ID A0A0N1LPL7_9SPHN Unreviewed; 303 AA.
AC A0A0N1LPL7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 18-JUN-2025, entry version 33.
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 ORFNames=IP81_17555 {ECO:0000313|EMBL:KPF88761.1};
OS Novosphingobium sp. AAP83.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Sphingomonadales; Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523425 {ECO:0000313|EMBL:KPF88761.1, ECO:0000313|Proteomes:UP000037998};
RN [1] {ECO:0000313|EMBL:KPF88761.1, ECO:0000313|Proteomes:UP000037998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP83 {ECO:0000313|EMBL:KPF88761.1,
RC ECO:0000313|Proteomes:UP000037998};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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 -!- 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:KPF88761.1}.
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DR EMBL; LJHY01000058; KPF88761.1; -; Genomic_DNA.
DR RefSeq; WP_054109291.1; NZ_LJHY01000058.1.
DR AlphaFoldDB; A0A0N1LPL7; -.
DR STRING; 1523425.IP81_17555; -.
DR PATRIC; fig|1523425.4.peg.3519; -.
DR OrthoDB; 9793586at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000037998; 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: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; 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 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, 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:UP000037998};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..303
FT /note="2-dehydropantoate 2-reductase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005877078"
FT DOMAIN 4..152
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 183..299
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 303 AA; 31263 MW; EA6932B2C06E0C2B CRC64;
MKRIVIVGAG AMGCLFAARL ALAGSAVTVV DVDPARLALI AAEGIVLHDD AGEHIACVEA
KLAAEVTGPV DLLMLFTKGM HSAAAVRSVA HLVHTECAVL TLQNGLGNVE AIAEVFPAAH
ILWGVTDFPA DLEAQNAVAS HGAGHIVLGN YPDGADELAG KVAGLFASAG LHAVADPQAI
IAVWEKVAFN AALNALCTVS GLPVGGLDHP AGRRAAKAVI DEIVTITKAL GVAIDRPRLD
DKVRFALANH RTHKPSMLQD RIAGRATEIE SINGAIIAVA DEHAIPAPAL RLLTDLVRLC
EGK
//
