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Protein

2-dehydropantoate 2-reductase

Gene

panE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.

Catalytic activityi

(R)-pantoate + NADP+ = 2-dehydropantoate + NADPH.

Kineticsi

  1. KM=30 µM for ketopantoate3 Publications
  2. KM=7.3 µM for NADPH3 Publications

    Pathwayi: (R)-pantothenate biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes (R)-pantoate from 3-methyl-2-oxobutanoate.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. 3-methyl-2-oxobutanoate hydroxymethyltransferase (panB)
    2. 2-dehydropantoate 2-reductase (panE)
    This subpathway is part of the pathway (R)-pantothenate biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-pantoate from 3-methyl-2-oxobutanoate, the pathway (R)-pantothenate biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei31NADP; via amide nitrogen2 Publications1
    Binding sitei98NADP; via amide nitrogen2 Publications1
    Binding sitei98Substrate1 Publication1
    Binding sitei122NADP; via amide nitrogen and carbonyl oxygen2 Publications1
    Active sitei176Proton donor1
    Binding sitei180Substrate1 Publication1
    Binding sitei184Substrate1 Publication1
    Binding sitei194Substrate1 Publication1
    Binding sitei241Substrate1 Publication1
    Binding sitei244Substrate1 Publication1
    Binding sitei256NADP2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi7 – 12NADP2 Publications6

    GO - Molecular functioni

    • 2-dehydropantoate 2-reductase activity Source: EcoCyc
    • NADP binding Source: EcoCyc

    GO - Biological processi

    • pantothenate biosynthetic process from valine Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Pantothenate biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:2-DEHYDROPANTOATE-REDUCT-MONOMER.
    ECOL316407:JW0415-MONOMER.
    MetaCyc:2-DEHYDROPANTOATE-REDUCT-MONOMER.
    BRENDAi1.1.1.169. 2026.
    SABIO-RKP0A9J4.
    UniPathwayiUPA00028; UER00004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-dehydropantoate 2-reductase (EC:1.1.1.169)
    Alternative name(s):
    Ketopantoate reductase
    Short name:
    KPA reductase
    Short name:
    KPR
    Gene namesi
    Name:panE
    Synonyms:apbA
    Ordered Locus Names:b0425, JW0415
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13271. panE.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi31R → A: Increases KM for NADP 4-fold. 1 Publication1
    Mutagenesisi72K → A: Increases KM for NADP 10-fold. 1 Publication1
    Mutagenesisi98N → A: Increases KM for ketopantoate 140-fold. Strongly decreases catalytic activity. 2 Publications1
    Mutagenesisi176K → A: Increases KM for ketopantoate 1400-fold. Decreases Vmax 230-fold. Loss of activity; when associated with A-256. 2 Publications1
    Mutagenesisi244S → A: Increases KM for ketopantoate 230-fold. 1 Publication1
    Mutagenesisi256E → A: Increases KM for ketopantoate 1100-fold. Decreases Vmax 40-fold. Loss of activity; when associated with A-176. 2 Publications1

    Chemistry databases

    ChEMBLiCHEMBL4855.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001573011 – 3032-dehydropantoate 2-reductaseAdd BLAST303

    Proteomic databases

    PaxDbiP0A9J4.
    PRIDEiP0A9J4.

    Interactioni

    Subunit structurei

    Monomer.4 Publications

    Protein-protein interaction databases

    BioGridi4262981. 324 interactors.
    IntActiP0A9J4. 5 interactors.
    STRINGi511145.b0425.

    Chemistry databases

    BindingDBiP0A9J4.

    Structurei

    Secondary structure

    1303
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 6Combined sources5
    Helixi10 – 21Combined sources12
    Beta strandi25 – 29Combined sources5
    Beta strandi35 – 42Combined sources8
    Beta strandi44 – 46Combined sources3
    Beta strandi48 – 56Combined sources9
    Helixi58 – 62Combined sources5
    Beta strandi65 – 69Combined sources5
    Helixi73 – 75Combined sources3
    Helixi76 – 84Combined sources9
    Beta strandi93 – 96Combined sources4
    Beta strandi98 – 100Combined sources3
    Helixi104 – 106Combined sources3
    Beta strandi113 – 118Combined sources6
    Beta strandi121 – 125Combined sources5
    Beta strandi128 – 133Combined sources6
    Beta strandi137 – 143Combined sources7
    Helixi144 – 146Combined sources3
    Helixi151 – 157Combined sources7
    Beta strandi163 – 165Combined sources3
    Turni167 – 169Combined sources3
    Helixi170 – 189Combined sources20
    Helixi194 – 199Combined sources6
    Helixi201 – 218Combined sources18
    Helixi224 – 237Combined sources14
    Turni238 – 240Combined sources3
    Helixi244 – 250Combined sources7
    Helixi257 – 259Combined sources3
    Helixi261 – 271Combined sources11
    Helixi276 – 290Combined sources15

