ID A0A852VWG8_9MICO Unreviewed; 358 AA.
AC A0A852VWG8;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 02-APR-2025, entry version 16.
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=BJY20_001996 {ECO:0000313|EMBL:NYF98604.1};
OS Janibacter cremeus.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Intrasporangiaceae; Janibacter.
OX NCBI_TaxID=1285192 {ECO:0000313|EMBL:NYF98604.1, ECO:0000313|Proteomes:UP000554054};
RN [1] {ECO:0000313|EMBL:NYF98604.1, ECO:0000313|Proteomes:UP000554054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26154 {ECO:0000313|EMBL:NYF98604.1,
RC ECO:0000313|Proteomes:UP000554054};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
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}.
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:NYF98604.1}.
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DR EMBL; JACCAE010000001; NYF98604.1; -; Genomic_DNA.
DR RefSeq; WP_185991393.1; NZ_JACCAE010000001.1.
DR AlphaFoldDB; A0A852VWG8; -.
DR Proteomes; UP000554054; 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:InterPro.
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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:NYF98604.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000554054}.
FT DOMAIN 19..176
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 198..337
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 358 AA; 37685 MW; BB97877136E8DDE8 CRC64;
MTTGAATARG GEAVRRTQVA IMGAGSIGCH LGGWLASNAE VTLIGRAPII DAIEAQGLTV
SDLDGHRRTV APTSLTLATE ASAVVDADYV LMTTKSNGTA RATRQIAPYL DPDSVVVSFQ
NGLRAASIID EALGSAFPSR ASRPLALSGM VPFNVVRTGD THWAQTVSGR MKVKDHPRID
PFIRAAHGAG LQIGVEPDMR AVLFGKLLLN LNNAVNALTG QPLAIQLRDR DCRTVLAACQ
DEALVLARRL GVSPARMTPL PPALVPSLLR SPNPVFTTLS RASLKVSPQA RSSMADDLSA
GRSTEIDEMQ GAIVALGRTH GTSTPVSSRI VDLVREAEEA GADRRRWTGA QLRDAVGL
//
