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Database: UniProt
Entry: A0A235GAG0_9NOCA
LinkDB: A0A235GAG0_9NOCA
Original site: A0A235GAG0_9NOCA 
ID   A0A235GAG0_9NOCA        Unreviewed;       314 AA.
AC   A0A235GAG0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|RuleBase:RU362068};
DE            EC=1.1.1.169 {ECO:0000256|RuleBase:RU362068};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|RuleBase:RU362068};
GN   ORFNames=BDB13_4196 {ECO:0000313|EMBL:OYD70570.1};
OS   Rhodococcus sp. OK302.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1882769 {ECO:0000313|EMBL:OYD70570.1, ECO:0000313|Proteomes:UP000215121};
RN   [1] {ECO:0000313|EMBL:OYD70570.1, ECO:0000313|Proteomes:UP000215121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK302 {ECO:0000313|EMBL:OYD70570.1,
RC   ECO:0000313|Proteomes:UP000215121};
RA   Pelletier D.;
RT   "Populus root and rhizosphere microbial communities from Tennessee, USA.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC       pantoic acid. {ECO:0000256|RuleBase:RU362068}.
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|RuleBase:RU362068};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000256|RuleBase:RU362068}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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:OYD70570.1}.
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DR   EMBL; NPJZ01000001; OYD70570.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A235GAG0; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000215121; 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; IPR003710; ApbA.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00745; apbA_panE; 1.
DR   PANTHER; PTHR21708:SF26; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR   PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 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   NADP {ECO:0000256|RuleBase:RU362068};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068}.
FT   DOMAIN          7..154
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          181..305
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   314 AA;  32225 MW;  504B881D952D53AC CRC64;
     MTARMKVAVV GCGAMGSVYA GRLSTAGHDV LVVDRWVDHV NAIATSGLRI SGPDGEQVAS
     IRAFSAIPDE VVDLVILAVK ASDVPAAAAS LGSLIGDDTV VLTIQNGLGS ADEVARHVGA
     DRLAVGIASG FGASLVAPGQ VNHNAMRAMR FGAYGDLSFA VVDRVAEAWR TAGFDALAVD
     DIAAMQWEKL ICNVAYSAPC ALTGLTVGEV LDHDEMGPVS QAAAIEAWEV AKARGIAIDV
     GDPVAFVRDF GARMPAAKPS ALLDHEAGRV SEIALINGAI PREAAKVGRL APVNATLVAL
     VRTREAGFGV RPGS
//
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