ID A0A142M453_AMIAI Unreviewed; 359 AA.
AC A0A142M453;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
GN ORFNames=FHS67_002217 {ECO:0000313|EMBL:MBB3705898.1};
OS Aminobacter aminovorans (Chelatobacter heintzii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Aminobacter.
OX NCBI_TaxID=83263 {ECO:0000313|EMBL:MBB3705898.1, ECO:0000313|Proteomes:UP000577697};
RN [1] {ECO:0000313|EMBL:MBB3705898.1, ECO:0000313|Proteomes:UP000577697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10368 {ECO:0000313|EMBL:MBB3705898.1,
RC ECO:0000313|Proteomes:UP000577697};
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 (AUG-2020) 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:MBB3705898.1}.
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DR EMBL; JACICB010000007; MBB3705898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A142M453; -.
DR STRING; 83263.AA2016_2193; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000577697; 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; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003421; Opine_DH.
DR PANTHER; PTHR38015; BLR6086 PROTEIN; 1.
DR PANTHER; PTHR38015:SF1; OCTOPINE_DH DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF02317; Octopine_DH; 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 Oxidoreductase {ECO:0000313|EMBL:MBB3705898.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655}.
FT DOMAIN 3..101
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 181..323
FT /note="Opine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF02317"
SQ SEQUENCE 359 AA; 37961 MW; 1242C25E4FAC08A4 CRC64;
MKVGIVGAGS IAFGTAVFLE QQGHKATLWS PSGERTKALA KGEALVAQGA VEGTFHPAAA
PSAEALVAGA EAIVIALPAY GHKVVLDAIA PYVRADQTVI ISSHASFGAL YLSRLLAARG
VVAPVVGWGT TVVSGRQLSP TLVNVNTVRK KVDLATVPAS RSADGLAVCQ TLFGDRFVDR
GSLMAIALSN LNPQNHMGIA LGNMTRMERG ETWSQGQNVT PNVGRLLEQL DEERIAIATK
LGLEVRNIFQ HFHLSFHVPM SSISEMNQEM HEAGNGGQGP TTADSRYVTE DVPFGLVMTA
KIGRLAGYPA ELHEAGVRIF SAMYGRDFTA ENDLLTALDL DAMSLAELNG LCRDGYAIA
//
