ID A0A4Q2Y4U9_9BACT Unreviewed; 309 AA.
AC A0A4Q2Y4U9;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465, ECO:0000256|RuleBase:RU362068};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014, ECO:0000256|RuleBase:RU362068};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024, ECO:0000256|RuleBase:RU362068};
GN ORFNames=EOP86_17320 {ECO:0000313|EMBL:RYD31709.1};
OS Verrucomicrobiaceae bacterium.
OC Bacteria; Pseudomonadati; Verrucomicrobiota; Verrucomicrobiia;
OC Verrucomicrobiales; Verrucomicrobiaceae.
OX NCBI_TaxID=2026800 {ECO:0000313|EMBL:RYD31709.1, ECO:0000313|Proteomes:UP000293567};
RN [1] {ECO:0000313|EMBL:RYD31709.1, ECO:0000313|Proteomes:UP000293567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PMG_210 {ECO:0000313|EMBL:RYD31709.1};
RX PubMed=30498029; DOI=.1073/pnas.1812668115;
RA Crombie A.T., Larke-Mejia N.L., Emery H., Dawson R., Pratscher J.,
RA Murphy G.P., McGenity T.J., Murrell J.C.;
RT "Poplar phyllosphere harbors disparate isoprene-degrading bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:13081-13086(2018).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|ARBA:ARBA00002919,
CC ECO:0000256|RuleBase:RU362068}.
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 ECO:0000256|RuleBase:RU362068};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004994, ECO:0000256|RuleBase:RU362068}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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:RYD31709.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SEGX01000734; RYD31709.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q2Y4U9; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000293567; Unassembled WGS sequence.
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; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
DR FunFam; 3.40.50.720:FF:000307; 2-dehydropantoate 2-reductase; 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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 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, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000293567}.
FT DOMAIN 2..148
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 177..295
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 309 AA; 32640 MW; CF6D7C391516C876 CRC64;
MAIVGSGALG SYYGARLAQH GQDVRFLMRS DLEHVREHGL DVRSHAGDFQ LPQVQAFGGT
EEIGPCDLVI ISLKTTANAA LARLLPPLLH PGTVVLTLQN GLGNEEFLST LHPARQVLGG
VCFVCINRLS PGVISHTAEG DIALGEFSGP ALPRTRAIGA MLEAAGIPCR VSDSLAAVRW
RKLVWNIPFN GLAITGGGIT TDLILQDPAL AKAVRGLMEE AIGAAAALGH PLPDGWADIQ
INRTPAMGAY RPSSMIDFVE GREVEVEAIW GEPCRRAQSA GAPSGRMEML YWMIQSAVAR
RQAGAASGG
//
