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Q8ZC51 (PANE_YERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 96. 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:YPO3171, y1014, YP_0760
OrganismYersinia pestis [Reference proteome] [HAMAP]
Taxonomic identifier632 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

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.

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
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_0000157307

Regions

Nucleotide binding7 – 126NADP By similarity

Sites

Active site1761Proton donor By similarity
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

Sequences

Sequence LengthMass (Da)Tools
Q8ZC51 [UniParc].

Last modified February 21, 2002. Version 1.
Checksum: 3B1D8198D053B9BE

FASTA30333,844
        10         20         30         40         50         60 
MKITVLGCGA LGQLWLSMLH QQDHDVQGWL RVPQPFCSVN VIMLNGESFN RNLTTNDPKH 

        70         80         90        100        110        120 
LLQSELLLVC LKAWQVSSAV TALLPKLNPE CKILLLHNGM GTQEELPLNE HVFLHGVTTH 

       130        140        150        160        170        180 
AARRDGNTII HVASGMTHIG PTSSVIIDDN HLADTLHQAL PDVAWHNDIS AACWQKLAVN 

       190        200        210        220        230        240 
CVINPLTGLY NCRNGDVQRY PELIERLCAE VASVMEMEGY HTSTESLLSY VNNVIRSTAD 

       250        260        270        280        290        300 
NTSSLLQDLR SQRHTEIDYI TGYLLRRARS HGMALPENAR LYELIKRKES DYERIGAGLP 


GSW 

« Hide

References

[1]"Genome sequence of Yersinia pestis, the causative agent of plague."
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. expand/collapse author list , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:523-527(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CO-92 / Biovar Orientalis.
[2]"Genome sequence of Yersinia pestis KIM."
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. expand/collapse author list , Matson J.S., Blattner F.R., Perry R.D.
J. Bacteriol. 184:4601-4611(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KIM10+ / Biovar Mediaevalis.
[3]"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. expand/collapse author list , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL590842 Genomic DNA. Translation: CAL21766.1.
AE009952 Genomic DNA. Translation: AAM84595.1.
AE017042 Genomic DNA. Translation: AAS61025.1.
PIRAC0385.
RefSeqNP_668344.1. NC_004088.1.
NP_992148.1. NC_005810.1.
YP_002348076.1. NC_003143.1.

3D structure databases

ProteinModelPortalQ8ZC51.
SMRQ8ZC51. Positions 1-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8ZC51. 2 interactions.
STRING214092.YPO3171.

Protocols and materials databases

DNASU1145961.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM84595; AAM84595; y1014.
AAS61025; AAS61025; YP_0760.
GeneID1145961.
1175986.
2764026.
KEGGype:YPO3171.
ypk:y1014.
ypm:YP_0760.

Phylogenomic databases

eggNOGCOG1893.
HOGENOMHOG000050223.
KOK00077.
OMAWATRLAR.
OrthoDBEOG68SVW3.
ProtClustDBPRK06522.

Enzyme and pathway databases

BioCycYPES214092:GKDD-3124-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_YERPE
AccessionPrimary (citable) accession number: Q8ZC51
Secondary accession number(s): Q0WCB2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: February 21, 2002
Last modified: November 13, 2013
This is version 96 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