ID A0A4Q8QW53_9BRAD Unreviewed; 353 AA.
AC A0A4Q8QW53;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 22.
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=CWO89_27215 {ECO:0000313|EMBL:TAI62907.1};
OS Bradyrhizobium sp. Leo170.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1571199 {ECO:0000313|EMBL:TAI62907.1, ECO:0000313|Proteomes:UP000292824};
RN [1] {ECO:0000313|EMBL:TAI62907.1, ECO:0000313|Proteomes:UP000292824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leo170 {ECO:0000313|EMBL:TAI62907.1,
RC ECO:0000313|Proteomes:UP000292824};
RA Avontuur J.R., Beukes C.W., Chan W.Y., Coetzee M.P., Palmer M., Shapiro N.,
RA Blom J., Stepkowski T., Venter S.N., Steenkamp E.T.;
RT "Genome-informed Bradyrhizobium taxonomy: where to from here?";
RL Submitted (JAN-2018) 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:TAI62907.1}.
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DR EMBL; PSRR01000191; TAI62907.1; -; Genomic_DNA.
DR RefSeq; WP_130581664.1; NZ_PSRR01000191.1.
DR AlphaFoldDB; A0A4Q8QW53; -.
DR OrthoDB; 9793586at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000292824; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000292824}.
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 277..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 353 AA; 38417 MW; D81F9ABB121AC5D1 CRC64;
MGRKIAIVGA GAVGGYVGAH MVQAGEDVTF IDPWPDHIEH MRKHGLRVTH ARDVAEFSVS
VRALHITDAQ QLAKERPVDI AFVCMKSYDT AWATMLIQQY LAPDGYVVSL QNCMNEETIA
GIVGWGRTLG CIASSITVNL PEPGHIHRGA GKGGAAHTVF RTGEVHGRVT ARAEEICRLV
GYSDSAKVTG NLWGERWSKL VANVMGNGLS ACTGLSGGDK LQSEPIRRFS TRLGSEAIRV
GQALGYQLEE ILHLSPETIA RAGEGDETAM RVCDEQRFRD GKRTSSEQRP SMGQDVQKGR
RTEIEFLNGL VVREGEKIGL SCAANAVLTD LVKRVERNEL SPDPRHITGL RLN
//