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1KS9X-ray1.70A1-291[»]
    1YJQX-ray2.09A1-303[»]
    1YONX-ray1.95A1-303[»]
    2OFPX-ray2.30A/B1-303[»]
    ProteinModelPortaliP0A9J4.
    SMRiP0A9J4.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9J4.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ketopantoate reductase family.Curated

    Phylogenomic databases

    eggNOGiENOG4108JZF. Bacteria.
    COG1893. LUCA.
    HOGENOMiHOG000050223.
    InParanoidiP0A9J4.
    KOiK00077.
    OMAiRIPQPYC.
    PhylomeDBiP0A9J4.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR013328. 6PGD_dom_2.
    IPR003710. ApbA.
    IPR013752. KPA_reductase.
    IPR013332. KPR_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF02558. ApbA. 1 hit.
    PF08546. ApbA_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 1 hit.
    SSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR00745. apbA_panE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0A9J4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKITVLGCGA LGQLWLTALC KQGHEVQGWL RVPQPYCSVN LVETDGSIFN
    60 70 80 90 100
    ESLTANDPDF LATSDLLLVT LKAWQVSDAV KSLASTLPVT TPILLIHNGM
    110 120 130 140 150
    GTIEELQNIQ QPLLMGTTTH AARRDGNVII HVANGITHIG PARQQDGDYS
    160 170 180 190 200
    YLADILQTVL PDVAWHNNIR AELWRKLAVN CVINPLTAIW NCPNGELRHH
    210 220 230 240 250
    PQEIMQICEE VAAVIEREGH HTSAEDLRDY VMQVIDATAE NISSMLQDIR
    260 270 280 290 300
    ALRHTEIDYI NGFLLRRARA HGIAVPENTR LFEMVKRKES EYERIGTGLP

    RPW
    Length:303
    Mass (Da):33,871
    Last modified:July 19, 2005 - v1
    Checksum:iED7027BFE6F86D6F
    GO

    Mass spectrometryi

    Molecular mass is 33976 Da from positions 1 - 303. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U82664 Genomic DNA. Translation: AAB40181.1.
    U00096 Genomic DNA. Translation: AAC73528.1.
    AP009048 Genomic DNA. Translation: BAE76205.1.
    U34923 Genomic DNA. Translation: AAA82703.1.
    PIRiA64772.
    RefSeqiNP_414959.1. NC_000913.3.
    WP_000705865.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73528; AAC73528; b0425.
    BAE76205; BAE76205; BAE76205.
    GeneIDi945065.
    KEGGiecj:JW0415.
    eco:b0425.
    PATRICi32116001. VBIEscCol129921_0442.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U82664 Genomic DNA. Translation: AAB40181.1.
    U00096 Genomic DNA. Translation: AAC73528.1.
    AP009048 Genomic DNA. Translation: BAE76205.1.
    U34923 Genomic DNA. Translation: AAA82703.1.
    PIRiA64772.
    RefSeqiNP_414959.1. NC_000913.3.
    WP_000705865.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1KS9X-ray1.70A1-291[»]
    1YJQX-ray2.09A1-303[»]
    1YONX-ray1.95A1-303[»]
    2OFPX-ray2.30A/B1-303[»]
    ProteinModelPortaliP0A9J4.
    SMRiP0A9J4.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262981. 324 interactors.
    IntActiP0A9J4. 5 interactors.
    STRINGi511145.b0425.

    Chemistry databases

    BindingDBiP0A9J4.
    ChEMBLiCHEMBL4855.

    Proteomic databases

    PaxDbiP0A9J4.
    PRIDEiP0A9J4.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73528; AAC73528; b0425.
    BAE76205; BAE76205; BAE76205.
    GeneIDi945065.
    KEGGiecj:JW0415.
    eco:b0425.
    PATRICi32116001. VBIEscCol129921_0442.

    Organism-specific databases

    EchoBASEiEB3056.
    EcoGeneiEG13271. panE.

    Phylogenomic databases

    eggNOGiENOG4108JZF. Bacteria.
    COG1893. LUCA.
    HOGENOMiHOG000050223.
    InParanoidiP0A9J4.
    KOiK00077.
    OMAiRIPQPYC.
    PhylomeDBiP0A9J4.

    Enzyme and pathway databases

    UniPathwayiUPA00028; UER00004.
    BioCyciEcoCyc:2-DEHYDROPANTOATE-REDUCT-MONOMER.
    ECOL316407:JW0415-MONOMER.
    MetaCyc:2-DEHYDROPANTOATE-REDUCT-MONOMER.
    BRENDAi1.1.1.169. 2026.
    SABIO-RKP0A9J4.

    Miscellaneous databases

    EvolutionaryTraceiP0A9J4.
    PROiP0A9J4.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR013328. 6PGD_dom_2.
    IPR003710. ApbA.
    IPR013752. KPA_reductase.
    IPR013332. KPR_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF02558. ApbA. 1 hit.
    PF08546. ApbA_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 1 hit.
    SSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR00745. apbA_panE. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPANE_ECOLI
    AccessioniPrimary (citable) accession number: P0A9J4
    Secondary accession number(s): P77728, Q2MC01, Q46947
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: November 30, 2016
    This is version 105 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

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

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    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.