Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0A9J4

- PANE_ECOLI

UniProt

P0A9J4 - PANE_ECOLI

Protein

2-dehydropantoate 2-reductase

Gene

panE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (19 Jul 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. 2-dehydropantoate 2-reductase activity Source: EcoCyc
    2. NADP binding Source: EcoCyc

    GO - Biological processi

    1. pantothenate biosynthetic process from valine Source: EcoCyc

    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.
    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG13271. panE.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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 – 65
    Helixi10 – 2112
    Beta strandi25 – 295
    Beta strandi35 – 428
    Beta strandi44 – 463
    Beta strandi48 – 569
    Helixi58 – 625
    Beta strandi65 – 695
    Helixi73 – 753
    Helixi76 – 849
    Beta strandi93 – 964
    Beta strandi98 – 1003
    Helixi104 – 1063
    Beta strandi113 – 1186
    Beta strandi121 – 1255
    Beta strandi128 – 1336
    Beta strandi137 – 1437
    Helixi144 – 1463
    Helixi151 – 1577
    Beta strandi163 – 1653
    Turni167 – 1693
    Helixi170 – 18920
    Helixi194 – 1996
    Helixi201 – 21818
    Helixi224 – 23714
    Turni238 – 2403
    Helixi244 – 2507
    Helixi257 – 2593
    Helixi261 – 27111
    Helixi276 – 29015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK00077.
    OMAiSQCHILL.
    OrthoDBiEOG68SVW3.
    PhylomeDBiP0A9J4.

    Family and domain databases

    Gene3Di1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR003710. ApbA.
    IPR013328. DH_multihelical.
    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

    MKITVLGCGA LGQLWLTALC KQGHEVQGWL RVPQPYCSVN LVETDGSIFN    50
    ESLTANDPDF LATSDLLLVT LKAWQVSDAV KSLASTLPVT TPILLIHNGM 100
    GTIEELQNIQ QPLLMGTTTH AARRDGNVII HVANGITHIG PARQQDGDYS 150
    YLADILQTVL PDVAWHNNIR AELWRKLAVN CVINPLTAIW NCPNGELRHH 200
    PQEIMQICEE VAAVIEREGH HTSAEDLRDY VMQVIDATAE NISSMLQDIR 250
    ALRHTEIDYI NGFLLRRARA HGIAVPENTR LFEMVKRKES EYERIGTGLP 300
    RPW 303
    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:
    EMBL
    GenBank
    DDBJ
    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.
    YP_488717.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73528; AAC73528; b0425.
    BAE76205; BAE76205; BAE76205.
    GeneIDi12933987.
    945065.
    KEGGiecj:Y75_p0413.
    eco:b0425.
    PATRICi32116001. VBIEscCol129921_0442.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi A64772.
    RefSeqi NP_414959.1. NC_000913.3.
    YP_488717.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KS9 X-ray 1.70 A 1-291 [» ]
    1YJQ X-ray 2.09 A 1-303 [» ]
    1YON X-ray 1.95 A 1-303 [» ]
    2OFP X-ray 2.30 A/B 1-303 [» ]
    ProteinModelPortali P0A9J4.
    SMRi P0A9J4. Positions 1-292.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P0A9J4. 5 interactions.
    STRINGi 511145.b0425.

    Chemistry

    BindingDBi P0A9J4.
    ChEMBLi CHEMBL4855.

    Proteomic databases

    PRIDEi P0A9J4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73528 ; AAC73528 ; b0425 .
    BAE76205 ; BAE76205 ; BAE76205 .
    GeneIDi 12933987.
    945065.
    KEGGi ecj:Y75_p0413.
    eco:b0425.
    PATRICi 32116001. VBIEscCol129921_0442.

    Organism-specific databases

    EchoBASEi EB3056.
    EcoGenei EG13271. panE.

    Phylogenomic databases

    eggNOGi COG1893.
    HOGENOMi HOG000050223.
    KOi K00077.
    OMAi SQCHILL.
    OrthoDBi EOG68SVW3.
    PhylomeDBi P0A9J4.

    Enzyme and pathway databases

    UniPathwayi UPA00028 ; UER00004 .
    BioCyci EcoCyc:2-DEHYDROPANTOATE-REDUCT-MONOMER.
    ECOL316407:JW0415-MONOMER.
    MetaCyc:2-DEHYDROPANTOATE-REDUCT-MONOMER.
    SABIO-RK P0A9J4.

    Miscellaneous databases

    EvolutionaryTracei P0A9J4.
    PROi P0A9J4.

    Gene expression databases

    Genevestigatori P0A9J4.

    Family and domain databases

    Gene3Di 1.10.1040.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR008927. 6-PGluconate_DH_C-like.
    IPR003710. ApbA.
    IPR013328. DH_multihelical.
    IPR013752. KPA_reductase.
    IPR013332. KPR_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF02558. ApbA. 1 hit.
    PF08546. ApbA_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48179. SSF48179. 1 hit.
    TIGRFAMsi TIGR00745. apbA_panE. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 89 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