PANE_ECO57
ID PANE_ECO57 Reviewed; 303 AA.
AC Q8XE72;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=Z0528, ECs0479;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG54775.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33902.1; -; Genomic_DNA.
DR PIR; C85539; C85539.
DR PIR; G90688; G90688.
DR RefSeq; NP_308506.1; NC_002695.1.
DR RefSeq; WP_000705859.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XE72; -.
DR BMRB; Q8XE72; -.
DR SMR; Q8XE72; -.
DR STRING; 155864.EDL933_0495; -.
DR EnsemblBacteria; AAG54775; AAG54775; Z0528.
DR EnsemblBacteria; BAB33902; BAB33902; ECs_0479.
DR GeneID; 914581; -.
DR KEGG; ece:Z0528; -.
DR KEGG; ecs:ECs_0479; -.
DR PATRIC; fig|386585.9.peg.580; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_0_1_6; -.
DR OMA; NYSSMYQ; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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;
KW Reference proteome.
FT CHAIN 1..303
FT /note="2-dehydropantoate 2-reductase"
FT /id="PRO_0000157302"
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; 33848 MW; 13D127AEF0E30C64 CRC64;
MKITVLGCGA LGQLWLTALC KQGHEVQGWL RVPQPYCSVN LVETDGSIFN ESLTANDPDF
LATSDLLLVT LKAWQVSDAV KSLASTLPVT TPILLIHNGM GTIEELQNIQ QPLLMGTTTH
AACRDGNVII HVANGITHIG PARQQDGDYS YLADILQTVL PDVAWHNNIR AELWRKLAVN
CVINPLTAIW NCPNGELRHH PQEIMQICEE VAAVIEREGH HTSAEDLRDY VMQVIDATAE
NISSMLQDIR TLRHTEIDYI NGFLLRRARA HGIAVPENTR LFEMVKRKES EYERIGTGLP
RPW
