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Database: UniProt
Entry: Q88IK1_PSEPK
LinkDB: Q88IK1_PSEPK
Original site: Q88IK1_PSEPK 
ID   Q88IK1_PSEPK            Unreviewed;       315 AA.
AC   Q88IK1;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 130.
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=PP_2998 {ECO:0000313|EMBL:AAN68606.1};
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488 {ECO:0000313|EMBL:AAN68606.1, ECO:0000313|Proteomes:UP000000556};
RN   [1] {ECO:0000313|EMBL:AAN68606.1, ECO:0000313|Proteomes:UP000000556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440
RC   {ECO:0000313|Proteomes:UP000000556};
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L., Beanan M., DeBoy R.T., Daugherty S., Kolonay J., Madupu R.,
RA   Nelson W., White O., Peterson J., Khouri H., Hance I., Chris Lee P.,
RA   Holtzapple E., Scanlan D., Tran K., Moazzez A., Utterback T., Rizzo M.,
RA   Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D.,
RA   Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N.,
RA   Dusterhoft A., Tummler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN68606.1; -; Genomic_DNA.
DR   RefSeq; NP_745142.1; NC_002947.4.
DR   RefSeq; WP_010953898.1; NC_002947.4.
DR   AlphaFoldDB; Q88IK1; -.
DR   STRING; 160488.PP_2998; -.
DR   PaxDb; 160488-PP_2998; -.
DR   GeneID; 83680437; -.
DR   KEGG; ppu:PP_2998; -.
DR   PATRIC; fig|160488.4.peg.3170; -.
DR   eggNOG; COG1893; Bacteria.
DR   HOGENOM; CLU_031468_0_0_6; -.
DR   OMA; VVRWGQR; -.
DR   OrthoDB; 6530772at2; -.
DR   PhylomeDB; Q88IK1; -.
DR   BioCyc; PPUT160488:G1G01-3181-MONOMER; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000000556; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000556}.
FT   DOMAIN          3..152
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          178..303
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   315 AA;  32933 MW;  1BB3A962A3C94CA1 CRC64;
     MKICILGAGA LGCAIGAALS EAGHETWLLN RGRAHVEAIN QHGLRVQDER GERHVPVKAA
     IEAVDVGVTD LVVVLVKSFH TAEAIAGAHG LIGPQTLVLS LQNGLGHEDI LAEVVGRERV
     LAGKTYVGGV LLAPGSIRAG VAGKQTFIGE LDGQLTPRVQ AIAEAFNNAG LATTVSDNIL
     GTMWDKLLVN VATGALSGIT RLSYGQLYSE PLLESTAKAA VAEAIAVAER AGIRLSLTSP
     EAAWSLAAEG LPASFRTSML QSLEKNSITE IDFINGSVVR WGQRHGVATP VNATLVACIK
     GIERAMADHQ KRETP
//
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