UniProtKB - Q5JGC2 (PANE_THEKO)
Protein
2-dehydropantoate 2-reductase
Gene
TK1968
Organism
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Status
Functioni
Catalyzes the NAD(P)H-dependent reduction of ketopantoate into pantoic acid. Prefers NADH rather than NADPH as the electron donor.1 Publication
Catalytic activityi
- This reaction proceeds in the backward1 Publication direction.
- EC:1.1.1.1691 PublicationThis reaction proceeds in the backward1 Publication direction.
Activity regulationi
Regulated by feedback inhibition by coenzyme A (CoA). CoA acts by competing with NAD(P)H (PubMed:23941541, PubMed:26757028). A disulfide bond is formed between CoA and Cys-84, which indicates an irreversible inhibition upon binding of CoA (PubMed:26757028).2 Publications
Kineticsi
kcat is 23.1 sec(-1) toward ketopantoate (in the presence of NADH). kcat is 19.7 sec(-1) toward NADH. kcat is 2.22 sec(-1) toward NADPH.1 Publication
- KM=6.03 µM for ketopantoate1 Publication
- KM=3.01 µM for NADH1 Publication
- KM=1.35 µM for NADPH1 Publication
- KM=130 µM for D-pantoate1 Publication
- KM=2040 µM for L-pantoate1 Publication
- KM=40.9 µM for NAD+1 Publication
- Vmax=40.7 µmol/min/mg enzyme toward ketopantoate (in the presence of NADH)1 Publication
- Vmax=34.7 µmol/min/mg enzyme toward NADH1 Publication
- Vmax=3.92 µmol/min/mg enzyme toward NADPH1 Publication
pH dependencei
Optimum pH is 6.4.1 Publication
Temperature dependencei
Optimum temperature is 90 degrees Celsius. Is extremely thermostable.1 Publication
: coenzyme A biosynthesis Pathwayi
This protein is involved in the pathway coenzyme A biosynthesis, which is part of Cofactor biosynthesis.1 PublicationView all proteins of this organism that are known to be involved in the pathway coenzyme A biosynthesis and in Cofactor biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 31 | Coenzyme A inhibitor1 Publication | 1 | |
Binding sitei | 31 | NAD(P)1 Publication | 1 | |
Binding sitei | 74 | Coenzyme A inhibitor1 Publication | 1 | |
Binding sitei | 74 | NAD(P)1 Publication | 1 | |
Binding sitei | 84 | Coenzyme A inhibitor1 Publication | 1 | |
Binding sitei | 100 | NAD(P)2 Publications | 1 | |
Binding sitei | 124 | NAD(P); via amide nitrogen and carbonyl oxygen2 Publications | 1 | |
Active sitei | 180 | Proton donorBy similarity | 1 | |
Binding sitei | 180 | Substrate1 Publication | 1 | |
Binding sitei | 184 | Substrate1 Publication | 1 | |
Binding sitei | 188 | Substrate1 Publication | 1 | |
Binding sitei | 198 | Substrate1 Publication | 1 | |
Binding sitei | 257 | Coenzyme A inhibitor1 Publication | 1 | |
Binding sitei | 262 | NAD(P)2 Publications | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 7 – 12 | NAD(P)2 Publications | 6 |
GO - Molecular functioni
- 2-dehydropantoate 2-reductase activity Source: CACAO
- nucleotide binding Source: UniProtKB-KW
GO - Biological processi
- coenzyme A biosynthetic process Source: UniProtKB-UniPathway
- pantothenate biosynthetic process Source: InterPro
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Coenzyme A biosynthesis |
Ligand | NAD, NADP, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | TKOD69014:G1G2A-1983-MONOMER |
UniPathwayi | UPA00241 |
Names & Taxonomyi
Protein namesi | Recommended name: 2-dehydropantoate 2-reductaseCurated (EC:1.1.1.1691 Publication)Alternative name(s): Ketopantoate reductase1 Publication Short name: KPR1 Publication |
Gene namesi | Ordered Locus Names:TK1968Imported |
Organismi | Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) |
Taxonomic identifieri | 69014 [NCBI] |
Taxonomic lineagei | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Thermococcus › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Other locations
- cytoplasm Source: GO_Central
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
Disruption of the gene results in a strain with growth defects that are complemented by addition of pantoate.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 60 | Y → A: Decreases efficiency of the inhibition by CoA. 1 Publication | 1 | |
Mutagenesisi | 84 | C → A: Decreases efficiency of the inhibition by CoA. Inhibition shows no time-dependency. 1 Publication | 1 | |
Mutagenesisi | 129 | W → A: Decreases efficiency of the inhibition by CoA. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000448239 | 1 – 309 | 2-dehydropantoate 2-reductaseAdd BLAST | 309 |
Interactioni
Subunit structurei
Homodimer.
3 PublicationsProtein-protein interaction databases
STRINGi | 69014.TK1968 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q5JGC2 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 8 – 10 | Coenzyme A inhibitor binding1 Publication | 3 | |
Regioni | 247 – 250 | Substrate binding1 Publication | 4 |
Domaini
Cooperative binding of CoA and ketopantoate induces a closed inhibited state by interacting with the N-terminal and C-terminal domains, and seems to facilitate the disulfide bond formation.1 Publication
Sequence similaritiesi
Belongs to the ketopantoate reductase family.Curated
Phylogenomic databases
eggNOGi | arCOG04139, Archaea |
HOGENOMi | CLU_031468_0_1_2 |
InParanoidi | Q5JGC2 |
OMAi | NGLGSQD |
OrthoDBi | 57213at2157 |
Family and domain databases
Gene3Di | 1.10.1040.10, 1 hit |
InterProi | View protein in InterPro IPR008927, 6-PGluconate_DH-like_C_sf IPR013328, 6PGD_dom2 IPR003710, ApbA IPR013752, KPA_reductase IPR013332, KPR_N IPR036291, NAD(P)-bd_dom_sf |
Pfami | View protein in Pfam PF02558, ApbA, 1 hit PF08546, ApbA_C, 1 hit |
SUPFAMi | SSF48179, SSF48179, 1 hit SSF51735, SSF51735, 1 hit |
TIGRFAMsi | TIGR00745, apbA_panE, 1 hit |
i Sequence
Sequence statusi: Complete.
Q5JGC2-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MRIYVLGAGS IGSLFGALLA RAGNDVTLIG RREQVDAINK NGLHVFGAEE
60 70 80 90 100
FTVKPKATIY APEEPPDLLI LAVKSYSTKT ALECARQCIG RNTWVLSIQN
110 120 130 140 150
GLGNEELALK YTPNVMGGVT TNGAMLVEWG KVLWAGKGIT VIGRYPTGRD
160 170 180 190 200
DFVDEVASVF NEAGIDTSVT ENAIGWKWAK AIVNSVINGL GTVLEVKNGH
210 220 230 240 250
LKDDPHLEGI SVDIAREGCM VAQQLGIEFE IHPLELLWDT IERTRENYNS
260 270 280 290 300
TLQDIWRGRE TEVDYIHGKI VEYARSVGME APRNELLWVL VKAKERINRG
KTRNISEGC
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AP006878 Genomic DNA Translation: BAD86157.1 |
RefSeqi | WP_011250918.1, NC_006624.1 |
Genome annotation databases
EnsemblBacteriai | BAD86157; BAD86157; TK1968 |
GeneIDi | 3234733 |
KEGGi | tko:TK1968 |
PATRICi | fig|69014.16.peg.1922 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AP006878 Genomic DNA Translation: BAD86157.1 |
RefSeqi | WP_011250918.1, NC_006624.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5AYV | X-ray | 1.65 | A/B | 1-309 | [»] | |
5HWS | X-ray | 2.30 | A/B/C/D | 1-309 | [»] | |
SMRi | Q5JGC2 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 69014.TK1968 |
Genome annotation databases
EnsemblBacteriai | BAD86157; BAD86157; TK1968 |
GeneIDi | 3234733 |
KEGGi | tko:TK1968 |
PATRICi | fig|69014.16.peg.1922 |
Phylogenomic databases
eggNOGi | arCOG04139, Archaea |
HOGENOMi | CLU_031468_0_1_2 |
InParanoidi | Q5JGC2 |
OMAi | NGLGSQD |
OrthoDBi | 57213at2157 |
Enzyme and pathway databases
UniPathwayi | UPA00241 |
BioCyci | TKOD69014:G1G2A-1983-MONOMER |
Family and domain databases
Gene3Di | 1.10.1040.10, 1 hit |
InterProi | View protein in InterPro IPR008927, 6-PGluconate_DH-like_C_sf IPR013328, 6PGD_dom2 IPR003710, ApbA IPR013752, KPA_reductase IPR013332, KPR_N IPR036291, NAD(P)-bd_dom_sf |
Pfami | View protein in Pfam PF02558, ApbA, 1 hit PF08546, ApbA_C, 1 hit |
SUPFAMi | SSF48179, SSF48179, 1 hit SSF51735, SSF51735, 1 hit |
TIGRFAMsi | TIGR00745, apbA_panE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PANE_THEKO | |
Accessioni | Q5JGC2Primary (citable) accession number: Q5JGC2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 16, 2019 |
Last sequence update: | February 15, 2005 | |
Last modified: | April 7, 2021 | |
This is version 112 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families