ID   PANE_PYRAE              Reviewed;         279 AA.
AC   Q8ZT70;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2002, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=PAE3409;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 /
RC   IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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}.
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DR   EMBL; AE009441; AAL64893.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZT70; -.
DR   SMR; Q8ZT70; -.
DR   STRING; 178306.PAE3409; -.
DR   EnsemblBacteria; AAL64893; AAL64893; PAE3409.
DR   KEGG; pai:PAE3409; -.
DR   PATRIC; fig|178306.9.peg.2562; -.
DR   eggNOG; arCOG04139; Archaea.
DR   HOGENOM; CLU_031468_0_0_2; -.
DR   InParanoid; Q8ZT70; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IBA:GO_Central.
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;
KW   Reference proteome.
FT   CHAIN           1..279
FT                   /note="2-dehydropantoate 2-reductase"
FT                   /id="PRO_0000157324"
FT   ACT_SITE        158
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         6..11
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT   BINDING         66
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT   BINDING         86
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT   BINDING         225..228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JGC2"
FT   BINDING         240
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JGC2"
SQ   SEQUENCE   279 AA;  29732 MW;  8A0A50DA29CD1328 CRC64;
     MLRVIGLGAV GSLFTYFLNR AGVVPEVVQR RRCGEFLFCV EGDCEKLKFR EGGAADDVGY
     TIVAVKAYDS RSVVPHLKGV AVVAQNGIGG YEEIKEAYPN SVPAVVTYGV YREGCRAELR
     GVGEIYLPSA VSTLAELLER GGGRVRLVED IEPYRWLKLA VNAAINAITA LLQAPNGVII
     SSPYAQTLAL EVAQEVLNVA TALGVKMPRN PVEEVLRVAS ATAKNLSSTA RDVAACAKTE
     IDYINGAVVK YGEALGVATP VNKALFNLIK ARESLCNSG
//