ID A0A0L6T958_9BURK Unreviewed; 330 AA.
AC A0A0L6T958;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=AD742_10710 {ECO:0000313|EMBL:KNZ32682.1};
OS Methylibium sp. NZG.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=1686064 {ECO:0000313|EMBL:KNZ32682.1, ECO:0000313|Proteomes:UP000053102};
RN [1] {ECO:0000313|Proteomes:UP000053102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bi G.;
RT "Draft Genome Sequences of the MTBE Degrading Bacterium Methylibium sp.
RT NZG.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KNZ32682.1}.
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DR EMBL; LGRD01000016; KNZ32682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6T958; -.
DR STRING; 1686064.AD742_10710; -.
DR PATRIC; fig|1686064.3.peg.2564; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000053102; 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; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR21708:SF42; 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 4: Predicted;
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000053102}.
FT DOMAIN 3..104
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 201..320
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 330 AA; 34638 MW; D2BE024A834EA6BF CRC64;
MKIAVVGVGA VGGLMAARLV QAGHEVCALA RGATLATVRD RGLRLRSAGQ ESVVPLRASA
QAHDLGEQDL VVIAVKGTTL ATVAETLQPL LGPKTAVMPA MNGVPWWFLQ TPPTCDRLAP
QDRRIASIDP DGRIEAALPL PRVLGCVVHL TCSSPEPGVV QHGFGERLIV GEPAGGSSAR
MAEVCAALSQ AGFKAEASAQ IRSDVWYKLW GNMTMNPLSA LTGSTTAAML DDPLVHGFIL
RTMAEAAEVG AQLGCPISQS GEERMALTRQ LGAFKTSMLQ DALAGRALEL DALVSAVHEI
GLRFGVAMPN IGALLGMTRL MARERGLYPR
//
