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Protein

2-dehydropantoate 2-reductase

Gene

panE

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Pathway:i(R)-pantothenate biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes (R)-pantoate from 3-methyl-2-oxobutanoate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 3-methyl-2-oxobutanoate hydroxymethyltransferase (panB)
  2. 2-dehydropantoate 2-reductase (panE), 2-dehydropantoate 2-reductase (panE)
This subpathway is part of the pathway (R)-pantothenate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-pantoate from 3-methyl-2-oxobutanoate, the pathway (R)-pantothenate biosynthesis and in Cofactor biosynthesis.

Sites

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

Regions

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

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:SF0362, S0370
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000002673 Componenti: Chromosome UP000001006 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3033032-dehydropantoate 2-reductasePRO_0000157305Add
BLAST

Proteomic databases

PaxDbiP0A9J5.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi198214.SF0362.

Structurei

3D structure databases

ProteinModelPortaliP0A9J5.
SMRiP0A9J5. Positions 1-292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ketopantoate reductase family.Curated

Phylogenomic databases

eggNOGiCOG1893.
HOGENOMiHOG000050223.
KOiK00077.
OMAiIDDDRGE.
OrthoDBiEOG68SVW3.

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.

P0A9J5-1 [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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN42020.1.
AE014073 Genomic DNA. Translation: AAP15896.1.
RefSeqiNP_706313.1. NC_004337.2.
WP_000705865.1. NZ_LM651928.1.

Genome annotation databases

EnsemblBacteriaiAAN42020; AAN42020; SF0362.
AAP15896; AAP15896; S0370.
GeneIDi1027702.
KEGGisfl:SF0362.
PATRICi18701740. VBIShiFle31049_0403.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN42020.1.
AE014073 Genomic DNA. Translation: AAP15896.1.
RefSeqiNP_706313.1. NC_004337.2.
WP_000705865.1. NZ_LM651928.1.

3D structure databases

ProteinModelPortaliP0A9J5.
SMRiP0A9J5. Positions 1-292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF0362.

Chemistry

BindingDBiP0A9J5.

Proteomic databases

PaxDbiP0A9J5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN42020; AAN42020; SF0362.
AAP15896; AAP15896; S0370.
GeneIDi1027702.
KEGGisfl:SF0362.
PATRICi18701740. VBIShiFle31049_0403.

Phylogenomic databases

eggNOGiCOG1893.
HOGENOMiHOG000050223.
KOiK00077.
OMAiIDDDRGE.
OrthoDBiEOG68SVW3.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00004.

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

  1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiPANE_SHIFL
AccessioniPrimary (citable) accession number: P0A9J5
Secondary accession number(s): P77728, Q46947
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: July 22, 2015
This is version 82 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

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.