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Protein

Aldo-keto reductase YhdN

Gene

yhdN

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

Functioni

Aldo-keto reductase (AKR) that displays broad substrate specificity in vitro. Is able to reduce the standard AKR substrates DL-glyceraldehyde, D-erythrose, methylglyoxal, p-nitrobenzaldehyde, benzaldehyde and butyraldehyde, in the presence of NADPH. Cannot use NADH as a cosubstrate. Does not act on glucose, 2-pyridine carboxyaldehyde, fructose and xylose. The physiological function of this enzyme is not clear. May play a role in bacterial stress response and/or in detoxification of reactive aldehydes.2 Publications

Kineticsi

kcat is 1.37 sec(-1) with DL-glyceraldehyde as substrate (PubMed:12554958). kcat is 1.09 sec(-1) with p-nitrobenzaldehyde as substrate (PubMed:12554958). kcat is 4.02 sec(-1) with D-erythrose as substrate (PubMed:15019785). kcat is 5.33 sec(-1) with methylglyoxal as substrate (PubMed:15019785). kcat is 2.59 sec(-1) with benzaldehyde as substrate (PubMed:15019785). kcat is 3.96 sec(-1) with butyraldehyde as substrate (PubMed:15019785).2 Publications
  1. KM=2.2 mM for DL-glyceraldehyde1 Publication
  2. KM=0.67 mM for p-nitrobenzaldehyde1 Publication
  3. KM=12.2 µM for NADPH1 Publication
  4. KM=0.54 mM for D-erythrose1 Publication
  5. KM=0.74 mM for methylglyoxal1 Publication
  6. KM=1.91 mM for benzaldehyde1 Publication
  7. KM=1.51 mM for butyraldehyde1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei52NADPCombined sources1 Publication1
    Active sitei57Proton donor1 Publication1
    Sitei84Lowers pKa of active site Tyr1 Publication1
    Binding sitei175NADPCombined sources1 Publication1
    Binding sitei214NADPCombined sources1 Publication1
    Binding sitei227NADPCombined sources1 Publication1
    Binding sitei286NADPCombined sources1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi20 – 21NADPCombined sources1 Publication2
    Nucleotide bindingi203 – 208NADPCombined sources1 Publication6
    Nucleotide bindingi280 – 282NADPCombined sources1 Publication3

    GO - Molecular functioni

    Keywordsi

    Molecular functionOxidoreductase
    Biological processStress response
    LigandNADP

    Enzyme and pathway databases

    BioCyciBSUB:BSU09530-MONOMER.
    SABIO-RKiP80874.

    Protein family/group databases

    TCDBi8.A.5.1.4. the voltage-gated k(+) channel -subunit (kv) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldo-keto reductase YhdN1 Publication (EC:1.1.1.-2 Publications)
    Alternative name(s):
    AKR11B1 Publication
    General stress protein 691 Publication
    Short name:
    GSP691 Publication
    Gene namesi
    Name:yhdN
    Ordered Locus Names:BSU09530
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001570 Componenti: Chromosome

    Pathology & Biotechi

    Chemistry databases

    DrugBankiDB03461. 2'-Monophosphoadenosine 5'-Diphosphoribose.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000703881 – 331Aldo-keto reductase YhdNAdd BLAST331

    Proteomic databases

    PaxDbiP80874.
    PRIDEiP80874.

    Expressioni

    Inductioni

    Is under the control of the sigma-B transcription factor. Is induced by heat shock, salt stress, oxidative stress, glucose limitation and oxygen limitation.1 Publication

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100005331.

    Structurei

    Secondary structure

    1331
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 5Combined sources3
    Beta strandi12 – 19Combined sources8
    Helixi22 – 24Combined sources3
    Turni26 – 29Combined sources4
    Helixi33 – 45Combined sources13
    Beta strandi50 – 52Combined sources3
    Helixi57 – 60Combined sources4
    Helixi61 – 73Combined sources13
    Helixi76 – 78Combined sources3
    Beta strandi80 – 85Combined sources6
    Beta strandi87 – 92Combined sources6
    Beta strandi94 – 96Combined sources3
    Helixi100 – 113Combined sources14
    Beta strandi119 – 124Combined sources6
    Helixi133 – 145Combined sources13
    Beta strandi148 – 150Combined sources3
    Beta strandi152 – 154Combined sources3
    Helixi159 – 166Combined sources8
    Helixi184 – 186Combined sources3
    Helixi189 – 195Combined sources7
    Beta strandi199 – 203Combined sources5
    Helixi207 – 209Combined sources3
    Helixi226 – 228Combined sources3
    Helixi231 – 233Combined sources3
    Turni235 – 237Combined sources3
    Helixi238 – 256Combined sources19
    Helixi260 – 269Combined sources10
    Beta strandi276 – 280Combined sources5
    Helixi284 – 287Combined sources4
    Beta strandi293 – 295Combined sources3
    Helixi300 – 313Combined sources14
    Helixi321 – 323Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1PZ1X-ray2.20A/B1-331[»]
    ProteinModelPortaliP80874.
    SMRiP80874.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP80874.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiENOG4108FN7. Bacteria.
    COG0667. LUCA.
    HOGENOMiHOG000250284.
    InParanoidiP80874.
    OMAiWGMSEAG.
    PhylomeDBiP80874.

    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.
    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.

    P80874-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEYTSIADTG IEASRIGLGT WAIGGTMWGG TDEKTSIETI RAALDQGITL
    60 70 80 90 100
    IDTAPAYGFG QSEEIVGKAI KEYGKRDQVI LATKTALDWK NNQLFRHANR
    110 120 130 140 150
    ARIVEEVENS LKRLQTDYID LYQVHWPDPL VPIEETAEVM KELYDAGKIR
    160 170 180 190 200
    AIGVSNFSIE QMDTFRAVAP LHTIQPPYNL FEREMEESVL PYAKDNKITT
    210 220 230 240 250
    LLYGSLCRGL LTGKMTEEYT FEGDDLRNHD PKFQKPRFKE YLSAVNQLDK
    260 270 280 290 300
    LAKTRYGKSV IHLAVRWILD QPGADIALWG ARKPGQLEAL SEITGWTLNS
    310 320 330
    EDQKDINTIL ENTISDPVGP EFMAPPTREE I
    Length:331
    Mass (Da):37,312
    Last modified:July 15, 1998 - v2
    Checksum:i82BC24D46E4994D0
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti25G → K AA sequence (PubMed:9298659).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y14082 Genomic DNA. Translation: CAA74498.1.
    AL009126 Genomic DNA. Translation: CAB12792.1.
    PIRiD69826.
    RefSeqiNP_388834.1. NC_000964.3.
    WP_003245422.1. NZ_JNCM01000035.1.

    Genome annotation databases

    EnsemblBacteriaiCAB12792; CAB12792; BSU09530.
    GeneIDi939270.
    KEGGibsu:BSU09530.
    PATRICifig|224308.179.peg.1026.

    Similar proteinsi

    Entry informationi

    Entry nameiGS69_BACSU
    AccessioniPrimary (citable) accession number: P80874
    Secondary accession number(s): O07583
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 15, 1998
    Last modified: September 27, 2017
    This is version 124 of the entry and version 2 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