(data stored in ACNUC7421 zone)

SWISSPROT: 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   05-JUL-2017, entry version 109.
DE   RecName: Full=2-dehydropantoate 2-reductase;
DE            EC=1.1.1.169;
DE   AltName: Full=Ketopantoate reductase;
DE            Short=KPA reductase;
DE            Short=KPR;
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate
CC       into pantoic acid.
CC   -!- CATALYTIC ACTIVITY: (R)-pantoate + NADP(+) = 2-dehydropantoate +
CC       NADPH.
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000305}.
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_MWVM01000009.1.
DR   ProteinModelPortal; Q8XE72; -.
DR   SMR; Q8XE72; -.
DR   STRING; 155864.Z0528; -.
DR   EnsemblBacteria; AAG54775; AAG54775; Z0528.
DR   EnsemblBacteria; BAB33902; BAB33902; BAB33902.
DR   GeneID; 914581; -.
DR   KEGG; ece:Z0528; -.
DR   KEGG; ecs:ECs0479; -.
DR   PATRIC; fig|386585.9.peg.580; -.
DR   eggNOG; ENOG4108JZF; Bacteria.
DR   eggNOG; COG1893; LUCA.
DR   HOGENOM; HOG000050223; -.
DR   KO; K00077; -.
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:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR013328; 6PGD_dom_2.
DR   InterPro; IPR003710; ApbA.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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;
DR   PRODOM; Q8XE72.
DR   SWISS-2DPAGE; Q8XE72.
KW   Complete proteome; Cytoplasm; NADP; Oxidoreductase;
KW   Pantothenate biosynthesis.
FT   CHAIN         1    303       2-dehydropantoate 2-reductase.
FT                                /FTId=PRO_0000157302.
FT   NP_BIND       7     12       NADP. {ECO:0000250}.
FT   ACT_SITE    176    176       Proton donor.
FT   BINDING      31     31       NADP; via amide nitrogen. {ECO:0000250}.
FT   BINDING      98     98       NADP; via amide nitrogen. {ECO:0000250}.
FT   BINDING      98     98       Substrate. {ECO:0000250}.
FT   BINDING     122    122       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000250}.
FT   BINDING     180    180       Substrate. {ECO:0000250}.
FT   BINDING     184    184       Substrate. {ECO:0000250}.
FT   BINDING     194    194       Substrate. {ECO:0000250}.
FT   BINDING     241    241       Substrate. {ECO:0000250}.
FT   BINDING     244    244       Substrate. {ECO:0000250}.
FT   BINDING     256    256       NADP. {ECO:0000250}.
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
//

If you have problems or comments...

PBIL Back to PBIL home page