ID A0A975U759_9VIBR Unreviewed; 308 AA.
AC A0A975U759;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 02-APR-2025, entry version 12.
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=KNV97_02595 {ECO:0000313|EMBL:QXO16417.1};
OS Vibrio ostreae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Vibrio.
OX NCBI_TaxID=2841925 {ECO:0000313|EMBL:QXO16417.1, ECO:0000313|Proteomes:UP000694232};
RN [1] {ECO:0000313|EMBL:QXO16417.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OG9-811 {ECO:0000313|EMBL:QXO16417.1};
RA Muhammad N., Nguyen T.H., Lee Y.-J., Ko J., Kim S.-G.;
RT "Vibrio nov. sp., novel gut bacterium isolated from Yellow Sea oyster.";
RL Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {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}.
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DR EMBL; CP076642; QXO16417.1; -; Genomic_DNA.
DR RefSeq; WP_218562053.1; NZ_CP076642.1.
DR KEGG; vos:KNV97_02595; -.
DR Proteomes; UP000694232; Chromosome 2.
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:UniProtKB-KW.
DR FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
DR InterPro; IPR003710; ApbA.
DR InterPro; IPR050838; Ketopantoate_reductase.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
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.
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:UP000694232}.
FT DOMAIN 3..151
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 177..301
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 308 AA; 33868 MW; 6914AB9C969E1745 CRC64;
MKIAVIGAGA MGCLYGAYLS QQHQVFMIDA LESQVTAIQQ SGITIEEQSG EKVNFPRVQA
YLSGRCDVAM DLVIVFVKST YTQVALEQNQ NLFKESTLVM TLQNGAGNDR LIQQYVKPEN
IIIGTSKHNA VNLGLGQIKH PASGVTTIGS NHNADKQVAL AQGALLEASF VVEATDDIQR
IIWSKLLVNL SVNTFTAITQ TPIGYMIKNE HAWDFAKRLI YEAIEVAEAD GTYFDRREAL
NMVKSVCETA GDGYSSMYQD RKNQVKMEID AINGAIVEQA KRYGVPTPYN TLIVDLIHAM
EGAYGLYD
//
