ID A0A1H8T7B1_9PSEU Unreviewed; 328 AA.
AC A0A1H8T7B1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE SubName: Full=Ketopantoate reductase {ECO:0000313|EMBL:SEO86837.1};
GN ORFNames=SAMN04489732_102465 {ECO:0000313|EMBL:SEO86837.1};
OS Amycolatopsis saalfeldensis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=394193 {ECO:0000313|EMBL:SEO86837.1, ECO:0000313|Proteomes:UP000198582};
RN [1] {ECO:0000313|EMBL:SEO86837.1, ECO:0000313|Proteomes:UP000198582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44993 {ECO:0000313|EMBL:SEO86837.1,
RC ECO:0000313|Proteomes:UP000198582};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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DR EMBL; FOEF01000002; SEO86837.1; -; Genomic_DNA.
DR RefSeq; WP_091614052.1; NZ_FOEF01000002.1.
DR AlphaFoldDB; A0A1H8T7B1; -.
DR STRING; 394193.SAMN04489732_102465; -.
DR OrthoDB; 9796561at2; -.
DR Proteomes; UP000198582; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
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; 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 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000198582}.
FT DOMAIN 3..170
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 197..316
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 328 AA; 34057 MW; C2D3EA0F48BB4987 CRC64;
MRVAVLGAGA IGAYVGAALH RGGADVHLVA RGPHLAAMRE HGVRVLSPRG DFTARPHVTD
DPAEVGPVDY VFLGLKAHSY PGCGPLVAPL LGPETALVAA QNGIPWWYFH GLDGHPLAGR
RVETVDPGGA TSAVLAVERA VGCVVYCSTV IEEPGVIRHL EGTRFSLGEP AGGRSARCLA
LAEAMVAGGL KAPVEPNLRD DIWVKLMGNV AFNPLSALTR ATMAQMCEHD DTRALVATMM
TETLAIARAA GADPQVSVAK RIDGAWRVGH HKTSMLQDLE AGKPLEIDAI IGAVVELAAL
TGVPAPALRH VHAAIGLLNH TATAVPVG
//
