ID PANE_PYRHO Reviewed; 301 AA. AC O50098; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 136. 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 OrderedLocusNames=PH1390; ORFNames=PHAA019; OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC OS 100139 / OT-3). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=70601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3; RX PubMed=9679194; DOI=10.1093/dnares/5.2.55; RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T., RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.; RT "Complete sequence and gene organization of the genome of a hyper- RT thermophilic archaebacterium, Pyrococcus horikoshii OT3."; RL DNA Res. 5:55-76(1998). 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; BA000001; BAA30496.1; -; Genomic_DNA. DR PIR; H71011; H71011. DR RefSeq; WP_010885478.1; NC_000961.1. DR AlphaFoldDB; O50098; -. DR SMR; O50098; -. DR STRING; 70601.gene:9378366; -. DR EnsemblBacteria; BAA30496; BAA30496; BAA30496. DR GeneID; 1443716; -. DR KEGG; pho:PH1390; -. DR eggNOG; arCOG04139; Archaea. DR OrthoDB; 201845at2157; -. DR UniPathway; UPA00241; -. DR Proteomes; UP000000752; 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..301 FT /note="2-dehydropantoate 2-reductase" FT /id="PRO_0000157326" 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 301 AA; 32811 MW; E2354787F603880C CRC64; MKIYILGAGA IGSLVGGLLA NVGEDVTLIG RGRHIEAINK RGLMIEGLTN LKINTKATTS IPGAKPDLII LTTKSYSTDD ALNSAKDIVR DTWVLSLQNG IGNEEKIMEL GGRPIGGITT NGAVLKEPGV VEWRGRGITL IGLYPKGRNE FVEEVKETFN RAGLETEVTE NIIGWKWAKT IVNSAINPIG AILEVKNGAI KDNDYLLSIA VEVVKEGCKI ALQNGIKFDI SPMELLIQTL EQTRENYNSM LQDIWRGKRT EIDFINGKII EYAKLVNLEA PLNFLLWALV KAKESLGGGS K //