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Database: UniProt
Entry: A0A090V0Z3_PSEVU
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ID   A0A090V0Z3_PSEVU        Unreviewed;       303 AA.
AC   A0A090V0Z3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   18-JUN-2025, entry version 39.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465, ECO:0000256|RuleBase:RU362068};
DE            EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014, ECO:0000256|RuleBase:RU362068};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024, ECO:0000256|RuleBase:RU362068};
GN   Name=panE {ECO:0000313|EMBL:GAL58545.1};
GN   ORFNames=EV102420_12_00510 {ECO:0000313|EMBL:GAL58545.1};
OS   Pseudescherichia vulneris NBRC 102420.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Pseudescherichia.
OX   NCBI_TaxID=1115515 {ECO:0000313|EMBL:GAL58545.1, ECO:0000313|Proteomes:UP000029462};
RN   [1] {ECO:0000313|EMBL:GAL58545.1, ECO:0000313|Proteomes:UP000029462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102420 {ECO:0000313|EMBL:GAL58545.1,
RC   ECO:0000313|Proteomes:UP000029462};
RA   Yoshida Y., Hosoyama A., Tsuchikane K., Ohji S., Ichikawa N., Kimura A.,
RA   Yamazoe A., Ezaki T., Fujita N.;
RT   "Whole genome shotgun sequence of Escherichia vulneris NBRC 102420.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC       pantoic acid. {ECO:0000256|RuleBase:RU362068}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH + H(+);
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:0000256|ARBA:ARBA00048793,
CC         ECO:0000256|RuleBase:RU362068};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004994, ECO:0000256|RuleBase:RU362068}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAL58545.1}.
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DR   EMBL; BBMZ01000012; GAL58545.1; -; Genomic_DNA.
DR   RefSeq; WP_042391588.1; NZ_BBMZ01000012.1.
DR   AlphaFoldDB; A0A090V0Z3; -.
DR   STRING; 1115515.EV102420_12_00510; -.
DR   eggNOG; COG1893; Bacteria.
DR   OrthoDB; 6530772at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000029462; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   FunFam; 1.10.1040.10:FF:000014; 2-dehydropantoate 2-reductase; 1.
DR   FunFam; 3.40.50.720:FF:000162; 2-dehydropantoate 2-reductase; 1.
DR   Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR003710; ApbA.
DR   InterPro; IPR050838; Ketopantoate_reductase.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00745; apbA_panE; 1.
DR   NCBIfam; NF005087; PRK06522.1-1; 1.
DR   PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW   ECO:0000256|RuleBase:RU362068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029462}.
FT   DOMAIN          3..143
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          169..289
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   303 AA;  33820 MW;  7AAEC8CC50E366B4 CRC64;
     MKITVLGCGA LGQLWLAALC KRGHEVQGWL RVPQPYCSVN VIDEDGSVFN ESLTANDPDF
     LAQSDLLLVT LKAWQVSDAV KSLASMLPTT TPVLLIHNGM GTVEELKAIP HPLLMGITTH
     AARRDGNIII HVASGTTHIG PARQQDGDYS YLADTLQEVL PDVAWHNTIR PQLWRKLAVN
     CVINPLTALW NCPNGELLAH PELTEAICNE VAAVMEREGH HTSADDLLYY VNQVIENTAK
     NISSMLQDFR AQRRTEADYI TGYLLRRARA HGIAVPENTR LYEQIKRKES EYERIGTDMP
     RPW
//
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