ID   PANE_AQUAE              Reviewed;         310 AA.
AC   O67619;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000250|UniProtKB:P0A9J4};
DE            EC=1.1.1.169 {ECO:0000250|UniProtKB:P0A9J4};
DE   AltName: Full=Ketopantoate reductase {ECO:0000250|UniProtKB:P0A9J4};
DE            Short=KPR {ECO:0000250|UniProtKB:P0A9J4};
GN   OrderedLocusNames=aq_1727;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC       pantoic acid. {ECO:0000250|UniProtKB:P0A9J4}.
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:P0A9J4};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000250|UniProtKB:P0A9J4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J4}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000657; AAC07585.1; -; Genomic_DNA.
DR   PIR; A70449; A70449.
DR   RefSeq; NP_214185.1; NC_000918.1.
DR   RefSeq; WP_010881122.1; NC_000918.1.
DR   AlphaFoldDB; O67619; -.
DR   SMR; O67619; -.
DR   STRING; 224324.aq_1727; -.
DR   EnsemblBacteria; AAC07585; AAC07585; aq_1727.
DR   KEGG; aae:aq_1727; -.
DR   PATRIC; fig|224324.8.peg.1327; -.
DR   eggNOG; COG1893; Bacteria.
DR   HOGENOM; CLU_031468_0_0_0; -.
DR   InParanoid; O67619; -.
DR   OMA; NYSSMYQ; -.
DR   OrthoDB; 427052at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000000798; 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:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1040.10; -; 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   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00745; apbA_panE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NADP; Oxidoreductase; Pantothenate biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..310
FT                   /note="2-dehydropantoate 2-reductase"
FT                   /id="PRO_0000157310"
FT   ACT_SITE        184
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         9..14
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         100
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         270
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
SQ   SEQUENCE   310 AA;  34776 MW;  E59FB12901C0ABE0 CRC64;
     MVMKFLIVGV GAIGSAYLAF LTRAGHEAAG LVRRNPVNRI KVEGIWGEFE IPVKTFTKVE
     EVPFIPDIVI ISVKSYDTEE ALKKVKPVVG ENTFIMIAQN GYGNYEKAVE IYGEGKVILS
     RIIFGSKVIK PGHIRITVSA DEVVIGDPSG KIDEEFLKNL ARTFTEAGIP TRYERDVYKY
     LVDKIIYNSA LNPLGALFEV NYGSLAENPH TKELMNRVID EIFQVIEKAK LPCFWKSADE
     YKKVFYEKLI PPTAEHYPSM LEDVKKGKTE IEALNGAIVE LGKKYGVSTP TNEFITKMVK
     AKELFNLKDT