ID A0A0A1VAD8_9BURK Unreviewed; 325 AA.
AC A0A0A1VAD8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=AVS7_00246 {ECO:0000313|EMBL:GAD20485.1};
OS Acidovorax sp. MR-S7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1268622 {ECO:0000313|EMBL:GAD20485.1};
RN [1] {ECO:0000313|EMBL:GAD20485.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-S7 {ECO:0000313|EMBL:GAD20485.1};
RX DOI=10.1128/genomeA.00412-13;
RA Miura T., Kusada H., Kamagata Y., Hanada S., Kimura N.;
RT "Genome Sequence of the Multiple-beta-Lactam-Antibiotic-Resistant Bacterium
RT Acidovorax sp. Strain MR-S7.";
RL Genome Announc. 1:e00412-13(2013).
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}.
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DR EMBL; DF238893; GAD20485.1; -; Genomic_DNA.
DR RefSeq; WP_020226682.1; NZ_DF238893.1.
DR AlphaFoldDB; A0A0A1VAD8; -.
DR STRING; 1268622.AVS7_00246; -.
DR eggNOG; COG1893; Bacteria.
DR OrthoDB; 9796561at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000030646; 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:UP000030646}.
FT DOMAIN 4..169
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 198..317
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 325 AA; 33936 MW; 8809572304EBE31A CRC64;
MKACIYGAGA IGGWLGAALA QAGCELNVVA RGATLAALQA EGLRLTRPDG TTAQVPVRAS
DAPAALGAQD LVVIAVKAPA LPDVARRIAP LIGPHTVVLT AMNGVPWWFT DGCEGPARGQ
ALASVDADGA IARAIPAGQV IGGVVHASCS LIAPGHVRQH QGNRLIVGEP GGQGSERLER
LAALLARGGI EAERSTRIQR DIWFKLWGNL TMNPISALTG ATTDRMLDDD LVRGFACAVM
LEAKAIGERL GLPIDQQPED RFAVTRQIGA FKTSMLQDVE AHKPLEVDAL VGAVCELGQR
TGVPTPHTDA LLGLTRLMAR TRGLY
//
