ID A0A5N8YDB6_9CHLR Unreviewed; 357 AA.
AC A0A5N8YDB6;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 02-APR-2025, entry version 14.
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=FIM03_00120 {ECO:0000313|EMBL:MQF63687.1};
OS SAR202 cluster bacterium AD-802-L14_MRT_200m.
OC Bacteria; Bacillati; Chloroflexota; Dehalococcoidia; SAR202 cluster.
OX NCBI_TaxID=2587837 {ECO:0000313|EMBL:MQF63687.1, ECO:0000313|Proteomes:UP000327263};
RN [1] {ECO:0000313|EMBL:MQF63687.1, ECO:0000313|Proteomes:UP000327263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD-802-L14_MRT_200m {ECO:0000313|EMBL:MQF63687.1};
RA Saw J.H., Nunoura T., Hirai M., Takaki Y., Parsons R., Michelsen M.,
RA Longnecker K., Kujawinski E.B., Stepanauskas R., Landry Z., Carlson C.A.,
RA Giovannoni S.J.;
RT "Pangenomics reveal diversification of enzyme families and niche
RT specialization in globally abundant SAR202 bacteria.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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:MQF63687.1}.
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DR EMBL; VEXG01000001; MQF63687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N8YDB6; -.
DR Proteomes; UP000327263; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
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; IPR050838; Ketopantoate_reductase.
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; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000327263}.
FT DOMAIN 10..153
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 196..336
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 357 AA; 38844 MW; 4B3C383BCF27C20B CRC64;
MSDQIKTKRI IFIGAGAVGS YLGGWLSHTG HDVTLVDIWD EHVKAIRDNG LVVNGPHEPF
VARPEIYHLH ENEHIARQPF FDIGFVAVKA YDTSWAATFV DKFVDPDGYI VSSQNTWTDP
EMAAAVGADR AVGLVMSSIS VAMWEAGKVE RPGDTRRRDH GHIVFRAGNH DGTDTPRLHE
LIEILDPIDG GKITTNLWGE RWAKLGQNSM GNPVAASTGM GMSDLNKHPR GRELQIRLAQ
ECASVGLAHG YEVENFGGRT ALEWASAARG EVYELLDAAL AERSTGANWR PSMAQDVVKG
RPTEILQMNA FVCDQGGLVN VDTPVNEAMV NVVKAIDAGE LESGFENVEL VLSSAGH
//
