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Q929X1 (PANE_LISIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 82. 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:
Putative 2-dehydropantoate 2-reductase

EC=1.1.1.169
Alternative name(s):
Ketopantoate reductase
Short name=KPA reductase
Short name=KPR
Gene names
Ordered Locus Names:lin2152
OrganismListeria innocua serovar 6a (strain CLIP 11262) [Complete proteome] [HAMAP]
Taxonomic identifier272626 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length301 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

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
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 – 301301Putative 2-dehydropantoate 2-reductase
PRO_0000157314

Regions

Nucleotide binding11 – 166NADP By similarity

Sites

Active site1871Proton donor By similarity
Binding site1071NADP; via amide nitrogen By similarity
Binding site1071Substrate By similarity
Binding site1911Substrate By similarity
Binding site1951Substrate By similarity
Binding site2511Substrate By similarity
Binding site2631NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q929X1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 9C550E518C238E92

FASTA30133,684
        10         20         30         40         50         60 
MENQINVGII GAGAMGLLYA ANFADKSKLT LFTHRKEQAD LLNQKGISLI DNETTKNIHI 

        70         80         90        100        110        120 
HAAQITEEEQ LTKQQLLIIA VKQYSLNEII PILQKLPTKI PILFIQNGAG HLERLSELGT 

       130        140        150        160        170        180 
TRTILLGISE HGAGREDDTT VIWRGHGRTK YSIFQGELND DLKELLTSSP AFPIEKHANY 

       190        200        210        220        230        240 
QAIIQEKLFI NAVINPLTAV LGVQNGKLLE NQEWHRLLIR VVNEVETVLP IENALEKVET 

       250        260        270        280        290        300 
ICRTTALNFS SMALDCMNER MTEIDGIVLP ILEKGDKTET SLPTLRTLYQ IIKGLEGERH 


V 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL596171 Genomic DNA. Translation: CAC97382.1.
PIRAF1701.
RefSeqNP_471486.1. NC_003212.1.

3D structure databases

ProteinModelPortalQ929X1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272626.lin2152.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC97382; CAC97382; CAC97382.
GeneID1130881.
KEGGlin:lin2152.
PATRIC20301123. VBILisInn102668_2200.

Organism-specific databases

GenoListLIN2152.
CMRSearch...

Phylogenomic databases

eggNOGCOG1893.
HOGENOMHOG000050222.
KOK00077.
OMAKEWHELL.
OrthoDBEOG68SVW3.
ProtClustDBPRK06522.

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_LISIN
AccessionPrimary (citable) accession number: Q929X1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: December 1, 2001
Last modified: November 13, 2013
This is version 82 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