(data stored in ACNUC10821 zone)

SWISSPROT: C8U2A9_ECO10

ID   C8U2A9_ECO10            Unreviewed;       303 AA.
AC   C8U2A9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|RuleBase:RU362068};
DE            EC=1.1.1.169 {ECO:0000256|RuleBase:RU362068};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|RuleBase:RU362068};
GN   Name=panE {ECO:0000313|EMBL:BAI29267.1};
GN   OrderedLocusNames=ECO103_0399 {ECO:0000313|EMBL:BAI29267.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29267.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29267.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate
CC       into pantoic acid. {ECO:0000256|RuleBase:RU362068}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:16233, ChEBI:CHEBI:11561,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.169;
CC         Evidence={ECO:0000256|RuleBase:RU362068};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000256|RuleBase:RU362068}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|RuleBase:RU362068}.
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DR   EMBL; AP010958; BAI29267.1; -; Genomic_DNA.
DR   RefSeq; WP_000705874.1; NC_013353.1.
DR   EnsemblBacteria; BAI29267; BAI29267; ECO103_0399.
DR   KEGG; eoh:ECO103_0399; -.
DR   HOGENOM; HOG000050223; -.
DR   KO; K00077; -.
DR   OMA; NGLGSQD; -.
DR   BioCyc; ECOL585395:ECO103_RS02090-MONOMER; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000000959; Chromosome.
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;
DR   PRODOM; C8U2A9.
DR   SWISS-2DPAGE; C8U2A9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   NADP {ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068}.
FT   DOMAIN        3    143       ApbA. {ECO:0000259|Pfam:PF02558}.
FT   DOMAIN      168    289       ApbA_C. {ECO:0000259|Pfam:PF08546}.
SQ   SEQUENCE   303 AA;  33947 MW;  5183EB352E54E187 CRC64;
     MKITVLGCGA LGQLWLTALC KQGHEVQGWL RVPQPYCSVN LVETDGSIFN ESLTANDPDF
     LATSDLLLVT LKAWQVYDAV KSLASTLPVT TPILLIHNGM GTIEELQNIQ QPLLMGTTTH
     AARRDGNVII HVANGITHIG PARQQDGDYS YLADILQTVL PDVAWHNNIR AELWRKLAVN
     CVINPLTAIW NCPNGELRHH PQEIMQICEE VAAVIEREGH HTSAEDLRDY VMQVIDATAE
     NISSMLQDIR ALRHTEIDYI NGFLLRRARA HGIAVPENTR LFEMVKRKES EYERIGTGLP
     RPW
//

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