ID A0A916QB20_9BACL Unreviewed; 319 AA.
AC A0A916QB20;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 02-APR-2025, entry version 13.
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:GFR37457.1};
GN ORFNames=PRECH8_07530 {ECO:0000313|EMBL:GFR37457.1};
OS Insulibacter thermoxylanivorax.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Insulibacter.
OX NCBI_TaxID=2749268 {ECO:0000313|EMBL:GFR37457.1, ECO:0000313|Proteomes:UP000654993};
RN [1] {ECO:0000313|EMBL:GFR37457.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DA-C8 {ECO:0000313|EMBL:GFR37457.1};
RA Uke A., Chhe C., Baramee S., Kosugi A.;
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GFR37457.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DA-C8 {ECO:0000313|EMBL:GFR37457.1};
RX DOI=10.1016/j.dib.2021.106784;
RA Chhe C., Uke A., Baramee S., Ungkulpasvich U., Tachaapaikoon C., Pason P.,
RA Waeonukul R., Ratanakhanokchai K., Kosugi A.;
RT "Draft genome sequence data of the facultative, thermophilic, xylanolytic
RT bacterium Paenibacillus sp. strain DA-C8.";
RL Data Brief 35:0-0(2021).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|ARBA:ARBA00002919,
CC 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:GFR37457.1}.
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DR EMBL; BMAQ01000005; GFR37457.1; -; Genomic_DNA.
DR RefSeq; WP_200965737.1; NZ_BMAQ01000005.1.
DR Proteomes; UP000654993; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-KW.
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:UP000654993}.
FT DOMAIN 3..160
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 195..316
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 144..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 319 AA; 34798 MW; 3D102A5E406F6DB0 CRC64;
MRIWVLGGGA IGLLYAAKLR ASGADVMLLT RTREQAAKIA ASGIEVCDEK GSWNIPCVSI
AVDDLTQPGE LGEEAPEWIL LTVKQYGITE RMLAWLNSLG QASPRMKLLA MQNGLGHLER
LAAHLPPERL YAAVVSEGAL RTGPASVQHT GSGVTKIGAA APDGEGEMQR RRTLRDLQKV
LQNAGFESIL SKQLIDDLWH KLIINSVINP LTALLGIPNG ELIEHQSLLT VMRQLMEEAR
TVAARSGAQT DDSIWESILE VCRRTASNRS SMLQDLEAGR PTELRWINGA VVEAARRCGL
SVPTHETILQ LVQAKERIR
//
