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P0A9J4

- PANE_ECOLI

UniProt

P0A9J4 - PANE_ECOLI

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Protein

2-dehydropantoate 2-reductase

Gene
panE, apbA, b0425, JW0415
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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 NADPH

Pathwayi

Sites

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

Regions

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

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.
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 Reviewed prediction

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.1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiP0A9J4.

Family & Domainsi

Sequence similaritiesi

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

« 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: September 3, 2014
This is version 88 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

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