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Q8XE72 (PANE_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 87. 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:Z0528, ECs0479
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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_0000157302

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

Sequences

Sequence LengthMass (Da)Tools
Q8XE72 [UniParc].

Last modified February 21, 2002. Version 1.
Checksum: 13D127AEF0E30C64

FASTA30333,848
        10         20         30         40         50         60 
MKITVLGCGA LGQLWLTALC KQGHEVQGWL RVPQPYCSVN LVETDGSIFN ESLTANDPDF 

        70         80         90        100        110        120 
LATSDLLLVT LKAWQVSDAV KSLASTLPVT TPILLIHNGM GTIEELQNIQ QPLLMGTTTH 

       130        140        150        160        170        180 
AACRDGNVII HVANGITHIG PARQQDGDYS YLADILQTVL PDVAWHNNIR AELWRKLAVN 

       190        200        210        220        230        240 
CVINPLTAIW NCPNGELRHH PQEIMQICEE VAAVIEREGH HTSAEDLRDY VMQVIDATAE 

       250        260        270        280        290        300 
NISSMLQDIR TLRHTEIDYI NGFLLRRARA HGIAVPENTR LFEMVKRKES EYERIGTGLP 


RPW 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG54775.1.
BA000007 Genomic DNA. Translation: BAB33902.1.
PIRC85539.
G90688.
RefSeqNP_286167.1. NC_002655.2.
NP_308506.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8XE72.
SMRQ8XE72. Positions 1-292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z0528.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG54775; AAG54775; Z0528.
BAB33902; BAB33902; BAB33902.
GeneID914581.
957394.
KEGGece:Z0528.
ecs:ECs0479.
PATRIC18349919. VBIEscCol44059_0480.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1893.
HOGENOMHOG000050223.
KOK00077.
OMAIDDDRGE.
OrthoDBEOG68SVW3.
ProtClustDBPRK06522.

Enzyme and pathway databases

BioCycECOL386585:GJFA-473-MONOMER.
ECOO157:APBA-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_ECO57
AccessionPrimary (citable) accession number: Q8XE72
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: February 21, 2002
Last modified: December 11, 2013
This is version 87 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