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Database: UniProt
Entry: A0A0D7KCL0_9BURK
LinkDB: A0A0D7KCL0_9BURK
Original site: A0A0D7KCL0_9BURK 
ID   A0A0D7KCL0_9BURK        Unreviewed;       366 AA.
AC   A0A0D7KCL0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
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}.
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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   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
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
//
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