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 15-JUN-2010, entry version 48. DE RecName: Full=Putative 2-dehydropantoate 2-reductase; DE EC=1.1.1.169; DE AltName: Full=Ketopantoate reductase; DE Short=KPA reductase; DE Short=KPR; GN Name=apbA; OrderedLocusNames=SPy_0852, M5005_Spy0659; OS Streptococcus pyogenes serotype M1. OC Bacteria; Firmicutes; 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 MEDLINE=21192684; 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., RA Yuan X., 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., RA Hoe N.P., Musser J.M.; RT "Evolutionary origin and emergence of a highly successful clone of RT serotype M1 group A Streptococcus involved multiple horizontal gene RT transfer events."; RL J. Infect. Dis. 192:771-782(2005). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate CC into pantoic acid (By similarity). CC -!- CATALYTIC ACTIVITY: (R)-pantoate + NADP(+) = 2-dehydropantoate + CC NADPH. CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; CC (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- SIMILARITY: Belongs to the ketopantoate reductase family. 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; AE004092; AAK33780.1; -; Genomic_DNA. DR EMBL; CP000017; AAZ51277.1; -; Genomic_DNA. DR RefSeq; NP_269059.1; -. DR RefSeq; YP_282022.1; -. DR SMR; P65666; 1-304. DR EnsemblBacteria; EBSTRT00000000038; EBSTRP00000000038; EBSTRG00000000038. DR EnsemblBacteria; EBSTRT00000028707; EBSTRP00000027725; EBSTRG00000028707. DR GeneID; 3572249; -. DR GeneID; 901016; -. DR GenomeReviews; AE004092_GR; SPy_0852. DR GenomeReviews; CP000017_GR; M5005_Spy0659. DR KEGG; spy:SPy_0852; -. DR KEGG; spz:M5005_Spy_0659; -. DR HOGENOM; HBG668370; -. DR OMA; IDSWQEH; -. DR ProtClustDB; PRK06522; -. DR BioCyc; SPYO160490:SPY0852-MONOMER; -. DR BioCyc; SPYO293653:M5005_SPY0659-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:EC. DR GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR003710; ApbA. DR InterPro; IPR013752; ApbA_C. DR InterPro; IPR013332; ApbA_N. DR InterPro; IPR013328; DH_multihelical. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Gene3D; G3DSA:1.10.1040.10; Opine_DH; 1. DR PANTHER; PTHR21708:SF21; ApbA; 1. DR Pfam; PF02558; ApbA; 1. DR Pfam; PF08546; ApbA_C; 1. DR SUPFAM; SSF48179; 6DGDH_C_like; 1. DR SUPFAM; SSF51735; NAD(P)-bd; 1. DR TIGRFAMs; TIGR00745; apbA_panE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; NADP; Oxidoreductase; KW Pantothenate biosynthesis. FT CHAIN 1 307 Putative 2-dehydropantoate 2-reductase. FT /FTId=PRO_0000157318. FT NP_BIND 7 12 NADP (By similarity). FT ACT_SITE 184 184 Proton donor (By similarity). FT BINDING 102 102 NADP; via amide nitrogen (By similarity). FT BINDING 102 102 Substrate (By similarity). FT BINDING 188 188 Substrate (By similarity). FT BINDING 192 192 Substrate (By similarity). FT BINDING 255 255 Substrate (By similarity). FT BINDING 268 268 NADP (By similarity). 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 //