ID A0A6H0IVF3_9GAMM Unreviewed; 324 AA.
AC A0A6H0IVF3;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 02-APR-2025, entry version 18.
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=HC341_04625 {ECO:0000313|EMBL:QIT54566.1};
OS Aquisalimonas sp. 2447.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Chromatiales; Ectothiorhodospiraceae; Aquisalimonas.
OX NCBI_TaxID=2740807 {ECO:0000313|EMBL:QIT54566.1, ECO:0000313|Proteomes:UP000502501};
RN [1] {ECO:0000313|EMBL:QIT54566.1, ECO:0000313|Proteomes:UP000502501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2447 {ECO:0000313|EMBL:QIT54566.1,
RC ECO:0000313|Proteomes:UP000502501};
RA Xue Q.;
RL Submitted (MAR-2020) 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}.
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DR EMBL; CP050695; QIT54566.1; -; Genomic_DNA.
DR RefSeq; WP_167781521.1; NZ_CP050695.1.
DR AlphaFoldDB; A0A6H0IVF3; -.
DR KEGG; nax:HC341_04625; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000502501; Chromosome.
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; IPR003710; ApbA.
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; TIGR00745; apbA_panE; 1.
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 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:UP000502501}.
FT DOMAIN 4..158
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 191..311
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 324 AA; 35006 MW; 566065802D6851AD CRC64;
MRMAVIGAGG VGGYYGARWL AAGNPVTFVA RGGHLEQLRE QGLRVEHPEF HYRHRVDATD
LAALCAGDPA EFDLLVLAVK SAATRDVAAT LHDWFQRYGR RVPVLSMQNG VDNEGELAAV
LGQDAVIGGL ALRVGTHVEA PGRITATGAG QVVTGPWPNR EEAVAGPATD ILPTFVQTAN
AAGTPVIETS DIRRELWRKL VINNGLNPIS ALTGWDSRRL TRNPEMVVTI RRLMHEAAAA
ARADRVTLDG ADVDEMFQLI HDLDPIKTSM LVDREHGRPM ELDAICGAVM ARLRQLGEDA
PATELLAGLL RNGIWSTEPD RDDA
//
