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Reviewed, UniProtKB/Swiss-Prot Q8P1F1 (PANE_STRP8)

Last modified February 9, 2010. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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 [Complete proteome] [HAMAP]
Taxonomic identifier301451 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

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 processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

pantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function2-dehydropantoate 2-reductase activity

Inferred from electronic annotation. Source: EC

NADP or NADPH 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
Q8P1F1-1 [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: 11917108] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS8232 / Serotype M18.

Cross-references

Sequence databases

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

3D structure databases

SMRQ8P1F1. Positions 1-304.
ModBaseSearch...

Genome annotation databases

GeneID994053.
GenomeReviewsGene locus spyM18_0911 in contig AE009949_GR.
KEGGspm:spyM18_0911.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG668370.
OMAIDSWQEH.

Enzyme and pathway databases

BioCycSPYO186103:SPYM18_0911-MONOMER.

Family and domain databases

InterProIPR008927. 6-PGluconate_DH_C-like.
IPR003710. ApbA.
IPR013752. ApbA_C.
IPR013332. ApbA_N.
IPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PANTHERPTHR21708:SF21. ApbA. 1 hit.
PfamPF02558. ApbA. 1 hit.
PF08546. ApbA_C. 1 hit.
[Graphical view]
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: February 9, 2010
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents