ID A0A1N7P4S8_9PROT Unreviewed; 333 AA.
AC A0A1N7P4S8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 18-JUN-2025, entry version 28.
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=SAMN05421779_10650 {ECO:0000313|EMBL:SIT05429.1};
OS Insolitispirillum peregrinum.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodospirillales; Novispirillaceae; Insolitispirillum.
OX NCBI_TaxID=80876 {ECO:0000313|EMBL:SIT05429.1, ECO:0000313|Proteomes:UP000185678};
RN [1] {ECO:0000313|EMBL:SIT05429.1, ECO:0000313|Proteomes:UP000185678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11589 {ECO:0000313|EMBL:SIT05429.1,
RC ECO:0000313|Proteomes:UP000185678};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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; FTOA01000006; SIT05429.1; -; Genomic_DNA.
DR RefSeq; WP_076401381.1; NZ_FTOA01000006.1.
DR AlphaFoldDB; A0A1N7P4S8; -.
DR STRING; 80876.SAMN05421779_10650; -.
DR OrthoDB; 247668at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000185678; 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; 1.10.1040.10:FF:000017; 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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; NF005089; PRK06522.1-4; 1.
DR PANTHER; PTHR21708:SF45; 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:UP000185678}.
FT DOMAIN 3..170
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 200..320
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 333 AA; 35684 MW; C2960F6C730D8087 CRC64;
MKITIIGAGA VGNLLAARLS ATPAQVSLLA RGEALEAVRR QGIMMVTPLR RVVYAQPHVT
DDAHELGPQD VVFLCVKAHA LRSALDSLSL LTGPHTVVVP MINGIPWWYP YQQPAPLADQ
PLNSVDPSEA LWRTINPAQV IGATTFVAVE NDGPGRIRHI SDQRFVFGAI SPDSPHTAAM
VTEIVDLFGQ AGFQSRATDD IREAVWVKLW GNLGFNPLSA LTGATLGTLC LDPGTRSVGR
AMMLEAKAVA EQLGITFGTS VDERIEMAAG VGDFKTSMLQ DFEAGRRLET AAIIGAVIEL
AERLGMAVPT LRTILALLEM RVRSRDHALQ SAA
//
