PANE_SALTI
ID PANE_SALTI Reviewed; 303 AA.
AC Q8Z8W3;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=STY0473, t2430;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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 -!- SUBUNIT: Monomer. {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; AL513382; CAD08890.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70019.1; -; Genomic_DNA.
DR RefSeq; NP_455028.1; NC_003198.1.
DR RefSeq; WP_000705818.1; NZ_QXGZ01000026.1.
DR AlphaFoldDB; Q8Z8W3; -.
DR SMR; Q8Z8W3; -.
DR STRING; 220341.16501702; -.
DR EnsemblBacteria; AAO70019; AAO70019; t2430.
DR KEGG; stt:t2430; -.
DR KEGG; sty:STY0473; -.
DR PATRIC; fig|220341.7.peg.474; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_0_1_6; -.
DR OMA; NYSSMYQ; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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.
FT CHAIN 1..303
FT /note="2-dehydropantoate 2-reductase"
FT /id="PRO_0000157303"
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"
FT CONFLICT 117
FT /note="A -> T (in Ref. 2; AAO70019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 303 AA; 33842 MW; 0369C148A42BF583 CRC64;
MKITVLGCGA LGQLWLSALC KHGHDVQGWL RVPQPYCSVN LIDTDGSFFN ESLTANDPDF
LAKSELLLVT LKAWQVSDAV RTLASTLPVT SPILLIHNGM GTIEELQSIQ QPMLMGAITH
AARRDGNIII HVANGTTHIG PAREQDGDYS YLAEILQGVL PDVAWHNNIR AEMWRKLAVN
CVINPLTALW NCPNGELRHH TDEINAICEE VAAVIEREGY HTSADDLCYY VEQVIDSTAE
NISSMLQDVR AMRHTEIDYI TGYLLKRARV HGLAVPENSR LFEMVKRKES EYERSGTGMP
RPW
