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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)DescriptionActionsGraphical viewLength
Binding sitei98NADP; via amide nitrogenBy similarity1
Binding sitei98SubstrateBy similarity1
Active sitei179Proton donorBy similarity1
Binding sitei183SubstrateBy similarity1
Binding sitei187SubstrateBy similarity1
Binding sitei246SubstrateBy similarity1
Binding sitei258NADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi7 – 12NADPBy similarity6

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
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001573111 – 298Probable 2-dehydropantoate 2-reductaseAdd BLAST298

Proteomic databases

PaxDbiO34661.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100008356.

Structurei

Secondary structure

1298
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi10 – 20Combined sources11
Beta strandi23 – 28Combined sources6
Helixi32 – 41Combined sources10
Beta strandi43 – 47Combined sources5
Beta strandi50 – 54Combined sources5
Beta strandi57 – 61Combined sources5
Beta strandi67 – 71Combined sources5
Helixi75 – 77Combined sources3
Helixi78 – 84Combined sources7
Beta strandi92 – 95Combined sources4
Beta strandi98 – 100Combined sources3
Helixi101 – 107Combined sources7
Beta strandi114 – 120Combined sources7
Beta strandi123 – 126Combined sources4
Beta strandi128 – 136Combined sources9
Beta strandi140 – 144Combined sources5
Helixi150 – 153Combined sources4
Turni154 – 157Combined sources4
Beta strandi166 – 168Combined sources3
Helixi172 – 193Combined sources22
Helixi199 – 202Combined sources4
Helixi204 – 221Combined sources18
Helixi226 – 239Combined sources14
Turni240 – 242Combined sources3
Helixi246 – 253Combined sources8
Helixi259 – 272Combined sources14
Helixi278 – 289Combined sources12

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO34661.

Family & Domainsi

Sequence similaritiesi

Belongs to the ketopantoate reductase family.Curated

Phylogenomic databases

eggNOGiCOG1893. LUCA.
HOGENOMiHOG000050222.
InParanoidiO34661.
KOiK00077.
OMAiCGAIGKL.
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.
SSF51735. SSF51735. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EGOX-ray1.90A/B2-297[»]
ProteinModelPortaliO34661.
SMRiO34661.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100008356.

Proteomic databases

PaxDbiO34661.

Protocols and materials databases

DNASUi936782.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG1893. LUCA.
HOGENOMiHOG000050222.
InParanoidiO34661.
KOiK00077.
OMAiCGAIGKL.
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.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00745. apbA_panE. 1 hit.
ProtoNetiSearch...

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: November 30, 2016
This is version 122 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

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 one 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.