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Protein

Probable 2-dehydropantoate 2-reductase

Gene

panE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei98 – 981NADP; via amide nitrogenBy similarity
Binding sitei98 – 981SubstrateBy similarity
Active sitei179 – 1791Proton donorBy similarity
Binding sitei183 – 1831SubstrateBy similarity
Binding sitei187 – 1871SubstrateBy similarity
Binding sitei246 – 2461SubstrateBy similarity
Binding sitei258 – 2581NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 126NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciBSUB:BSU15110-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 2-dehydropantoate 2-reductase (EC:1.1.1.169)
Alternative name(s):
Ketopantoate reductase
Short name:
KPA reductase
Gene namesi
Name:panE
Synonyms:apbA, ylbQ
Ordered Locus Names:BSU15110
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU15110. [Micado]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 298298Probable 2-dehydropantoate 2-reductasePRO_0000157311Add
BLAST

Proteomic databases

PaxDbiO34661.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU15110.

Structurei

Secondary structure

1
298
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi10 – 2011Combined sources
Beta strandi23 – 286Combined sources
Helixi32 – 4110Combined sources
Beta strandi43 – 475Combined sources
Beta strandi50 – 545Combined sources
Beta strandi57 – 615Combined sources
Beta strandi67 – 715Combined sources
Helixi75 – 773Combined sources
Helixi78 – 847Combined sources
Beta strandi92 – 954Combined sources
Beta strandi98 – 1003Combined sources
Helixi101 – 1077Combined sources
Beta strandi114 – 1207Combined sources
Beta strandi123 – 1264Combined sources
Beta strandi128 – 1369Combined sources
Beta strandi140 – 1445Combined sources
Helixi150 – 1534Combined sources
Turni154 – 1574Combined sources
Beta strandi166 – 1683Combined sources
Helixi172 – 19322Combined sources
Helixi199 – 2024Combined sources
Helixi204 – 22118Combined sources
Helixi226 – 23914Combined sources
Turni240 – 2423Combined sources
Helixi246 – 2538Combined sources
Helixi259 – 27214Combined sources
Helixi278 – 28912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EGOX-ray1.90A/B2-297[»]
ProteinModelPortaliO34661.
SMRiO34661. Positions 10-291.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34661.

Family & Domainsi

Sequence similaritiesi

Belongs to the ketopantoate reductase family.Curated

Phylogenomic databases

eggNOGiCOG1893.
HOGENOMiHOG000050222.
InParanoidiO34661.
KOiK00077.
OMAiFEKIFNC.
OrthoDBiEOG68SVW3.
PhylomeDBiO34661.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR003710. ApbA.
IPR013752. KPA_reductase.
IPR013332. KPR_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF02558. ApbA. 1 hit.
PF08546. ApbA_C. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR00745. apbA_panE. 1 hit.

Sequencei

Sequence statusi: Complete.

O34661-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIGIIGGGS VGLLCAYYLS LYHDVTVVTR RQEQAAAIQS EGIRLYKGGE
60 70 80 90 100
EFRADCSADT SINSDFDLLV VTVKQHQLQS VFSSLERIGK TNILFLQNGM
110 120 130 140 150
GHIHDLKDWH VGHSIYVGIV EHGAVRKSDT AVDHTGLGAI KWSAFDDAEP
160 170 180 190 200
DRLNILFQHN HSDFPIYYET DWYRLLTGKL IVNACINPLT ALLQVKNGEL
210 220 230 240 250
LTTPAYLAFM KLVFQEACRI LKLENEEKAW ERVQAVCGQT KENRSSMLVD
260 270 280 290
VIGGRQTEAD AIIGYLLKEA SLQGLDAVHL EFLYGSIKAL ERNTNKVF
Length:298
Mass (Da):33,287
Last modified:January 1, 1998 - v1
Checksum:iA0B645A0A415FFD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z98682 Genomic DNA. Translation: CAB11364.1.
AL009126 Genomic DNA. Translation: CAB13384.1.
PIRiF69875.
RefSeqiNP_389394.1. NC_000964.3.
WP_003232206.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13384; CAB13384; BSU15110.
GeneIDi936782.
KEGGibsu:BSU15110.
PATRICi18974827. VBIBacSub10457_1605.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z98682 Genomic DNA. Translation: CAB11364.1.
AL009126 Genomic DNA. Translation: CAB13384.1.
PIRiF69875.
RefSeqiNP_389394.1. NC_000964.3.
WP_003232206.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EGOX-ray1.90A/B2-297[»]
ProteinModelPortaliO34661.
SMRiO34661. Positions 10-291.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU15110.

Proteomic databases

PaxDbiO34661.

Protocols and materials databases

DNASUi936782.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13384; CAB13384; BSU15110.
GeneIDi936782.
KEGGibsu:BSU15110.
PATRICi18974827. VBIBacSub10457_1605.

Organism-specific databases

GenoListiBSU15110. [Micado]

Phylogenomic databases

eggNOGiCOG1893.
HOGENOMiHOG000050222.
InParanoidiO34661.
KOiK00077.
OMAiFEKIFNC.
OrthoDBiEOG68SVW3.
PhylomeDBiO34661.

Enzyme and pathway databases

BioCyciBSUB:BSU15110-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO34661.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR003710. ApbA.
IPR013752. KPA_reductase.
IPR013332. KPR_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF02558. ApbA. 1 hit.
PF08546. ApbA_C. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR00745. apbA_panE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPANE_BACSU
AccessioniPrimary (citable) accession number: O34661
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: May 27, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.