(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 139.
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;
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}.
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   SMR; P37402; -.
DR   PaxDb; P37402; -.
DR   PRIDE; P37402; -.
DR   EnsemblBacteria; AAL19388; AAL19388; STM0434.
DR   GeneID; 1251953; -.
DR   KEGG; stm:STM0434; -.
DR   PATRIC; fig|99287.12.peg.463; -.
DR   eggNOG; ENOG4108JZF; Bacteria.
DR   eggNOG; COG1893; LUCA.
DR   HOGENOM; HOG000050223; -.
DR   KO; K00077; -.
DR   OMA; NGLGSQD; -.
DR   PhylomeDB; P37402; -.
DR   BioCyc; SENT99287:STM0434-MONOMER; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0033317; P:pantothenate biosynthetic process from valine; IBA:GO_Central.
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;
DR   PRODOM; P37402.
DR   SWISS-2DPAGE; P37402.
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   NP_BIND         7..12
FT                   /note="NADP"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   ACT_SITE        176
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         98
FT                   /note="NADP; via amide nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         98
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         122
FT                   /note="NADP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         180
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         184
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         194
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         244
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         256
FT                   /note="NADP"
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
//

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