PANE_SALTY
ID PANE_SALTY Reviewed; 303 AA.
AC P37402;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=2-dehydropantoate 2-reductase;
DE EC=1.1.1.169 {ECO:0000269|PubMed:9488683};
DE AltName: Full=Ketopantoate reductase {ECO:0000303|PubMed:9488683};
DE Short=KPA reductase;
DE Short=KPR;
GN Name=panE {ECO:0000303|PubMed:9721324};
GN Synonyms=apbA {ECO:0000303|PubMed:7519593}; OrderedLocusNames=STM0434;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=7519593; DOI=10.1128/jb.176.16.4858-4864.1994;
RA Downs D.M., Petersen L.;
RT "apbA, a new genetic locus involved in thiamine biosynthesis in Salmonella
RT typhimurium.";
RL J. Bacteriol. 176:4858-4864(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=9488683; DOI=10.1074/jbc.273.10.5572;
RA Frodyma M.E., Downs D.M.;
RT "ApbA, the ketopantoate reductase enzyme of Salmonella typhimurium is
RT required for the synthesis of thiamine via the alternative pyrimidine
RT biosynthetic pathway.";
RL J. Biol. Chem. 273:5572-5576(1998).
RN [4]
RP SHOWS THAT APBA IS PANE.
RX PubMed=9721324; DOI=10.1128/jb.180.17.4757-4759.1998;
RA Frodyma M.E., Downs D.M.;
RT "The panE gene, encoding ketopantoate reductase, maps at 10 minutes and is
RT allelic to apbA in Salmonella typhimurium.";
RL J. Bacteriol. 180:4757-4759(1998).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. Has a strong preference for NADPH over NADH as the
CC electron acceptor. Pantoate, ketoisovalerate, oxaloacetate, pyruvate,
CC 3-hydroxypyruvate, alpha-ketoglutarate, alpha-ketobutyrate, and
CC acetaldehyde cannot serve as substrates for reduction.
CC {ECO:0000269|PubMed:9488683}.
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:0000269|PubMed:9488683};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.0776 mM for NADPH {ECO:0000269|PubMed:9488683};
CC KM=0.0742 mM for 2-dehydropantoate {ECO:0000269|PubMed:9488683};
CC Vmax=89.3 umol/min/mg enzyme {ECO:0000269|PubMed:9488683};
CC pH dependence:
CC Optimum pH is 6.25. {ECO:0000269|PubMed:9488683};
CC Temperature dependence:
CC Optimum temperature is 42 degrees Celsius.
CC {ECO:0000269|PubMed:9488683};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9488683}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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; U09529; AAA56681.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19388.1; -; Genomic_DNA.
DR PIR; A55849; A55849.
DR RefSeq; NP_459429.1; NC_003197.2.
DR RefSeq; WP_000705816.1; NC_003197.2.
DR AlphaFoldDB; P37402; -.
DR SMR; P37402; -.
DR STRING; 99287.STM0434; -.
DR PaxDb; P37402; -.
DR EnsemblBacteria; AAL19388; AAL19388; STM0434.
DR GeneID; 1251953; -.
DR KEGG; stm:STM0434; -.
DR PATRIC; fig|99287.12.peg.463; -.
DR HOGENOM; CLU_031468_0_1_6; -.
DR OMA; NYSSMYQ; -.
DR PhylomeDB; P37402; -.
DR BioCyc; SENT99287:STM0434-MON; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase;
KW Pantothenate biosynthesis; Reference proteome.
FT CHAIN 1..303
FT /note="2-dehydropantoate 2-reductase"
FT /id="PRO_0000157304"
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 VARIANT 121
FT /note="A -> T (in strain: DM4593)"
FT CONFLICT 74..86
FT /note="WQVSDAVRTLAST -> GFRRSTNPGVN (in Ref. 1; AAA56681)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="Missing (in Ref. 1; AAA56681)"
FT /evidence="ECO:0000305"
FT CONFLICT 246..247
FT /note="LQ -> FE (in Ref. 1; AAA56681)"
FT /evidence="ECO:0000305"
FT CONFLICT 275..303
FT /note="VPENSRLFEMVKRKESEYERSGTGMPRPW -> FRKIAACLKW (in Ref.
FT 1; AAA56681)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 303 AA; 33938 MW; 060DA21B75B891A4 CRC64;
MKITVLGCGA LGQLWLSALC KHGHDVQGWL RVPQPYCSVN LIDTDGSFFN ESLTANDPDF
LAKSELLLVT LKAWQVSDAV RTLASTLPVT SPILLIHNGM GTIEELQNIQ QPMLMGTITH
AARRDGNIII HVANGTTHIG PAREQDGDYS YLADILQGVL PDVAWHNNIR AEMWRKLAVN
CVINPLTALW NCPNGELRHH TDEINAICEE VAAVIEREGY HTSADDLRYY VEQVIDSTAE
NISSMLQDVR AMRHTEIDYI TGYLLKRARV HGLAVPENSR LFEMVKRKES EYERSGTGMP
RPW
