ID A0A929KQI3_9PROT Unreviewed; 318 AA.
AC A0A929KQI3;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
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=IAI18_19690 {ECO:0000313|EMBL:MBE9607094.1};
OS Acetobacteraceae bacterium H6797.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Acetobacterales; Acetobacteraceae.
OX NCBI_TaxID=2571211 {ECO:0000313|EMBL:MBE9607094.1, ECO:0000313|Proteomes:UP000646848};
RN [1] {ECO:0000313|EMBL:MBE9607094.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H6797 {ECO:0000313|EMBL:MBE9607094.1};
RA Gulvik C.A.;
RL Submitted (OCT-2020) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:MBE9607094.1}.
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DR EMBL; JADFCQ010000006; MBE9607094.1; -; Genomic_DNA.
DR Proteomes; UP000646848; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; NF005089; PRK06522.1-4; 1.
DR PANTHER; PTHR21708:SF45; 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 Oxidoreductase {ECO:0000313|EMBL:MBE9607094.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000646848}.
FT DOMAIN 3..169
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 196..312
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 318 AA; 33107 MW; 297AA149E7A3EC0E CRC64;
MRVAVIGAGS IGGHMAVRLA RAGLDVSVVA RGAHGEAMAR EGLVLETGGE TIRAHPRVAT
PERAAELGVQ DAVVVAVKAL SLDGIAPLLP PLMGKGSLAL FAVNGLPWWY MEELCGPAHL
PPLAMGLALR GLLAPGQVLG CVANSANHKQ APGVIHNSDS LNRFTIGRAD GAECLTGRAL
AAALTQGGAE GVWSEDIRYD VWQKLLTNGW SAPLGCLTGL STKAVAADPA LRRIMASLIG
EIRGLAARCG VPLPEQPLPD PAKLPDHRTS MLQDLQAGIP VEFDAVLGAP NYLAHLMGSD
RCAMNTVLDL LRWRLAAA
//
