ID A0A0D7KCL0_9BURK Unreviewed; 366 AA.
AC A0A0D7KCL0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
GN ORFNames=RP29_02110 {ECO:0000313|EMBL:KJA12141.1};
OS Acidovorax temperans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=80878 {ECO:0000313|EMBL:KJA12141.1, ECO:0000313|Proteomes:UP000032566};
RN [1] {ECO:0000313|EMBL:KJA12141.1, ECO:0000313|Proteomes:UP000032566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KY4 {ECO:0000313|EMBL:KJA12141.1,
RC ECO:0000313|Proteomes:UP000032566};
RA Sheng K.-Y., Chin P.-S., Chan K.-G., Tan G.S.;
RT "Isolation of bacteria from lake water.";
RL Submitted (DEC-2014) 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:KJA12141.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JXYQ01000005; KJA12141.1; -; Genomic_DNA.
DR RefSeq; WP_044395370.1; NZ_JXYQ01000005.1.
DR AlphaFoldDB; A0A0D7KCL0; -.
DR STRING; 80878.RP29_02110; -.
DR PATRIC; fig|80878.5.peg.2715; -.
DR OrthoDB; 1073746at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000032566; 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; IPR029752; D-isomer_DH_CS1.
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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000032566}.
FT DOMAIN 10..133
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 191..329
FT /note="Opine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF02317"
SQ SEQUENCE 366 AA; 39707 MW; FFA157F955CBDA5C CRC64;
MKETYPMGKI AIVGAGNVGQ AIAGHMTLLG HDVRLYSRWE RDFEAINSTG GIELSGDVEG
RAAKPLLTTD IERAVKGADT VIVAAPAFAH AYLSQQLAAL LEPEQLVVFQ PSVLGSSLEL
ARHFASARRP PCLIAETPTS LYTCRLRGPA KVYIGAIKHA VQLATIPHMA CDKALNRLSQ
YFGNRYVAGT DTLSVGLGNC NAIYHVPPAV LNIKTVEDSD KLPQHTLVTP RIAEVINALD
EERLSLAAAL DVKTHSFWQF LEAAYGVTDG TYVERIVQGY GRQAFPEPDS LTHRYFTEDI
PFGLVTWSSL AKQIGLPLPL TDAFIRISGI LCDTDFEATG RTARVLGLEE NDPVSIKAAF
LNGVPR
//