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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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei31 – 311NADP; via amide nitrogen2 Publications
    Binding sitei98 – 981NADP; via amide nitrogen2 Publications
    Binding sitei98 – 981Substrate1 Publication
    Binding sitei122 – 1221NADP; via amide nitrogen and carbonyl oxygen2 Publications
    Active sitei176 – 1761Proton donor
    Binding sitei180 – 1801Substrate1 Publication
    Binding sitei184 – 1841Substrate1 Publication
    Binding sitei194 – 1941Substrate1 Publication
    Binding sitei241 – 2411Substrate1 Publication
    Binding sitei244 – 2441Substrate1 Publication
    Binding sitei256 – 2561NADP2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi7 – 126NADP2 Publications

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi31 – 311R → A: Increases KM for NADP 4-fold. 1 Publication
    Mutagenesisi72 – 721K → A: Increases KM for NADP 10-fold. 1 Publication
    Mutagenesisi98 – 981N → A: Increases KM for ketopantoate 140-fold. Strongly decreases catalytic activity. 2 Publications
    Mutagenesisi176 – 1761K → A: Increases KM for ketopantoate 1400-fold. Decreases Vmax 230-fold. Loss of activity; when associated with A-256. 2 Publications
    Mutagenesisi244 – 2441S → A: Increases KM for ketopantoate 230-fold. 1 Publication
    Mutagenesisi256 – 2561E → A: Increases KM for ketopantoate 1100-fold. Decreases Vmax 40-fold. Loss of activity; when associated with A-176. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3033032-dehydropantoate 2-reductasePRO_0000157301Add
    BLAST

    Proteomic databases

    PRIDEiP0A9J4.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A9J4.

    Interactioni

    Subunit structurei

    Monomer.4 Publications

    Protein-protein interaction databases

    IntActiP0A9J4. 5 interactions.
    STRINGi511145.b0425.

    Structurei

    Secondary structure

    1
    303
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65Combined sources
    Helixi10 – 2112Combined sources
    Beta strandi25 – 295Combined sources
    Beta strandi35 – 428Combined sources
    Beta strandi44 – 463Combined sources
    Beta strandi48 – 569Combined sources
    Helixi58 – 625Combined sources
    Beta strandi65 – 695Combined sources
    Helixi73 – 753Combined sources
    Helixi76 – 849Combined sources
    Beta strandi93 – 964Combined sources
    Beta strandi98 – 1003Combined sources
    Helixi104 – 1063Combined sources
    Beta strandi113 – 1186Combined sources
    Beta strandi121 – 1255Combined sources
    Beta strandi128 – 1336Combined sources
    Beta strandi137 – 1437Combined sources
    Helixi144 – 1463Combined sources
    Helixi151 – 1577Combined sources
    Beta strandi163 – 1653Combined sources
    Turni167 – 1693Combined sources
    Helixi170 – 18920Combined sources
    Helixi194 – 1996Combined sources
    Helixi201 – 21818Combined sources
    Helixi224 – 23714Combined sources
    Turni238 – 2403Combined sources
    Helixi244 – 2507Combined sources
    Helixi257 – 2593Combined sources
    Helixi261 – 27111Combined sources
    Helixi276 – 29015Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KS9X-ray1.70A1-291[»]
    1YJQX-ray2.09A1-303[»]
    1YONX-ray1.95A1-303[»]
    2OFPX-ray2.30A/B1-303[»]
    ProteinModelPortaliP0A9J4.
    SMRiP0A9J4. Positions 1-292.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9J4.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ketopantoate reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG1893.
    HOGENOMiHOG000050223.
    InParanoidiP0A9J4.
    KOiK00077.
    OMAiWKWAKAI.
    OrthoDBiEOG68SVW3.
    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.
    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.

    Genome annotation databases

    EnsemblBacteriaiAAC73528; AAC73528; b0425.
    BAE76205; BAE76205; BAE76205.
    GeneIDi945065.
    KEGGiecj:Y75_p0413.
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KS9X-ray1.70A1-291[»]
    1YJQX-ray2.09A1-303[»]
    1YONX-ray1.95A1-303[»]
    2OFPX-ray2.30A/B1-303[»]
    ProteinModelPortaliP0A9J4.
    SMRiP0A9J4. Positions 1-292.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP0A9J4. 5 interactions.
    STRINGi511145.b0425.

