PANE_YERPE
ID PANE_YERPE Reviewed; 303 AA.
AC Q8ZC51; Q0WCB2;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
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=panE; Synonyms=apbA; OrderedLocusNames=YPO3171, y1014, YP_0760;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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; AL590842; CAL21766.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84595.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS61025.1; -; Genomic_DNA.
DR PIR; AC0385; AC0385.
DR RefSeq; WP_002208656.1; NZ_WUCM01000043.1.
DR RefSeq; YP_002348076.1; NC_003143.1.
DR AlphaFoldDB; Q8ZC51; -.
DR SMR; Q8ZC51; -.
DR IntAct; Q8ZC51; 2.
DR STRING; 214092.YPO3171; -.
DR PaxDb; Q8ZC51; -.
DR DNASU; 1145961; -.
DR EnsemblBacteria; AAM84595; AAM84595; y1014.
DR EnsemblBacteria; AAS61025; AAS61025; YP_0760.
DR GeneID; 66842627; -.
DR KEGG; ype:YPO3171; -.
DR KEGG; ypk:y1014; -.
DR KEGG; ypm:YP_0760; -.
DR PATRIC; fig|214092.21.peg.3627; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_0_1_6; -.
DR OMA; NYSSMYQ; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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..303
FT /note="2-dehydropantoate 2-reductase"
FT /id="PRO_0000157307"
FT ACT_SITE 176
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 98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 122
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT BINDING 256
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P0A9J4"
SQ SEQUENCE 303 AA; 33844 MW; 3B1D8198D053B9BE CRC64;
MKITVLGCGA LGQLWLSMLH QQDHDVQGWL RVPQPFCSVN VIMLNGESFN RNLTTNDPKH
LLQSELLLVC LKAWQVSSAV TALLPKLNPE CKILLLHNGM GTQEELPLNE HVFLHGVTTH
AARRDGNTII HVASGMTHIG PTSSVIIDDN HLADTLHQAL PDVAWHNDIS AACWQKLAVN
CVINPLTGLY NCRNGDVQRY PELIERLCAE VASVMEMEGY HTSTESLLSY VNNVIRSTAD
NTSSLLQDLR SQRHTEIDYI TGYLLRRARS HGMALPENAR LYELIKRKES DYERIGAGLP
GSW
