ID A0A3E0U4Z8_9GAMM Unreviewed; 340 AA.
AC A0A3E0U4Z8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 02-APR-2025, entry version 19.
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=DXX94_15850 {ECO:0000313|EMBL:REL32071.1};
OS Thalassotalea euphylliae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Alteromonadales; Colwelliaceae; Thalassotalea.
OX NCBI_TaxID=1655234 {ECO:0000313|EMBL:REL32071.1, ECO:0000313|Proteomes:UP000256899};
RN [1] {ECO:0000313|Proteomes:UP000256899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3 {ECO:0000313|Proteomes:UP000256899};
RA Summers S., Rice S.A., Freckelton M.L., Nedved B.T., Hadfield M.G.;
RT "Thalassotalea euphylliae genome.";
RL Submitted (AUG-2018) 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}.
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:REL32071.1}.
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DR EMBL; QUOT01000001; REL32071.1; -; Genomic_DNA.
DR RefSeq; WP_116017376.1; NZ_QUOT01000001.1.
DR AlphaFoldDB; A0A3E0U4Z8; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000256899; 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:0050661; F:NADP binding; IEA:TreeGrafter.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
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, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000256899}.
FT DOMAIN 22..184
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 210..331
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 340 AA; 36559 MW; E8BC824EDFA2B5E6 CRC64;
MSKAPEMKAA ALTTDKCKHL NIVVAGQGAI GSLWCWYLTQ YSAVNLSTVT RAPAFPTSPT
ISSFPNTPSA PKLKKQLSFS HFNGQSYQYH CLLADDKTLN NADLLVVCLK SYDAAQLVNN
IASKLAPTTD ILLVHNGMGV YEALSDKIKA THNIYTCLTT HGAFRPTKSH VIHTGLGSFD
IGRHAFVQNE PAPWFNALKC ALPNAHWQSD IKTKQWQKLA INCVINPLTA LNNVCNGEIT
QAQYLPQISA IAKEVSEVAS SQDITLEANT IVEQALAVAQ ATANNVSSTL ADVRADRTTE
INAINGYICQ LAIEAGISVP SNSALVEQVN ALLKSAAPSQ
//
