ID A0A4R6QP29_9BURK Unreviewed; 327 AA.
AC A0A4R6QP29;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 20.
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=DES47_102511 {ECO:0000313|EMBL:TDP72766.1};
OS Roseateles toxinivorans.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=270368 {ECO:0000313|EMBL:TDP72766.1, ECO:0000313|Proteomes:UP000295361};
RN [1] {ECO:0000313|EMBL:TDP72766.1, ECO:0000313|Proteomes:UP000295361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16998 {ECO:0000313|EMBL:TDP72766.1,
RC ECO:0000313|Proteomes:UP000295361};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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 -!- 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:TDP72766.1}.
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DR EMBL; SNXS01000002; TDP72766.1; -; Genomic_DNA.
DR RefSeq; WP_133700210.1; NZ_SNXS01000002.1.
DR AlphaFoldDB; A0A4R6QP29; -.
DR InParanoid; A0A4R6QP29; -.
DR OrthoDB; 9796561at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000295361; 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:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR FunFam; 1.10.1040.10:FF:000017; 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 4: Predicted;
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000295361}.
FT DOMAIN 3..107
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 200..319
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 327 AA; 34434 MW; D1392F619FB13AF6 CRC64;
MKICIVGAGA IGGWFAAHLG HRVASEVQLS ALARGATLAA LREHGLRMDS NGERIHVPIT
ASDRPEDLGP QDLIVIAVKG PALAAVAPAV KAMLAPHTRV LVAMNGVPWW FFDGLGGPCE
GLQLESVDPG GFVAAAIPSH QVIGCVVHAS CAVPEPGLVR HVMGMGLIIG APEGGRPEHI
DQLAALLSRA GFNATVSERI QKDIWYKLWG NMTMNPISAL TGATCDRILD DELVRGFVTA
VMREAAAIGA HIGCPVDQTP EERHEMTRKL GAFKTSMLQD AEAGRPLELA ALVGSVREIG
QHIALATPHT DAMLGLTRLM AQTRGLA
//