ID A0A549THA2_9HYPH Unreviewed; 324 AA.
AC A0A549THA2;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 18-JUN-2025, entry version 20.
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=FNA46_02240 {ECO:0000313|EMBL:TRL42310.1};
OS Rhizobium straminoryzae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=1387186 {ECO:0000313|EMBL:TRL42310.1, ECO:0000313|Proteomes:UP000316801};
RN [1] {ECO:0000313|EMBL:TRL42310.1, ECO:0000313|Proteomes:UP000316801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM12 {ECO:0000313|EMBL:TRL42310.1,
RC ECO:0000313|Proteomes:UP000316801};
RA Tani A.;
RT "Ln-dependent methylotrophs.";
RL Submitted (JUL-2019) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TRL42310.1}.
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DR EMBL; VJMG01000006; TRL42310.1; -; Genomic_DNA.
DR RefSeq; WP_142880716.1; NZ_VJMG01000006.1.
DR AlphaFoldDB; A0A549THA2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000316801; 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: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; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR050838; Ketopantoate_reductase.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
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; SSF51905; FAD/NAD(P)-binding domain; 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 Reference proteome {ECO:0000313|Proteomes:UP000316801}.
FT DOMAIN 5..146
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 214..303
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 324 AA; 34940 MW; B9A8B3DB886DD496 CRC64;
MTRYIIIGAG AVGASLAAEF ERSGIAYALV GRGQQAAHIA AHGLTYRRPK ETRNVRLNIH
DTASPPSLAP GDILLLTVKS QDVEAATEFW AWQPVEGGGL AADLPLVTFQ NGLAAEDIAL
RRFAHVYAAS ILIPARFTVT GEVVVGSEPQ LGVVTVGRYP HGLDDTARTI AADLTAANYL
VEARADIRRW KSAKLEHNVT NVVELFAGDR EVRTKAADAL VTEARRVLQA AGHDPAARSE
RSVDISGWRI VEGSGIERGQ QSTWQSFTRG ASSEVDYLNG EIVRLGRLHG VETPLNAAFQ
RAAAELARDG RKPGTRDIHE VARF
//
