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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

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

GO - Biological processi

  1. 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

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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.
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

        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.
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:
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.
YP_488717.1. NC_007779.1.

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.
GeneIDi12933987.
945065.
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.
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.
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 (DEC-1996) 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(2005) [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 (1995), 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(1999) [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(1999) [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(2004) [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(2005) [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(2000) [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(2004) [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(2006) [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(2006) [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: April 1, 2015
This is version 93 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.