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Q8P1F1 (PANE_STRP8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. 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
Name:apbA
Ordered Locus Names:spyM18_0911
OrganismStreptococcus pyogenes serotype M18 (strain MGAS8232) [Complete proteome] [HAMAP]
Taxonomic identifier186103 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length307 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 – 307307Putative 2-dehydropantoate 2-reductase
PRO_0000157321

Regions

Nucleotide binding7 – 126NADP By similarity

Sites

Active site1841Proton donor By similarity
Binding site1021NADP; via amide nitrogen By similarity
Binding site1021Substrate By similarity
Binding site1881Substrate By similarity
Binding site1921Substrate By similarity
Binding site2551Substrate By similarity
Binding site2681NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8P1F1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: AC4DCD25E5A1CE96

FASTA30733,841
        10         20         30         40         50         60 
MLVYIAGSGA MGCRFGYQIS KTNNDVILLD NWEDHINAIK ENGLVVTGDV EETVKLPIMK 

        70         80         90        100        110        120 
PTEATQEADL IILFTKAMQL PQMLQDIKGI IGKETKVLCL LNGLGHEDVI RQYIPEHNIL 

       130        140        150        160        170        180 
MGVTVWTAGL EGPGRAHLQG VGALNLQSMD PNNQDAGHQV ADLLNKANLN ATYDENVVPN 

       190        200        210        220        230        240 
IWRKACVNGT MNSTCALLDC TIGELFASED GLKMVKEIIH EFVIVGQAEG VELNEEEITQ 

       250        260        270        280        290        300 
YVMDTSVKAA HHYPSMHQDL VQNHRLTEID FINGAVNTKG EKLGINTPYC RMITELVHAK 


EAVLNIQ 

« Hide

References

[1]"Genome sequence and comparative microarray analysis of serotype M18 group A Streptococcus strains associated with acute rheumatic fever outbreaks."
Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S., Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A., Veasy L.G., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS8232.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009949 Genomic DNA. Translation: AAL97561.1.
RefSeqNP_607062.1. NC_003485.1.

3D structure databases

ProteinModelPortalQ8P1F1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186103.spyM18_0911.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL97561; AAL97561; spyM18_0911.
GeneID994053.
KEGGspm:spyM18_0911.
PATRIC19748427. VBIStrPyo4396_0803.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1893.
HOGENOMHOG000050222.
KOK00077.
OMAMGLEPML.
OrthoDBEOG6P5ZHG.

Enzyme and pathway databases

BioCycSPYO186103:GHJG-781-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_STRP8
AccessionPrimary (citable) accession number: Q8P1F1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: October 1, 2002
Last modified: May 14, 2014
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