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O34661 (PANE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Probable 2-dehydropantoate 2-reductase

EC=1.1.1.169
Alternative name(s):
Ketopantoate reductase
Short name=KPA reductase
Gene names
Name:panE
Synonyms:apbA, ylbQ
Ordered Locus Names:BSU15110
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

(R)-pantoate + NADP+ = 2-dehydropantoate + NADPH.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the ketopantoate reductase family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpantothenate 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: 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 – 298298Probable 2-dehydropantoate 2-reductase
PRO_0000157311

Regions

Nucleotide binding7 – 126NADP By similarity

Sites

Active site1791Proton donor By similarity
Binding site981NADP; via amide nitrogen By similarity
Binding site981Substrate By similarity
Binding site1831Substrate By similarity
Binding site1871Substrate By similarity
Binding site2461Substrate By similarity
Binding site2581NADP By similarity

Secondary structure

..................................................... 298
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O34661 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: A0B645A0A415FFD5

FASTA29833,287
        10         20         30         40         50         60 
MKIGIIGGGS VGLLCAYYLS LYHDVTVVTR RQEQAAAIQS EGIRLYKGGE EFRADCSADT 

        70         80         90        100        110        120 
SINSDFDLLV VTVKQHQLQS VFSSLERIGK TNILFLQNGM GHIHDLKDWH VGHSIYVGIV 

       130        140        150        160        170        180 
EHGAVRKSDT AVDHTGLGAI KWSAFDDAEP DRLNILFQHN HSDFPIYYET DWYRLLTGKL 

       190        200        210        220        230        240 
IVNACINPLT ALLQVKNGEL LTTPAYLAFM KLVFQEACRI LKLENEEKAW ERVQAVCGQT 

       250        260        270        280        290 
KENRSSMLVD VIGGRQTEAD AIIGYLLKEA SLQGLDAVHL EFLYGSIKAL ERNTNKVF 

« Hide

References

« Hide 'large scale' references
[1]"Bacillus subtilis chromosomal region downstream nprE."
Bertero M., Presecan E., Glaser P., Richou A., Danchin A.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z98682 Genomic DNA. Translation: CAB11364.1.
AL009126 Genomic DNA. Translation: CAB13384.1.
PIRF69875.
RefSeqNP_389394.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EGOX-ray1.90A/B2-297[»]
ProteinModelPortalO34661.
SMRO34661. Positions 10-291.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU15110.

Proteomic databases

PaxDbO34661.

Protocols and materials databases

DNASU936782.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13384; CAB13384; BSU15110.
GeneID936782.
KEGGbsu:BSU15110.
PATRIC18974827. VBIBacSub10457_1605.

Organism-specific databases

GenoListBSU15110. [Micado]

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBSUB:BSU15110-MONOMER.

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...

Other

EvolutionaryTraceO34661.

Entry information

Entry namePANE_BACSU
AccessionPrimary (citable) accession number: O34661
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: November 13, 2013
This is version 103 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList