ID PANE_PYRAB Reviewed; 300 AA. AC Q9V0N0; G8ZGW0; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 135. DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000250|UniProtKB:Q5JGC2}; DE EC=1.1.1.169 {ECO:0000250|UniProtKB:Q5JGC2}; DE AltName: Full=Ketopantoate reductase {ECO:0000250|UniProtKB:Q5JGC2}; DE Short=KPR {ECO:0000250|UniProtKB:Q5JGC2}; GN Name=apbA; OrderedLocusNames=PYRAB07590; ORFNames=PAB0512; OS Pyrococcus abyssi (strain GE5 / Orsay). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=272844; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GE5 / Orsay; RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x; RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., RA Weissenbach J., Zivanovic Y., Forterre P.; RT "An integrated analysis of the genome of the hyperthermophilic archaeon RT Pyrococcus abyssi."; RL Mol. Microbiol. 47:1495-1512(2003). RN [2] RP GENOME REANNOTATION. RC STRAIN=GE5 / Orsay; RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x; RA Gao J., Wang J.; RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and RT Pyrococcus furiosus DSM 3638."; RL Curr. Microbiol. 64:118-129(2012). CC -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of ketopantoate CC into pantoic acid. {ECO:0000250|UniProtKB:Q5JGC2}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-pantoate + NAD(+) = 2-dehydropantoate + H(+) + NADH; CC Xref=Rhea:RHEA:61292, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15980, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; CC Evidence={ECO:0000250|UniProtKB:Q5JGC2}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:61294; CC Evidence={ECO:0000250|UniProtKB:Q5JGC2}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH; CC Xref=Rhea:RHEA:16233, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15980, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC EC=1.1.1.169; Evidence={ECO:0000250|UniProtKB:Q5JGC2}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16235; CC Evidence={ECO:0000250|UniProtKB:Q5JGC2}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis. CC {ECO:0000250|UniProtKB:Q5JGC2}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5JGC2}. CC -!- SIMILARITY: Belongs to the ketopantoate reductase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ248285; CAB49673.1; -; Genomic_DNA. DR EMBL; HE613800; CCE70155.1; -; Genomic_DNA. DR PIR; H75119; H75119. DR RefSeq; WP_010867881.1; NC_000868.1. DR AlphaFoldDB; Q9V0N0; -. DR SMR; Q9V0N0; -. DR STRING; 272844.PAB0512; -. DR GeneID; 1496099; -. DR KEGG; pab:PAB0512; -. DR PATRIC; fig|272844.11.peg.799; -. DR eggNOG; arCOG04139; Archaea. DR HOGENOM; CLU_031468_6_1_2; -. DR OrthoDB; 201845at2157; -. DR PhylomeDB; Q9V0N0; -. DR UniPathway; UPA00241; -. DR Proteomes; UP000000810; Chromosome. DR Proteomes; UP000009139; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR013328; 6PGD_dom2. DR InterPro; IPR003710; ApbA. DR InterPro; IPR013752; KPA_reductase. DR InterPro; IPR013332; KPR_N. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR00745; apbA_panE; 1. DR PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1. DR PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1. DR Pfam; PF02558; ApbA; 1. DR Pfam; PF08546; ApbA_C; 1. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 3: Inferred from homology; KW Coenzyme A biosynthesis; Cytoplasm; NAD; NADP; Oxidoreductase. FT CHAIN 1..300 FT /note="2-dehydropantoate 2-reductase" FT /id="PRO_0000157325" FT ACT_SITE 179 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P0A9J4" FT BINDING 7..12 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q5JGC2" FT BINDING 74 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q5JGC2" FT BINDING 99 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q5JGC2" FT BINDING 123 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q5JGC2" FT BINDING 179 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q5JGC2" FT BINDING 183 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q5JGC2" FT BINDING 187 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q5JGC2" FT BINDING 197 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q5JGC2" FT BINDING 246..249 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q5JGC2" FT BINDING 261 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:Q5JGC2" SQ SEQUENCE 300 AA; 32773 MW; F559625B73F691DC CRC64; MKIYILGAGA IGSLFGGLLA NAGEDVLLIG RDPHVSAINE KGLKIVGIKD LNVKVEATTR VPEEKPDLIV LATKSYSTIE ALKSARHIVK GSWVLSIQNG IGNEDKIIEF GGKAIGGITT NGAMVEAPGV IKWTGKGVTI IGLYPQGKEK FIEKVADVFN SADIETHVSE NIISWIWAKA IVNSAINPIG TLLEVKNKVI RENDFLLSMA MEVVKEGCRV ALQNGIEFDV PPMDLFFQTL EQTRENYNSM LQDIWRGKKT EVDYINGKIV EYAKAVNLEA PMNLLLWGLI KGKEALEGKK //