    Chemistry

    BindingDBiP0A9J4.
    ChEMBLiCHEMBL4855.

    Proteomic databases

    PRIDEiP0A9J4.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73528; AAC73528; b0425.
    BAE76205; BAE76205; BAE76205.
    GeneIDi945065.
    KEGGiecj:Y75_p0413.
    eco:b0425.
    PATRICi32116001. VBIEscCol129921_0442.

    Organism-specific databases

    EchoBASEiEB3056.
    EcoGeneiEG13271. panE.

    Phylogenomic databases

    eggNOGiCOG1893.
    HOGENOMiHOG000050223.
    InParanoidiP0A9J4.
    KOiK00077.
    OMAiWKWAKAI.
    OrthoDBiEOG68SVW3.
    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.

    Gene expression databases

    GenevestigatoriP0A9J4.

    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.
    TIGRFAMsiTIGR00745. apbA_panE. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "The biosynthesis of thiamin in Escherichia coli K-12: structural genes for thiamin biosynthetic enzymes (thiCEFGH and thiJ) and function of the thiE gene product (thiamin phosphate synthase [E.C. 2.5.1.3])."
      Backstrom A.D.
      Thesis (1996), Cornell University, United States
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-303.
      Strain: K12.
    5. "Kinetic and mechanistic analysis of the E. coli panE-encoded ketopantoate reductase."
      Zheng R., Blanchard J.S.
      Biochemistry 39:3708-3717(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Strain: K12.
    6. "Identification of active site residues in E. coli ketopantoate reductase by mutagenesis and chemical rescue."
      Zheng R., Blanchard J.S.
      Biochemistry 39:16244-16251(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-176 AND GLU-256, BIOPHYSICOCHEMICAL PROPERTIES.
    7. "Biophysical tools to monitor enzyme-ligand interactions of enzymes involved in vitamin biosynthesis."
      Ciulli A., Abell C.
      Biochem. Soc. Trans. 33:767-771(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: LIGAND BINDING.
    8. "Probing hot spots at protein-ligand binding sites: a fragment-based approach using biophysical methods."
      Ciulli A., Williams G., Smith A.G., Blundell T.L., Abell C.
      J. Med. Chem. 49:4992-5000(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: LIGAND BINDING, MUTAGENESIS OF ARG-31 AND ASN-98.
    9. "Crystal structure of Escherichia coli ketopantoate reductase at 1.7 A resolution and insight into the enzyme mechanism."
      Matak-Vinkovic D., Vinkovic M., Saldanha S.A., Ashurst J.L., von Delft F., Inoue T., Miguel R.N., Smith A.G., Blundell T.L., Abell C.
      Biochemistry 40:14493-14500(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), PROTEIN SEQUENCE OF 1-9, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    10. "The crystal structure of Escherichia coli ketopantoate reductase with NADP+ bound."
      Lobley C.M.C., Ciulli A., Whitney H.M., Williams G., Smith A.G., Abell C., Blundell T.L.
      Biochemistry 44:8930-8939(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) IN COMPLEX WITH NADP.
    11. "pH-tuneable binding of 2'-phospho-ADP-ribose to ketopantoate reductase: a structural and calorimetric study."
      Ciulli A., Lobley C.M.C., Tuck K.L., Smith A.G., Blundell T.L., Abell C.
      Acta Crystallogr. D 63:171-178(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH NADP ANALOG, MUTAGENESIS OF ASN-98; LYS-176 AND GLU-256.
    12. "Crystal structure of Escherichia coli ketopantoate reductase in a ternary complex with NADP+ and pantoate bound: substrate recognition, conformational change, and cooperativity."
      Ciulli A., Chirgadze D.Y., Smith A.G., Blundell T.L., Abell C.
      J. Biol. Chem. 282:8487-8497(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NADP, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-72 AND SER-244.

    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: May 27, 2015
    This is version 95 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

    External Data

    Dasty 3

    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 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.