ID A0A073IJL9_9RHOB Unreviewed; 327 AA.
AC A0A073IJL9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 18-JUN-2025, entry version 42.
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=DSW25_06115 {ECO:0000313|EMBL:KEJ89795.1};
OS Sulfitobacter donghicola DSW-25 = KCTC 12864 = JCM 14565.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1300350 {ECO:0000313|EMBL:KEJ89795.1, ECO:0000313|Proteomes:UP000027734};
RN [1] {ECO:0000313|EMBL:KEJ89795.1, ECO:0000313|Proteomes:UP000027734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14565 {ECO:0000313|EMBL:KEJ89795.1,
RC ECO:0000313|Proteomes:UP000027734};
RA Lai Q., Hong Z.;
RT "Sulfitobacter donghicola JCM 14565 Genome Sequencing.";
RL Submitted (JAN-2014) 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:KEJ89795.1}.
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DR EMBL; JAMC01000002; KEJ89795.1; -; Genomic_DNA.
DR RefSeq; WP_025058268.1; NZ_JAMC01000002.1.
DR AlphaFoldDB; A0A073IJL9; -.
DR STRING; 1300350.Z948_805; -.
DR eggNOG; COG1893; Bacteria.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000027734; 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 NCBIfam; NF006083; PRK08229.1; 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:UP000027734}.
FT DOMAIN 3..153
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 174..312
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 327 AA; 34841 MW; F8277E653513CB3F CRC64;
MHIVVAGAGA IGCYVGGLLA HAGREVSFLG RPRILDVLGK NGLRVSDFSG LEAQLSAQSL
DLHNTPEVLG RGDLILVCVK SAATAEIAKQ IAAYAKPEAI IVSLQNGMGH ADTLRKELPN
HDVRAAMVPF NVVPSDKGHF HRATSGDIVI GAGPTPLGKI MNVKGLGVSE SDEIEAVQWG
KFLLNLNNAP NALSGMTLHA QLLSRPWRRL MADQMAEALR VLKAHNCPIR PTTPLPVGLV
PHILRLPTPL FRRIAAKMLT IDPQARTSMA HDLMAGRKTE VDALQGRIIA MGQEKSVPTP
LCQGMLAAIK QAEENGATPQ TPDSLRG
//
