ID K9NFQ1_9PSED Unreviewed; 316 AA.
AC K9NFQ1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
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 Name=panE1 {ECO:0000313|EMBL:AFY18624.1};
GN ORFNames=PputUW4_01418 {ECO:0000313|EMBL:AFY18624.1};
OS Pseudomonas sp. UW4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1207075 {ECO:0000313|EMBL:AFY18624.1, ECO:0000313|Proteomes:UP000010397};
RN [1] {ECO:0000313|EMBL:AFY18624.1, ECO:0000313|Proteomes:UP000010397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UW4 {ECO:0000313|EMBL:AFY18624.1,
RC ECO:0000313|Proteomes:UP000010397};
RX PubMed=23516524;
RA Duan J., Jiang W., Cheng Z., Heikkila J.J., Glick B.R.;
RT "The Complete Genome Sequence of the Plant Growth-Promoting Bacterium
RT Pseudomonas sp. UW4.";
RL PLoS ONE 8:E58640-E58640(2013).
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 + 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; CP003880; AFY18624.1; -; Genomic_DNA.
DR AlphaFoldDB; K9NFQ1; -.
DR STRING; 1207075.PputUW4_01418; -.
DR KEGG; ppuu:PputUW4_01418; -.
DR PATRIC; fig|1207075.3.peg.1450; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_2_1_6; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000010397; 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; 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|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}.
FT DOMAIN 9..158
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 189..309
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 316 AA; 33854 MW; 9127AF634FB3F077 CRC64;
MGTVARPTIG IIGTGAIGGF YGVMLARAGF DVHFLLRSEF CAVAEHGLRV DSAPHGALML
NPVQAYSKAE DMPPCDWLLV GAKTTSNADL APAILQAAAP DAKVLLLQNG LDVEDSLRAL
LPDSLHVLGG LCYICVHREA PGVITHQALG AVHVGYHSGP ADGPTRTAIV EEGVGLFRSA
GLDSQAMANL HQARWQKLVW NIPYNGLSVL LGASTTPLMA DADSRELIKA LMAEVVQGAI
ACGHDVPAGY AEHLFMVTEK MPDYWPSMYH DFLHKRPLEL AAIYARPLAA ARAAGCEMPR
IEALYRSLSF IDRRNT
//
