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
//