ID   PANE_STRP1              Reviewed;         307 AA.
AC   P65666; Q48ZE1; Q9A0B3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 139.
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   Name=apbA; OrderedLocusNames=SPy_0852, M5005_Spy0659;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(2005).
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; AE004092; AAK33780.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ51277.1; -; Genomic_DNA.
DR   RefSeq; NP_269059.1; NC_002737.2.
DR   AlphaFoldDB; P65666; -.
DR   SMR; P65666; -.
DR   PaxDb; 1314-HKU360_00672; -.
DR   KEGG; spy:SPy_0852; -.
DR   KEGG; spz:M5005_Spy0659; -.
DR   PATRIC; fig|160490.10.peg.729; -.
DR   HOGENOM; CLU_031468_0_0_9; -.
DR   OMA; ANYSSMY; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000000750; 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; 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   Cytoplasm; NADP; Oxidoreductase; Pantothenate biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..307
FT                   /note="2-dehydropantoate 2-reductase"
FT                   /id="PRO_0000157318"
FT   ACT_SITE        184
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:P0A9J4"
FT   BINDING         102
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         128
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
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         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         268
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
SQ   SEQUENCE   307 AA;  33829 MW;  46F6298D3BD958E6 CRC64;
     MLVYIAGSGA MGCRFGYQIS KTNNDVILLD NWEDHINAIK ENGLVVTGDV EETVKLPIMK
     PTEATQEADL IILFTKAMQL PQMLQDIKGI IGKETKVLCL LNGLGHEDVI RQYIPEHNIL
     MGVTVWTAGL EGPGRAHLQG VGALNLQSMD PSNQEAGHQV ADLLNEANLN ATYDENVVPN
     IWRKACVNGT MNSTCALLDC TIGELFASED GLKMVKEIIH EFVIVGQAEG VELNEEEITQ
     YVMDTSVKAA HHYPSMHQDL VQNHRLTEID FINGAVNTKG EKLGINTPYC RMITELVHAK
     EAVLNIQ
//