ID A0A1X6ZC25_9RHOB Unreviewed; 339 AA.
AC A0A1X6ZC25;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 18-JUN-2025, entry version 23.
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 ORFNames=PSM7751_02215 {ECO:0000313|EMBL:SLN47321.1};
OS Pseudooceanicola marinus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=396013 {ECO:0000313|EMBL:SLN47321.1, ECO:0000313|Proteomes:UP000193963};
RN [1] {ECO:0000313|EMBL:SLN47321.1, ECO:0000313|Proteomes:UP000193963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7751 {ECO:0000313|EMBL:SLN47321.1,
RC ECO:0000313|Proteomes:UP000193963};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004994}.
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DR EMBL; FWFN01000004; SLN47321.1; -; Genomic_DNA.
DR RefSeq; WP_085888272.1; NZ_FWFN01000004.1.
DR AlphaFoldDB; A0A1X6ZC25; -.
DR OrthoDB; 9796561at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000193963; 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 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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 4: Predicted;
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000193963}.
FT DOMAIN 3..102
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 190..308
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 339 AA; 35297 MW; 4BAB07ADBEDC11A9 CRC64;
MKIAIIGAGN IGTAMAALIC NSGAEVTVVA RGARLQAIAE GGLALDDRGT RHDARPKATE
ALSEVQDAVF LCVKSQQLGA ALDTNRAGIG PETLVIPMVN GLPFWFFLPD ARPVPHTDPE
GILARLLRPE QVLGAVLLMT VSMDETGVAL STNTPTLSLA PVAPGADGAK VDALIESLNA
GGVVTDLSDD IRAKVLVKLM ANVTTNPLSA LVGCTLEEIG QRDDLCALAF AVADEFRAWA
KADLGRDLPP NPWLRELLLD AGPFATSMLQ DARAGRTLEL DAIARAAMTL AEDQGQPMRC
LAAIVHALDI ATTLPLDGTA CAAALSDLTS LTSLERTPS
//
