ID K0EU89_NOCB7 Unreviewed; 341 AA.
AC K0EU89;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 18-JUN-2025, entry version 52.
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=O3I_026770 {ECO:0000313|EMBL:AFU03303.1};
OS Nocardia brasiliensis (strain ATCC 700358 / HUJEG-1).
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Nocardiaceae; Nocardia.
OX NCBI_TaxID=1133849 {ECO:0000313|EMBL:AFU03303.1, ECO:0000313|Proteomes:UP000006304};
RN [1] {ECO:0000313|EMBL:AFU03303.1, ECO:0000313|Proteomes:UP000006304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700358 {ECO:0000313|Proteomes:UP000006304};
RX PubMed=22535940; DOI=10.1128/JB.00210-12;
RA Vera-Cabrera L., Ortiz-Lopez R., Elizondo-Gonzalez R., Perez-Maya A.A.,
RA Ocampo-Candiani J.;
RT "Complete genome sequence of Nocardia brasiliensis HUJEG-1.";
RL J. Bacteriol. 194:2761-2762(2012).
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}.
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DR EMBL; CP003876; AFU03303.1; -; Genomic_DNA.
DR RefSeq; WP_014986158.1; NC_018681.1.
DR AlphaFoldDB; K0EU89; -.
DR STRING; 1133849.O3I_026770; -.
DR KEGG; nbr:O3I_026770; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_0_0_11; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000006304; Chromosome.
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 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 NCBIfam; NF006083; PRK08229.1; 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:UP000006304}.
FT DOMAIN 5..153
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 177..315
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 341 AA; 36655 MW; 8EC5156D18A005F5 CRC64;
MSSRVMVIGA GSIGIFVGGK LAVAGADVTF VGRPRLLDEI VASGIRLTDL DGGDDALAAD
RFRVATEPDD IGSAELVLVT VKSAATADAV RELAGKIRPG TVVLSLQNGI GNDTVIREIL
PHCVVLAGMV MFNVVHHPGG RFHRGTEGGL AVQDDPELAP FLGVFEQAGL PLRRYPDLRP
VQWAKLLLNL NNPINALSGR PLREQLADRD YRRCLALTQR EALTVMNKAR IAPARLTPVP
PRVMATLLTV PDGIFRRVFG QVLAVDPMAR SSMSDDLALG RRTEISWLCG EIVGLGAMVD
LPTPVNQRLI ELVVAAEQGD RRTWTGPELL AQLRAARAAI R
//
