ID A0A8J7KNZ8_9ENTR Unreviewed; 271 AA.
AC A0A8J7KNZ8;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 02-APR-2025, entry version 13.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN ORFNames=EKD82_01280 {ECO:0000313|EMBL:MBG6246919.1};
OS Candidatus Symbiopectobacterium sp. PLON1.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Enterobacterales; Enterobacteriaceae.
OX NCBI_TaxID=2794575 {ECO:0000313|EMBL:MBG6246919.1, ECO:0000313|Proteomes:UP000654998};
RN [1] {ECO:0000313|EMBL:MBG6246919.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PLON1 {ECO:0000313|EMBL:MBG6246919.1};
RA Husnik F.;
RT "Repeated replacement of an intrabacterial symbiont in the tripartite
RT nested mealybug symbiosis.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004994}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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:MBG6246919.1}.
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DR EMBL; RYVO01000007; MBG6246919.1; -; Genomic_DNA.
DR RefSeq; WP_252319899.1; NZ_RYVO01000007.1.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000654998; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:TreeGrafter.
DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR050838; Ketopantoate_reductase.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000654998}.
FT DOMAIN 6..134
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 167..225
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 271 AA; 28320 MW; B5587D89D8542709 CRC64;
MMAPHIAVVG AGAVGGFIGA RLAAAGENVT LIDRWREHGD TARRNGLRID GAVPQDNAIA
PVRILADDDI DSLKALPPLD IVFISVKSYD TRWAAELVLP YLHADAVVVS AQNGCNEATL
AEIVGASRTA GLIAARIGEL DGQRSARIET LATLLRQVDS VAVIDNLAGE RWSKLAVNAM
RNGVSAATGL TIDALDSHQQ LRRFSIKVAG EEVRVGQRLG YSLTALGAIP AALFAAATDG
SATALAEIEQ RLIDAAQRGA VGQRPSMGAG Y
//
