ID K0DBS2_LEUCJ Unreviewed; 336 AA.
AC K0DBS2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 OrderedLocusNames=C270_06995 {ECO:0000313|EMBL:AFT82308.1};
OS Leuconostoc carnosum (strain JB16).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=1229758 {ECO:0000313|EMBL:AFT82308.1, ECO:0000313|Proteomes:UP000006299};
RN [1] {ECO:0000313|EMBL:AFT82308.1, ECO:0000313|Proteomes:UP000006299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB16 {ECO:0000313|EMBL:AFT82308.1,
RC ECO:0000313|Proteomes:UP000006299};
RX PubMed=23144413; DOI=10.1128/JB.01805-12;
RA Jung J.Y., Lee S.H., Jeon C.O.;
RT "Complete genome sequence of Leuconostoc carnosum strain JB16, isolated
RT from Kimchi.";
RL J. Bacteriol. 194:6672-6673(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 + H(+) + NADPH;
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:ARBA00000784,
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; CP003851; AFT82308.1; -; Genomic_DNA.
DR RefSeq; WP_014974918.1; NC_018673.1.
DR AlphaFoldDB; K0DBS2; -.
DR STRING; 1229758.C270_06995; -.
DR GeneID; 61187246; -.
DR KEGG; lcn:C270_06995; -.
DR PATRIC; fig|1229758.3.peg.1404; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_0_0_9; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000006299; Chromosome.
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; 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; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00745; apbA_panE; 1.
DR PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR PANTHER; PTHR43765:SF2; 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|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000006299}.
FT DOMAIN 3..146
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 184..310
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 336 AA; 37509 MW; 0B43BDE28A401F2D CRC64;
MKYAVVGAGA MGLRYGILLQ ENAGVAVDFI EPTQASLDKI HEQDDQVWKS RDHQDKHKIK
INIFSPEEYN GTPDVWIFFM KQMQLQDALD RLKPKFKPGQ TALGAMNGMG HIEKLQNYFD
DAHIIGGTAM IATVLNDYGD VDFMGAESAG SSVYANLTEQ PSETMDLLQK DFQAAHLNPS
YTENFMGTLL TKVFFNAVEN SIATMFQSRM GQLMAYDNFL EGIARPLINE AYDAAEAAGI
KLIETRDEMV AQVDYVSNVA NPLHFPSMYQ DFVKGRPTEV DYINGWIADL ADKHGTQAPN
HRLVTHFVHL AESMREFTPP VNKLAPDYKE AAATQA
//
