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P37402 (PANE_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:STM0434
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

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. Has a strong preference for NADPH over NADH as the electron acceptor. Pantoate, ketoisovalerate, oxaloacetate, pyruvate, 3-hydroxypyruvate, alpha-ketoglutarate, alpha-ketobutyrate, and acetaldehyde can not served as substrates for reduction. Ref.3

Catalytic activity

(R)-pantoate + NADP+ = 2-dehydropantoate + NADPH. Ref.3

Pathway

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

Subunit structure

Monomer. Ref.3

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the ketopantoate reductase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.0776 mM for NADPH Ref.3

KM=0.0742 mM for 2-dehydropantoate

Vmax=89.3 µmol/min/mg enzyme

pH dependence:

Optimum pH is 6.25.

Temperature dependence:

Optimum temperature is 42 degrees Celsius.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processpantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function2-dehydropantoate 2-reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

NADP binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3033032-dehydropantoate 2-reductase
PRO_0000157304

Regions

Nucleotide binding7 – 126NADP By similarity

Sites

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

Natural variations

Natural variant1211A → T in strain: DM4593.

Experimental info

Sequence conflict74 – 8613WQVSD…TLAST → GFRRSTNPGVN in AAA56681. Ref.1
Sequence conflict1241Missing in AAA56681. Ref.1
Sequence conflict246 – 2472LQ → FE in AAA56681. Ref.1
Sequence conflict275 – 30329VPENS…MPRPW → FRKIAACLKW in AAA56681. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P37402 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 060DA21B75B891A4

FASTA30333,938
        10         20         30         40         50         60 
MKITVLGCGA LGQLWLSALC KHGHDVQGWL RVPQPYCSVN LIDTDGSFFN ESLTANDPDF 

        70         80         90        100        110        120 
LAKSELLLVT LKAWQVSDAV RTLASTLPVT SPILLIHNGM GTIEELQNIQ QPMLMGTITH 

       130        140        150        160        170        180 
AARRDGNIII HVANGTTHIG PAREQDGDYS YLADILQGVL PDVAWHNNIR AEMWRKLAVN 

       190        200        210        220        230        240 
CVINPLTALW NCPNGELRHH TDEINAICEE VAAVIEREGY HTSADDLRYY VEQVIDSTAE 

       250        260        270        280        290        300 
NISSMLQDVR AMRHTEIDYI TGYLLKRARV HGLAVPENSR LFEMVKRKES EYERSGTGMP 


RPW 

« Hide

References

« Hide 'large scale' references
[1]"apbA, a new genetic locus involved in thiamine biosynthesis in Salmonella typhimurium."
Downs D.M., Petersen L.
J. Bacteriol. 176:4858-4864(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"ApbA, the ketopantoate reductase enzyme of Salmonella typhimurium is required for the synthesis of thiamine via the alternative pyrimidine biosynthetic pathway."
Frodyma M.E., Downs D.M.
J. Biol. Chem. 273:5572-5576(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[4]"The panE gene, encoding ketopantoate reductase, maps at 10 minutes and is allelic to apbA in Salmonella typhimurium."
Frodyma M.E., Downs D.M.
J. Bacteriol. 180:4757-4759(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SHOWS THAT APBA IS PANE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09529 Genomic DNA. Translation: AAA56681.1.
AE006468 Genomic DNA. Translation: AAL19388.1.
PIRA55849.
RefSeqNP_459429.1. NC_003197.1.

3D structure databases

ProteinModelPortalP37402.
SMRP37402. Positions 1-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM0434.

Proteomic databases

PaxDbP37402.
PRIDEP37402.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL19388; AAL19388; STM0434.
GeneID1251953.
KEGGstm:STM0434.
PATRIC32379203. VBISalEnt20916_0463.

Phylogenomic databases

eggNOGCOG1893.
HOGENOMHOG000050223.
KOK00077.
OMAIEFINGW.
OrthoDBEOG68SVW3.
PhylomeDBP37402.

Enzyme and pathway databases

BioCycSENT99287:GCTI-435-MONOMER.
UniPathwayUPA00028; UER00004.

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...

Entry information

Entry namePANE_SALTY
AccessionPrimary (citable) accession number: P37402
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 109 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways