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Q8Z8W3 (PANE_SALTI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 95. 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:STY0473, t2430
OrganismSalmonella typhi [Complete proteome] [HAMAP]
Taxonomic identifier90370 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the ketopantoate reductase family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete 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_0000157303

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

Experimental info

Sequence conflict1171A → T in AAO70019. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8Z8W3 [UniParc].

Last modified February 21, 2002. Version 1.
Checksum: 0369C148A42BF583

FASTA30333,842
        10         20         30         40         50         60 
MKITVLGCGA LGQLWLSALC KHGHDVQGWL RVPQPYCSVN LIDTDGSFFN ESLTANDPDF 

        70         80         90        100        110        120 
LAKSELLLVT LKAWQVSDAV RTLASTLPVT SPILLIHNGM GTIEELQSIQ QPMLMGAITH 

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

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

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


RPW 

« Hide

References

[1]"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18."
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. expand/collapse author list , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:848-852(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CT18.
[2]"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
J. Bacteriol. 185:2330-2337(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL513382 Genomic DNA. Translation: CAD08890.1.
AE014613 Genomic DNA. Translation: AAO70019.1.
RefSeqNP_455028.1. NC_003198.1.
NP_806159.1. NC_004631.1.

3D structure databases

ProteinModelPortalQ8Z8W3.
SMRQ8Z8W3. Positions 1-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220341.STY0473.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO70019; AAO70019; t2430.
CAD08890; CAD08890; CAD08890.
GeneID1246947.
KEGGsty:STY0473.
PATRIC18538780. VBISalEnt120419_0474.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1893.
HOGENOMHOG000050223.
KOK00077.
OMAIEFINGW.
OrthoDBEOG68SVW3.

Enzyme and pathway databases

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_SALTI
AccessionPrimary (citable) accession number: Q8Z8W3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: February 21, 2002
Last modified: May 14, 2014
This is version 95 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

PATHWAY comments

Index of metabolic and biosynthesis pathways