ID A0A1S6QI90_9LACO Unreviewed; 331 AA.
AC A0A1S6QI90;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 05-FEB-2025, entry version 29.
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=PL11_005025 {ECO:0000313|EMBL:AQW21335.1};
OS Lentilactobacillus curieae.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1138822 {ECO:0000313|EMBL:AQW21335.1, ECO:0000313|Proteomes:UP000030361};
RN [1] {ECO:0000313|EMBL:AQW21335.1, ECO:0000313|Proteomes:UP000030361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC M 2011381 {ECO:0000313|EMBL:AQW21335.1,
RC ECO:0000313|Proteomes:UP000030361};
RX PubMed=26021929;
RA Wang Y., Wang Y., Lang C., Wei D., Xu P., Xie J.;
RT "Genome Sequence of Lactobacillus curieae CCTCC M 2011381T, a Novel
RT Producer of Gamma-aminobutyric Acid.";
RL Genome Announc. 3:0-0(2015).
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; CP018906; AQW21335.1; -; Genomic_DNA.
DR RefSeq; WP_035167787.1; NZ_CP018906.1.
DR AlphaFoldDB; A0A1S6QI90; -.
DR KEGG; lcu:PL11_005025; -.
DR eggNOG; COG1893; Bacteria.
DR OrthoDB; 9800163at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000030361; 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 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:UP000030361}.
FT DOMAIN 4..143
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 182..308
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 331 AA; 37494 MW; 5962C0FB57FE9440 CRC64;
MKYTVLGAGA MGLRYGVLLQ EAGYDVDFVD TWEPQVNTIH EQNGVYVSRD GQDKHLVPVN
IYFPEDYEGD PDVLIVFTKQ YGLADMLERC SRFFNDRQYV VTCMNGMGHI EKLNQYFAKE
KVLGGTALIG TVLNKAGDVD FIGKKGAGSM NIANETEVPD EMTHKIVEEF QNANLNPNLT
TNFMGTLMAK VVFNSVINTL CTMFKIRMGE FIQSDVAKKL GVQLIDEAFD VCERAGITLL
NTREEEWQTV QTVSEVSNPL HFPSMYQDIS KQRPTEVDYI NGYIYELGTK YHYEAKTHDF
LRNLVHLAEF SDKFDVDAYV KSVRSADKTT V
//
