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P0A9J4 (PANE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-dehydropantoate 2-reductase

EC=1.1.1.169
Alternative name(s):
Ketopantoate reductase
Short name=KPA reductase
Short name=KPR
Gene names
Name:panE
Synonyms:apbA
Ordered Locus Names:b0425, JW0415
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.

Subunit structure

Monomer. Ref.9

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the ketopantoate reductase family.

Biophysicochemical properties

Kinetic parameters:

KM=30 µM for ketopantoate Ref.6 Ref.9 Ref.12

KM=7.3 µM for NADPH

Mass spectrometry

Molecular mass is 33976 Da from positions 1 - 303. Determined by ESI. Ref.9

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processpantothenate biosynthetic process from valine

Inferred from mutant phenotype PubMed 10553653. Source: EcoCyc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function2-dehydropantoate 2-reductase activity

Inferred from direct assay Ref.5. Source: EcoCyc

NADP binding

Inferred from direct assay Ref.5. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3033032-dehydropantoate 2-reductase
PRO_0000157301

Regions

Nucleotide binding7 – 126NADP

Sites

Active site1761Proton donor
Binding site311NADP; via amide nitrogen
Binding site981NADP; via amide nitrogen
Binding site981Substrate
Binding site1221NADP; via amide nitrogen and carbonyl oxygen
Binding site1801Substrate
Binding site1841Substrate
Binding site1941Substrate
Binding site2411Substrate
Binding site2441Substrate
Binding site2561NADP

Experimental info

Mutagenesis311R → A: Increases KM for NADP 4-fold. Ref.8
Mutagenesis721K → A: Increases KM for NADP 10-fold. Ref.12
Mutagenesis981N → A: Increases KM for ketopantoate 140-fold. Strongly decreases catalytic activity. Ref.8 Ref.11
Mutagenesis1761K → A: Increases KM for ketopantoate 1400-fold. Decreases Vmax 230-fold. Loss of activity; when associated with A-256. Ref.6 Ref.11
Mutagenesis2441S → A: Increases KM for ketopantoate 230-fold. Ref.12
Mutagenesis2561E → A: Increases KM for ketopantoate 1100-fold. Decreases Vmax 40-fold. Loss of activity; when associated with A-176. Ref.6 Ref.11

Secondary structure

......................................................... 303
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A9J4 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: ED7027BFE6F86D6F

FASTA30333,871
        10         20         30         40         50         60 
MKITVLGCGA LGQLWLTALC KQGHEVQGWL RVPQPYCSVN LVETDGSIFN ESLTANDPDF 

        70         80         90        100        110        120 
LATSDLLLVT LKAWQVSDAV KSLASTLPVT TPILLIHNGM GTIEELQNIQ QPLLMGTTTH 

       130        140        150        160        170        180 
AARRDGNVII HVANGITHIG PARQQDGDYS YLADILQTVL PDVAWHNNIR AELWRKLAVN 

       190        200        210        220        230        240 
CVINPLTAIW NCPNGELRHH PQEIMQICEE VAAVIEREGH HTSAEDLRDY VMQVIDATAE 

       250        260        270        280        290        300 
NISSMLQDIR ALRHTEIDYI NGFLLRRARA HGIAVPENTR LFEMVKRKES EYERIGTGLP 


RPW 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U82664 Genomic DNA. Translation: AAB40181.1.
U00096 Genomic DNA. Translation: AAC73528.1.
AP009048 Genomic DNA. Translation: BAE76205.1.
U34923 Genomic DNA. Translation: AAA82703.1.
PIRA64772.
RefSeqNP_414959.1. NC_000913.3.
YP_488717.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KS9X-ray1.70A1-291[»]
1YJQX-ray2.09A1-303[»]
1YONX-ray1.95A1-303[»]
2OFPX-ray2.30A/B1-303[»]
ProteinModelPortalP0A9J4.
SMRP0A9J4. Positions 1-292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0A9J4. 5 interactions.
STRING511145.b0425.

Chemistry

BindingDBP0A9J4.
ChEMBLCHEMBL4855.

Proteomic databases

PRIDEP0A9J4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73528; AAC73528; b0425.
BAE76205; BAE76205; BAE76205.
GeneID12933987.
945065.
KEGGecj:Y75_p0413.
eco:b0425.
PATRIC32116001. VBIEscCol129921_0442.

Organism-specific databases

EchoBASEEB3056.
EcoGeneEG13271. panE.

Phylogenomic databases

eggNOGCOG1893.
HOGENOMHOG000050223.
KOK00077.
OMASQCHILL.
OrthoDBEOG68SVW3.
PhylomeDBP0A9J4.

Enzyme and pathway databases

BioCycEcoCyc:2-DEHYDROPANTOATE-REDUCT-MONOMER.
ECOL316407:JW0415-MONOMER.
MetaCyc:2-DEHYDROPANTOATE-REDUCT-MONOMER.
SABIO-RKP0A9J4.
UniPathwayUPA00028; UER00004.

Gene expression databases

GenevestigatorP0A9J4.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR003710. ApbA.
IPR013752. ApbA_C.
IPR013332. ApbA_N.
IPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF02558. ApbA. 1 hit.
PF08546. ApbA_C. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 1 hit.
TIGRFAMsTIGR00745. apbA_panE. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A9J4.
PROP0A9J4.

Entry information

Entry namePANE_ECOLI
AccessionPrimary (citable) accession number: P0A9J4
Secondary accession number(s): P77728, Q2MC01, Q46947
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: May 14, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene