ID A1BAQ0_PARDP Unreviewed; 355 AA.
AC A1BAQ0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN OrderedLocusNames=Pden_4530 {ECO:0000313|EMBL:ABL72594.1};
OS Paracoccus denitrificans (strain Pd 1222).
OG Plasmid pPD1222 {ECO:0000313|Proteomes:UP000000361}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL72594.1, ECO:0000313|Proteomes:UP000000361};
RN [1] {ECO:0000313|Proteomes:UP000000361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RC PLASMID=pPD1222 {ECO:0000313|Proteomes:UP000000361};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of plasmid 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|ARBA:ARBA00002919}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH;
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:ARBA00000784};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004994}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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DR EMBL; CP000491; ABL72594.1; -; Genomic_DNA.
DR RefSeq; WP_011750755.1; NC_008688.1.
DR AlphaFoldDB; A1BAQ0; -.
DR EnsemblBacteria; ABL72594; ABL72594; Pden_4530.
DR GeneID; 75503907; -.
DR KEGG; pde:Pden_4530; -.
DR eggNOG; COG1893; Bacteria.
DR HOGENOM; CLU_031468_0_0_5; -.
DR OrthoDB; 9793586at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000000361; Plasmid pPD1222.
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 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; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00745; apbA_panE; 1.
DR PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR PANTHER; PTHR43765:SF2; 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 Oxidoreductase {ECO:0000313|EMBL:ABL72594.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Plasmid {ECO:0000313|EMBL:ABL72594.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000361}.
FT DOMAIN 4..140
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 180..319
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 355 AA; 37948 MW; 4E22EC35604807FF CRC64;
MRAAIIGAGS LGTIIGALMA KGGRPVDLVD TNREHVDALD RDGARVTGEM DLLVPVHALT
PDAMSGQYDL VFLLSKQTAN KAVLSHLLPF LHGESVVCTL QNGIPEPSVA AVVGQGRTIG
GAVGFGATWL GPGVSSLTTT AEAVRKFAFE IGEMDGVIRP RLTGVQDYLS CVGRTELLDD
LMGIRWSKVL MNATFSGMSA ALGCTFGEVM DDPRALLCVA FIADETVRAA HAAGHRMAPM
QGEDFERFAL ASPASVLGVL PLIRKIWSQH RQLRASMLQD LEKGRDTEID FINGIVCRTG
REHGLATPFN DRVVELVSGA QAARSVPGFS NIDRFDDLLR PHRALLDSIS RGNHG
//
