ID A0A0Q6WB38_9BURK Unreviewed; 337 AA.
AC A0A0Q6WB38;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=ASD15_05305 {ECO:0000313|EMBL:KQV84604.1};
OS Massilia sp. Root351.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV84604.1, ECO:0000313|Proteomes:UP000051876};
RN [1] {ECO:0000313|EMBL:KQV84604.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV84604.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV84604.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV84604.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KQV84604.1}.
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DR EMBL; LMDJ01000012; KQV84604.1; -; Genomic_DNA.
DR RefSeq; WP_057155446.1; NZ_LMDJ01000012.1.
DR AlphaFoldDB; A0A0Q6WB38; -.
DR OrthoDB; 9796561at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000051876; 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; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR21708:SF42; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051876}.
FT DOMAIN 3..172
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 198..320
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 337 AA; 36096 MW; 60B54C136E7F6ACC CRC64;
MKIAIVGAGA IGGLVGARLA LAGEQVTFLV RGANLLAIRN KGIKLIEHDG SEQVATNVAA
TDDYAEAGPQ DVVILALKAH QVAAVADQLP LLFGPDTCVV TMQNGIPYWY FHQHGGHLEG
RTVHSVDPDG SLAVRIPPSR VIGCVVYPAS ELVAPGVVRH VEGERFPLGE LDGSTTPRVQ
AISECFTRAG FKAPVLDNIR SEIWLKLWGN LTFNPISALC HATLEGICQY PVARSLAADM
MKEAEAVANK LGVTFRVTLD KRIAGAEKVG RHKTSMLMDV EAGRGPEIDA LVGSVVELGR
FTDTATPHID AVYALVKLLE RTMTEERGQL RLQKMAA
//