ID A0A2S1XU19_9PROT Unreviewed; 357 AA.
AC A0A2S1XU19;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 18-JUN-2025, entry version 25.
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=TSH58p_30410 {ECO:0000313|EMBL:AWJ87824.1};
OS Azospirillum sp. TSH58.
OG Plasmid tsh58_p05 {ECO:0000313|Proteomes:UP000244967}.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodospirillales; Azospirillaceae; Azospirillum.
OX NCBI_TaxID=664962 {ECO:0000313|EMBL:AWJ87824.1, ECO:0000313|Proteomes:UP000244967};
RN [1] {ECO:0000313|EMBL:AWJ87824.1, ECO:0000313|Proteomes:UP000244967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSH58 {ECO:0000313|EMBL:AWJ87824.1,
RC ECO:0000313|Proteomes:UP000244967};
RC PLASMID=tsh58_p05 {ECO:0000313|Proteomes:UP000244967};
RA Jang J., Ishii S.;
RT "Denitrification Functional Genes Identified in Mobile Genetic Elements in
RT Azospirillum Denitrifiers.";
RL Submitted (JUL-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}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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DR EMBL; CP022369; AWJ87824.1; -; Genomic_DNA.
DR RefSeq; WP_109067918.1; NZ_CP022369.1.
DR AlphaFoldDB; A0A2S1XU19; -.
DR KEGG; azt:TSH58p_30410; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000244967; Plasmid tsh58_p05.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
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; IPR003710; ApbA.
DR InterPro; IPR050838; Ketopantoate_reductase.
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:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR43765; 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Plasmid {ECO:0000313|EMBL:AWJ87824.1}.
FT DOMAIN 7..166
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 194..338
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 357 AA; 37164 MW; A19D4A631E8C0B4C CRC64;
MSDTRRVLIA GAGAVGGYIG AHLARAGHAV TLIDPWWENV AAIRARGLSI TGITAEEAFT
QPVRALGVGE AQSLVREAPF DYAFVAMKSY DTRWAAELVL PHLGPDGVIA SAQNGINDPT
IAAVAGPERT VGIVVAGIAA ELVEPARIRR AVPRGRPGNL EIGELDGRST ERVAALADLL
SAVDSTLVTT DLPSRRWTKL VVNAMRNAVS AATGLSGNDI TRVDAVRRAA IRIGGEAVRV
GRAKGLTVGR VTGIDPDDLQ GAAEGDAERL ARVEAIMLAG TRDGTRLDAQ RPSMGQDVLR
GRRTEIDHIN GLVVAGAEET GTAAPGNRAV LDIVRAIERG RLTPAPDRLA GVAVGPG
//
