ID A6SUY6_JANMA Unreviewed; 336 AA.
AC A6SUY6;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 18-JUN-2025, entry version 90.
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 Name=apbA {ECO:0000313|EMBL:ABR88522.1};
GN OrderedLocusNames=mma_0393 {ECO:0000313|EMBL:ABR88522.1};
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286 {ECO:0000313|EMBL:ABR88522.1, ECO:0000313|Proteomes:UP000006388};
RN [1] {ECO:0000313|EMBL:ABR88522.1, ECO:0000313|Proteomes:UP000006388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille {ECO:0000313|EMBL:ABR88522.1,
RC ECO:0000313|Proteomes:UP000006388};
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|ARBA:ARBA00002919}.
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}.
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DR EMBL; CP000269; ABR88522.1; -; Genomic_DNA.
DR RefSeq; WP_012078258.1; NC_009659.1.
DR AlphaFoldDB; A6SUY6; -.
DR STRING; 375286.mma_0393; -.
DR KEGG; mms:mma_0393; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_6_1_4; -.
DR OrthoDB; 9796561at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000006388; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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 FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
DR FunFam; 3.40.50.720:FF:000307; 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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; NF005089; PRK06522.1-4; 1.
DR PANTHER; PTHR21708:SF45; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 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 ECO:0000313|EMBL:ABR88522.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655}.
FT DOMAIN 3..172
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 198..318
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 336 AA; 36203 MW; 445289D2A4CF351A CRC64;
MKIAIIGAGA IGGYVGVKLA LAGEDVTFIV RGANLEAIRK NGAKLIMHDG SEHVAANVKA
TNNYDEAGPQ DIIVLAMKAH QLEAIADDLP KLIGPETVIV TMQNGIPFWY FHKHGGKLTG
TRVESVDPTG KITAKIPADR VLGCVVYPAS ELIAPGVIKH IEGDRFPIGE LDGSTSERAT
RVSECFTNAG FKSPVLDNIR SEIWLKLWGN LTFNPISALS HSTLQDICQY PLSRELAAAM
MTEAQTIAHK LGIEFRVTLE KRIAGAEKVG KHKTSMLQDV EAGRDPEIDA LVGSVAELGR
LTETPTPHID TVYALVKLLA KTMNEETGQV KLQKVA
//
