ID A0A1H3QNU4_9MICO Unreviewed; 347 AA.
AC A0A1H3QNU4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 02-APR-2025, entry version 23.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|RuleBase:RU362068};
DE EC=1.1.1.169 {ECO:0000256|RuleBase:RU362068};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|RuleBase:RU362068};
GN ORFNames=SAMN05216554_2660 {ECO:0000313|EMBL:SDZ15232.1};
OS Herbiconiux ginsengi.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Microbacteriaceae; Herbiconiux.
OX NCBI_TaxID=381665 {ECO:0000313|EMBL:SDZ15232.1, ECO:0000313|Proteomes:UP000198891};
RN [1] {ECO:0000313|EMBL:SDZ15232.1, ECO:0000313|Proteomes:UP000198891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3491 {ECO:0000313|EMBL:SDZ15232.1,
RC ECO:0000313|Proteomes:UP000198891};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|RuleBase:RU362068};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|RuleBase:RU362068}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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DR EMBL; FNPZ01000002; SDZ15232.1; -; Genomic_DNA.
DR RefSeq; WP_092554412.1; NZ_FNPZ01000002.1.
DR AlphaFoldDB; A0A1H3QNU4; -.
DR STRING; 381665.SAMN05216554_2660; -.
DR OrthoDB; 9793586at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000198891; 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 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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00745; apbA_panE; 1.
DR PANTHER; PTHR21708:SF26; 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, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000198891}.
FT DOMAIN 6..154
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 184..323
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 347 AA; 37378 MW; 8D876718B249B56F CRC64;
MTGPRIAVLG AGANGASIGA DLIRAGLDVT LIEQWPEHVA AMRERGLTVN LPDRSENTAV
RVLHLCEVAT LTEPFDVVLL LMKAYDSRWA AHLIEPHLAP DGLLVGVQNG MTVDAIAEVV
GAHRTLGCVI EVSSTMFTPS VVERHSGPDR SWFAVGSLSD ATRGREREVA DLLAHAGRVE
VVDDIRSAKW MKLVSNATTL VTTASLGLPM MAALEHPGMR ELMLRSGQEA LDVAVAAGHR
IMPIFGLGHD DVSRPETVVE TLLDTLYRGF VLPNTTTTIL QDWTKRRHSE VDDLNGYVVT
EAKRLGLQAP VNAAVVEVAH RIERHELDPS PENAALLRHL AGAGLAA
//
