ID A0A142MG78_AMIAI Unreviewed; 362 AA.
AC A0A142MG78;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
GN ORFNames=FHS67_006747 {ECO:0000313|EMBL:MBB3710382.1};
OS Aminobacter aminovorans (Chelatobacter heintzii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Aminobacter.
OX NCBI_TaxID=83263 {ECO:0000313|EMBL:MBB3710382.1, ECO:0000313|Proteomes:UP000577697};
RN [1] {ECO:0000313|EMBL:MBB3710382.1, ECO:0000313|Proteomes:UP000577697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10368 {ECO:0000313|EMBL:MBB3710382.1,
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:MBB3710382.1}.
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DR EMBL; JACICB010000054; MBB3710382.1; -; Genomic_DNA.
DR RefSeq; WP_067969815.1; NZ_JACICB010000054.1.
DR AlphaFoldDB; A0A142MG78; -.
DR OrthoDB; 6135265at2; -.
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:MBB3710382.1}.
FT DOMAIN 3..92
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 181..330
FT /note="Opine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF02317"
SQ SEQUENCE 362 AA; 37716 MW; 2F04CE56C44E12ED CRC64;
MKVAVLGAGA GGAASVAELV QAGHDVHFWA RSAETLEPHV KLGGVAYEGK LGEGVAKPAL
ITTDLKAAIA GVDVAVVVLP TFSHSAIASA LAGAGWSSSR PVVLNPGHTG GALEFAETFS
RTGRAAPPVV EFSTLTYVAR KYRPDGVTVS GRAKQLKAAA LKGGSEVLEI AGKLYPGLTP
VADVIASDLS NVNMVLHPPA AVLAAAWVEA TGGNFTFYVD AMTPGVARVM KQLDDERLAV
AKAFGHDLPN LVEEMKLLGT VEADVVDTSD FRAAIAGGEA NKRIKGPDSL EYRYYKEDFG
HGLLPFLEFA KIAGVETPVA HSLYSLAQIA VGTDYRKGGR TAEAMGIAGM SRDQVIQKVR
AQ
//