ID A0A318EDU9_9GAMM Unreviewed; 329 AA.
AC A0A318EDU9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=C8D93_10488 {ECO:0000313|EMBL:PXV68393.1};
OS Sinimarinibacterium flocculans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Sinimarinibacterium.
OX NCBI_TaxID=985250 {ECO:0000313|EMBL:PXV68393.1, ECO:0000313|Proteomes:UP000248330};
RN [1] {ECO:0000313|EMBL:PXV68393.1, ECO:0000313|Proteomes:UP000248330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 104150 {ECO:0000313|EMBL:PXV68393.1,
RC ECO:0000313|Proteomes:UP000248330};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (APR-2018) 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 -!- 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:PXV68393.1}.
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DR EMBL; QICN01000004; PXV68393.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318EDU9; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000248330; 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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000248330}.
FT DOMAIN 3..151
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 174..308
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 329 AA; 35932 MW; BBC3CBC7393D80AC CRC64;
MMLVVGAGAV GTILCAHLTA ARREPAKLYV REKDVETLQT VQTLRVEHAG AGHPPIVAPK
PQLTRSLALD DIDYLLLCVK FPQLDAVLDQ LGDVPQRCSI VSTLNGVGAL RRIRERYPDA
RTVPMTIMFN GQLLEPLHAR ITTRPQVLIG SDDERLLRAF GTGMQVTRVA GESAAWGKLL
INLANAICAL THTTFKDLLT HPDLRAIYVA VLDEAIRLLD AAGIDYKLPM PIPYGVYRAL
LGGRTPLPWW FAKLRNGLQE GSYPSMVADV DAGRPTEIGQ LNGEIVCLGL EHKVPTPVNA
RIIGLIQKFE GQSPPPYLTP AALRQRLGV
//
