ID W8X883_CASD6 Unreviewed; 425 AA.
AC W8X883;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 18-JUN-2025, entry version 41.
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=BN940_00721 {ECO:0000313|EMBL:CDM22625.1};
OS Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen)
OS (Alcaligenes defragrans).
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Alcaligenaceae; Castellaniella.
OX NCBI_TaxID=1437824 {ECO:0000313|EMBL:CDM22625.1, ECO:0000313|Proteomes:UP000019805};
RN [1] {ECO:0000313|EMBL:CDM22625.1, ECO:0000313|Proteomes:UP000019805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=65Phen {ECO:0000313|EMBL:CDM22625.1};
RX PubMed=24952578; DOI=10.1186/1471-2180-14-164;
RA Petasch J., Disch E.M., Markert S., Becher D., Schweder T., Huttel B.,
RA Reinhardt R., Harder J.;
RT "The oxygen-independent metabolism of cyclic monoterpenes in Castellaniella
RT defragrans 65Phen.";
RL BMC Microbiol. 14:164-164(2014).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|ARBA:ARBA00002919}.
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 -!- 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}.
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DR EMBL; HG916765; CDM22625.1; -; Genomic_DNA.
DR RefSeq; WP_084330430.1; NZ_HG916765.1.
DR AlphaFoldDB; W8X883; -.
DR STRING; 1437824.BN940_00721; -.
DR KEGG; cdn:BN940_00721; -.
DR PATRIC; fig|1437824.5.peg.146; -.
DR eggNOG; COG0346; Bacteria.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_0_0_4; -.
DR OrthoDB; 8555723at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000019805; 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:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR FunFam; 3.40.50.720:FF:000307; 2-dehydropantoate 2-reductase; 1.
DR Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1.
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; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR037523; VOC.
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 Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51819; VOC; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CDM22625.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000019805}.
FT DOMAIN 316..425
FT /note="VOC"
FT /evidence="ECO:0000259|PROSITE:PS51819"
SQ SEQUENCE 425 AA; 44379 MW; 27D26A9953C7FB2C CRC64;
MKICILGAGA LGSALGASLA EGGSEVVLLS RNAAHVEAIR AGGLRLRDQD DERRVRLRAE
TEAAAVGPVD LVVVLVKSFQ TREALAQAGP LFGPGTLALS LQNGLGHEDI LAESIGRERV
LAGKTYVGGT LLGPGHVLAG VRGKETLLGE LDGARTGRAL AIAREFERAG LPVRLSDNIL
GTIWDKLLIN VATGALTAIT RMPYGPLFQC APLEAVGVAA VREAMEIAHA AGVRLSITDP
LEAWRRAGAG LPADFRTSML QSLDKGSATE IDYINGAVVE RGLRLGIAAP VNATLAACVK
GIEAMAGRTA LARPPGIDHA AVRVEDIGWH VRFFEEVLGM PVREIDGPPE APRQVWLEGG
VQLIAAPAAA GDAGRAQSRI AHVALRVRGL EAALARAAGW PVTVLPQGPN WLRTPDGVAL
ELFDC
//
