58Proton donor1 Publication1
    Sitei84Lowers pKa of active site Tyr1 Publication1
    Binding sitei175NADP1 Publication1
    Binding sitei214NADP1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi155 – 156NADP1 Publication2
    Nucleotide bindingi203 – 208NADP1 Publication6

    GO - Molecular functioni

    Keywordsi

    Molecular functionOxidoreductase
    LigandNADP

    Enzyme and pathway databases

    BioCyciBSUB:BSU39780-MONOMER.
    SABIO-RKiP46336.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldo-keto reductase IolS1 Publication (EC:1.1.1.-2 Publications)
    Alternative name(s):
    AKR11A1 Publication
    Vegetative protein 1471 Publication
    Short name:
    VEG1471 Publication
    Gene namesi
    Name:iolS1 Publication
    Synonyms:yxbF
    Ordered Locus Names:BSU39780
    ORF Names:SS92ER
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001570 Componenti: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

    Disruption of this gene affects neither growth on inositol nor the inducibility and catabolite repression of Idh synthesis.1 Publication

    Chemistry databases

    DrugBankiDB03461. 2'-Monophosphoadenosine 5'-Diphosphoribose.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000703821 – 310Aldo-keto reductase IolSAdd BLAST310

    Proteomic databases

    PaxDbiP46336.
    PRIDEiP46336.

    Expressioni

    Inductioni

    Induced by inositol (PubMed:9226270). Repressed by glucose (PubMed:11160890). Is cotranscribed with iolR, the repressor of the iol operon (PubMed:9226270).2 Publications

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100021456.

    Structurei

    Secondary structure

    1310
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni26 – 28Combined sources3
    Beta strandi29 – 31Combined sources3
    Helixi34 – 46Combined sources13
    Beta strandi51 – 53Combined sources3
    Turni56 – 61Combined sources6
    Helixi62 – 71Combined sources10
    Helixi76 – 78Combined sources3
    Beta strandi80 – 85Combined sources6
    Beta strandi87 – 90Combined sources4
    Beta strandi93 – 96Combined sources4
    Helixi100 – 114Combined sources15
    Beta strandi119 – 124Combined sources6
    Beta strandi129 – 131Combined sources3
    Helixi133 – 145Combined sources13
    Beta strandi148 – 150Combined sources3
    Beta strandi152 – 156Combined sources5
    Helixi159 – 165Combined sources7
    Turni166 – 168Combined sources3
    Beta strandi173 – 177Combined sources5
    Helixi184 – 186Combined sources3
    Helixi189 – 196Combined sources8
    Beta strandi199 – 204Combined sources6
    Turni205 – 209Combined sources5
    Helixi210 – 212Combined sources3
    Helixi226 – 229Combined sources4
    Helixi231 – 233Combined sources3
    Helixi235 – 246Combined sources12
    Helixi249 – 254Combined sources6
    Helixi259 – 269Combined sources11
    Helixi283 – 290Combined sources8
    Helixi291 – 294Combined sources4
    Helixi299 – 308Combined sources10

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1PYFX-ray1.80A1-310[»]
    1PZ0X-ray2.35A1-310[»]
    ProteinModelPortaliP46336.
    SMRiP46336.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46336.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family. Aldo/keto reductase 11 subfamily.1 Publication

    Phylogenomic databases

    eggNOGiENOG4105CPC. Bacteria.
    COG0667. LUCA.
    HOGENOMiHOG000250284.
    InParanoidiP46336.
    KOiK06607.
    OMAiAVSIQNP.
    PhylomeDBiP46336.

    Family and domain databases

    CDDicd06660. Aldo_ket_red. 1 hit.
    Gene3Di3.20.20.100. 1 hit.
    InterProiView protein in InterPro
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase.
    IPR023210. NADP_OxRdtase_dom.
    IPR036812. NADP_OxRdtase_dom_sf.
    PfamiView protein in Pfam
    PF00248. Aldo_ket_red. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiView protein in PROSITE
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P46336-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKKAKLGKSD LQVFPIGLGT NAVGGHNLYP NLNEETGKEL VREAIRNGVT
    60 70 80 90 100
    MLDTAYIYGI GRSEELIGEV LREFNREDVV IATKAAHRKQ GNDFVFDNSP
    110 120 130 140 150
    DFLKKSVDES LKRLNTDYID LFYIHFPDEH TPKDEAVNAL NEMKKAGKIR
    160 170 180 190 200
    SIGVSNFSLE QLKEANKDGL VDVLQGEYNL LNREAEKTFF PYTKEHNISF
    210 220 230 240 250
    IPYFPLVSGL LAGKYTEDTT FPEGDLRNEQ EHFKGERFKE NIRKVNKLAP
    260 270 280 290 300
    IAEKHNVDIP HIVLAWYLAR PEIDILIPGA KRADQLIDNI KTADVTLSQE
    310
    DISFIDKLFA
    Length:310
    Mass (Da):35,168
    Last modified:November 1, 1995 - v1
    Checksum:iA870F226F8684867
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB005554 Genomic DNA. Translation: BAA21607.1.
    AL009126 Genomic DNA. Translation: CAB16014.1.
    PIRiD69646.
    RefSeqiNP_391857.1. NC_000964.3.
    WP_003243075.1. NZ_JNCM01000034.1.

    Genome annotation databases

    EnsemblBacteriaiCAB16014; CAB16014; BSU39780.
    GeneIDi937636.
    KEGGibsu:BSU39780.
    PATRICifig|224308.179.peg.4303.

    Similar proteinsi

    Entry informationi

    Entry nameiIOLS_BACSU
    AccessioniPrimary (citable) accession number: P46336
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 25, 2017
    This is version 131 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families