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Database: UniProt
Entry: A0A0R3MGB9_9BRAD
LinkDB: A0A0R3MGB9_9BRAD
Original site: A0A0R3MGB9_9BRAD 
ID   A0A0R3MGB9_9BRAD        Unreviewed;       353 AA.
AC   A0A0R3MGB9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=CQ14_18980 {ECO:0000313|EMBL:KRR18972.1};
OS   Bradyrhizobium lablabi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=722472 {ECO:0000313|EMBL:KRR18972.1, ECO:0000313|Proteomes:UP000051660};
RN   [1] {ECO:0000313|EMBL:KRR18972.1, ECO:0000313|Proteomes:UP000051660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCBAU 23086 {ECO:0000313|EMBL:KRR18972.1,
RC   ECO:0000313|Proteomes:UP000051660};
RA   Duran D., Rey L., Navarro A., Busquets A., Imperial J., Ruiz-Argueso T.;
RT   "Bradyrhizobium valentinum sp. nov., isolated from effective nodules of
RT   Lupinus mariae-josephae, a lupine endemic of basic-lime soils in Eastern
RT   Spain.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC       pantoic acid. {ECO:0000256|ARBA:ARBA00002919}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH;
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:ARBA00000784};
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:KRR18972.1}.
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DR   EMBL; LLYB01000101; KRR18972.1; -; Genomic_DNA.
DR   RefSeq; WP_057861307.1; NZ_LLYB01000101.1.
DR   AlphaFoldDB; A0A0R3MGB9; -.
DR   STRING; 722472.SAMN05444321_0749; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000051660; Unassembled WGS sequence.
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   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; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00745; apbA_panE; 1.
DR   PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43765:SF2; 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}.
FT   DOMAIN          5..149
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          191..336
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          276..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   353 AA;  38345 MW;  65956AFB54491304 CRC64;
     MGRKIAIVGA GAVGGYAGAH MVQAGEDVTF IDPWPEHVEH MRKHGLRVTH AMDVAEFSVP
     VRALHVTDAQ QLSKEKPVDI AFVCMKSYDR AWATMLIQQY LAADGYVVSL QNCMNEETIA
     GVVGWGKTLG CIASSITVNL PDPGHIHRGA GKGGAAHTVF RAGEVHGRIT PRAEEVCRLV
     GYSDSAKVTE NLWGERWSKL VANVMGNGLS ACTGLPGGEI LQSEPLRRFS TRLGSEAIRV
     GQAHGYQLEE ILHLAPDTIA RAGEGDEAAM RACDEQRFKD SKRTSAAQRP SMGQDMQKGR
     RTEIEFLNGF VVREGEKLGL SCTANAALTD IVKRVERGEL SPDPRHITEL RLN
//
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