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Q8YX96 (PANE_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 81. 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:all1319
OrganismNostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length319 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 – 319319Putative 2-dehydropantoate 2-reductase
PRO_0000157309

Regions

Nucleotide binding10 – 156NADP By similarity

Sites

Active site1921Proton donor By similarity
Binding site1051NADP; via amide nitrogen By similarity
Binding site1051Substrate By similarity
Binding site1961Substrate By similarity
Binding site2001Substrate By similarity
Binding site2621Substrate By similarity
Binding site2741NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YX96 [UniParc].

Last modified February 21, 2002. Version 1.
Checksum: 7A53C6138C39A483

FASTA31935,574
        10         20         30         40         50         60 
MNERKYAILG TGALGGYYGA KLQKAGSDVH FLLKSDYEKV NQDGLLVESK DGDFTLPQVN 

        70         80         90        100        110        120 
AYNDVAKMPK CDVVVVALKT TQNHLLPKLL PPIVKNDGIV LVLQNGLGVE EEIAEILPQV 

       130        140        150        160        170        180 
HIIGGLCFLC SNKVGAGYIH HLDYGQITLG EYAHGYSNMG ITDRMQQISH DFQTAGISIE 

       190        200        210        220        230        240 
LLEDLLLGRW KKLVWNIPYN GLSVVLNART DELMADTYTR TLVEQLMYEV KAGAKSMGRN 

       250        260        270        280        290        300 
IPDSFIQTML DYTVKMKPYR TSMKIDYDEC RPLEVEAIVG NPLHKAQEVG VNLPQINCLY 

       310 
HQLKFLDGRN RTGQLTVDS 

« Hide

References

[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7120 / UTEX 2576.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000019 Genomic DNA. Translation: BAB73276.1.
PIRAD1971.
RefSeqNP_485362.1. NC_003272.1.

3D structure databases

ProteinModelPortalQ8YX96.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING103690.all1319.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB73276; BAB73276; BAB73276.
GeneID1104914.
KEGGana:all1319.
PATRIC22772598. VBINosSp37423_1783.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1893.
HOGENOMHOG000050222.
KOK00077.
OMADMPPCDW.
OrthoDBEOG693GMJ.
ProtClustDBPRK06249.

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_NOSS1
AccessionPrimary (citable) accession number: Q8YX96
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: February 21, 2002
Last modified: November 13, 2013
This is version 81 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