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Q9V0N0 (PANE_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Name:apbA
Ordered Locus Names:PYRAB07590
ORF Names:PAB0512
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus ›

Protein attributes

Sequence length300 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: EC

NADP binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 300300Putative 2-dehydropantoate 2-reductase
PRO_0000157325

Regions

Nucleotide binding7 – 126NADP By similarity

Sites

Active site1791Proton donor By similarity
Binding site991NADP; via amide nitrogen By similarity
Binding site991Substrate By similarity
Binding site1831Substrate By similarity
Binding site1871Substrate By similarity
Binding site2491Substrate By similarity
Binding site2611NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9V0N0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: F559625B73F691DC

FASTA30032,773
        10         20         30         40         50         60 
MKIYILGAGA IGSLFGGLLA NAGEDVLLIG RDPHVSAINE KGLKIVGIKD LNVKVEATTR 

        70         80         90        100        110        120 
VPEEKPDLIV LATKSYSTIE ALKSARHIVK GSWVLSIQNG IGNEDKIIEF GGKAIGGITT 

       130        140        150        160        170        180 
NGAMVEAPGV IKWTGKGVTI IGLYPQGKEK FIEKVADVFN SADIETHVSE NIISWIWAKA 

       190        200        210        220        230        240 
IVNSAINPIG TLLEVKNKVI RENDFLLSMA MEVVKEGCRV ALQNGIEFDV PPMDLFFQTL 

       250        260        270        280        290        300 
EQTRENYNSM LQDIWRGKKT EVDYINGKIV EYAKAVNLEA PMNLLLWGLI KGKEALEGKK

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ248285 Genomic DNA. Translation: CAB49673.1.
HE613800 Genomic DNA. Translation: CCE70155.1.
PIRH75119.
RefSeqNP_126442.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9V0N0.
ModBaseSearch...

Protein-protein interaction databases

STRING272844.PAB0512.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB49673; CAB49673; PAB0512.
GeneID1496099.
KEGGpab:PAB0512.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1893.
HOGENOMHOG000050222.
KOK00077.
OMANCAYNAI.
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. 6DGDH_C_like. 1 hit.
TIGRFAMsTIGR00745. apbA_panE. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANE_PYRAB
AccessionPrimary (citable) accession number: Q9V0N0
Secondary accession number(s): G8ZGW0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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