ID   PANE_NOSS1              Reviewed;         319 AA.
AC   Q8YX96;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2002, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=all1319;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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}.
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; BA000019; BAB73276.1; -; Genomic_DNA.
DR   PIR; AD1971; AD1971.
DR   RefSeq; WP_010995491.1; NZ_RSCN01000060.1.
DR   AlphaFoldDB; Q8YX96; -.
DR   SMR; Q8YX96; -.
DR   STRING; 103690.17130666; -.
DR   EnsemblBacteria; BAB73276; BAB73276; BAB73276.
DR   KEGG; ana:all1319; -.
DR   eggNOG; COG1893; Bacteria.
DR   OMA; WEKWVFL; -.
DR   OrthoDB; 427052at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000002483; 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: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..319
FT                   /note="2-dehydropantoate 2-reductase"
FT                   /id="PRO_0000157309"
FT   ACT_SITE        192
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         10..15
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         105
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         274
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
SQ   SEQUENCE   319 AA;  35574 MW;  7A53C6138C39A483 CRC64;
     MNERKYAILG TGALGGYYGA KLQKAGSDVH FLLKSDYEKV NQDGLLVESK DGDFTLPQVN
     AYNDVAKMPK CDVVVVALKT TQNHLLPKLL PPIVKNDGIV LVLQNGLGVE EEIAEILPQV
     HIIGGLCFLC SNKVGAGYIH HLDYGQITLG EYAHGYSNMG ITDRMQQISH DFQTAGISIE
     LLEDLLLGRW KKLVWNIPYN GLSVVLNART DELMADTYTR TLVEQLMYEV KAGAKSMGRN
     IPDSFIQTML DYTVKMKPYR TSMKIDYDEC RPLEVEAIVG NPLHKAQEVG VNLPQINCLY
     HQLKFLDGRN RTGQLTVDS