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Entry: I0QSM2_9GAMM
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Original site: I0QSM2_9GAMM 
ID   I0QSM2_9GAMM            Unreviewed;       364 AA.
AC   I0QSM2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
DE            EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN   ORFNames=SPM24T3_12489 {ECO:0000313|EMBL:EIC84295.1};
OS   Serratia sp. M24T3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=932213 {ECO:0000313|EMBL:EIC84295.1, ECO:0000313|Proteomes:UP000011072};
RN   [1] {ECO:0000313|EMBL:EIC84295.1, ECO:0000313|Proteomes:UP000011072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M24T3 {ECO:0000313|EMBL:EIC84295.1,
RC   ECO:0000313|Proteomes:UP000011072};
RX   PubMed=22740681; DOI=10.1128/JB.00670-12;
RA   Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT   "Draft Genome Sequence of Serratia sp. Strain M24T3, Isolated from Pinewood
RT   Disease Nematode Bursaphelenchus xylophilus.";
RL   J. Bacteriol. 194:3764-3764(2012).
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   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004994}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIC84295.1}.
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DR   EMBL; AJHJ01000013; EIC84295.1; -; Genomic_DNA.
DR   RefSeq; WP_009637103.1; NZ_AJHJ01000013.1.
DR   AlphaFoldDB; I0QSM2; -.
DR   STRING; 932213.SPM24T3_12489; -.
DR   PATRIC; fig|932213.3.peg.2530; -.
DR   eggNOG; COG1893; Bacteria.
DR   OrthoDB; 6530772at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000011072; Unassembled WGS sequence.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655}.
FT   DOMAIN          22..169
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          196..337
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   364 AA;  39382 MW;  E39A49ECF3CDA5A6 CRC64;
     MSVATLVEED MYPYQPQALS PIVIWGAGAI GGAIGASLIE SGRSVIFVDN VAEHVEAINL
     HGLRITGPLG ERKVQAQAYL PQQLEGFYNC VLLAVKSHHT PDAIHQIAPL LAPEGYVVSM
     QNGLNERVIA DVIGVERTVG AFLNFGADFI EPGVIHHGGR GAVVLGELDG ITRPRTEELY
     SLLLNFDSSA ILTPNIWGFL WAKMIYGALL FATALTDDSI ADVLAMPKFR PVLTALAREL
     GAVAHAQSIV LQGFDGFDPS AFLPDATKEH TSQSFDDMVA HNRRSAKSHS GIWRDLAVRK
     RQTEIDAQIA PAIDIGIGFN LPMPLTTRLV NLIHLVERGE LPQTLETLAL LEINEAGSPY
     AKSF
//
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