ID A0A4R0Y694_9PROT Unreviewed; 310 AA.
AC A0A4R0Y694;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 20.
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=EJV46_12320 {ECO:0000313|EMBL:TCH97991.1};
OS Roseococcus sp. SYP-B2431.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Acetobacterales; Roseomonadaceae; Roseococcus.
OX NCBI_TaxID=2496640 {ECO:0000313|EMBL:TCH97991.1, ECO:0000313|Proteomes:UP000292335};
RN [1] {ECO:0000313|EMBL:TCH97991.1, ECO:0000313|Proteomes:UP000292335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SYP-B2431 {ECO:0000313|EMBL:TCH97991.1,
RC ECO:0000313|Proteomes:UP000292335};
RA Cheng J., Zhang Y.-X.;
RL Submitted (FEB-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 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:TCH97991.1}.
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DR EMBL; SJXD01000025; TCH97991.1; -; Genomic_DNA.
DR RefSeq; WP_131549346.1; NZ_SJXD01000025.1.
DR AlphaFoldDB; A0A4R0Y694; -.
DR OrthoDB; 247668at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000292335; 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; 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|ARBA:ARBA00022655,
KW ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000292335}.
FT DOMAIN 3..151
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 178..294
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 310 AA; 33115 MW; 5139C6F2EC467122 CRC64;
MRVLVLGAGA LGGYFGGRLA EAGGDVTFLV RPGRAAALAR DGLVIESPFG DAKLAVKTIQ
AAELRRGWDI ILLSNKAYDL DDAIAAIRPG VDDRTVILPV LNGLSHIDIL AREFGAERVL
GGLCKIQATL TPAGVVKQLN DWRWLTFGER DGTMSPRVQA LEAAFSKAVG VEAKAVPNID
QRMWEKLVHL GTSAVGTVLM RANVGEIVRA GGSPMLLTLL ERNAAIAAHH GHPMPDAFMA
EYRALFGDAA SAYATSMLRD VEAGNRIEGE HILGFLAEAA HRAGIDTAIH DMAALQARSY
EQRRAANRLP
//
