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Database: UniProt
Entry: B9BGX2_9BURK
LinkDB: B9BGX2_9BURK
Original site: B9BGX2_9BURK 
ID   B9BGX2_9BURK            Unreviewed;       312 AA.
AC   B9BGX2;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465, ECO:0000256|RuleBase:RU362068};
DE            EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014, ECO:0000256|RuleBase:RU362068};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024, ECO:0000256|RuleBase:RU362068};
GN   Name=panE {ECO:0000313|EMBL:EEE08945.1};
GN   ORFNames=BURMUCGD2_4317 {ECO:0000313|EMBL:EEE08945.1};
OS   Burkholderia multivorans CGD2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=513052 {ECO:0000313|EMBL:EEE08945.1, ECO:0000313|Proteomes:UP000004535};
RN   [1] {ECO:0000313|EMBL:EEE08945.1, ECO:0000313|Proteomes:UP000004535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGD2 {ECO:0000313|EMBL:EEE08945.1,
RC   ECO:0000313|Proteomes:UP000004535};
RX   PubMed=23105085; DOI=10.1128/JB.01306-12;
RA   Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., Radune D.,
RA   Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., Greenberg D.E.,
RA   Holland S.M., Goldberg J.B.;
RT   "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic
RT   Granulomatous Disease Burkholderia multivorans Isolates.";
RL   J. Bacteriol. 194:6356-6357(2012).
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|ARBA:ARBA00000784,
CC         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|ARBA:ARBA00004994, 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:EEE08945.1}.
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DR   EMBL; ACFC01000001; EEE08945.1; -; Genomic_DNA.
DR   RefSeq; WP_006403052.1; NZ_ACFC01000001.1.
DR   AlphaFoldDB; B9BGX2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000004535; 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   ECO:0000313|EMBL:EEE08945.1};
KW   Pantothenate biosynthesis {ECO:0000256|RuleBase:RU362068}.
FT   DOMAIN          3..150
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          178..279
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   312 AA;  33365 MW;  6A63883C6C01808A CRC64;
     MRILVVGAGA VGGYFGGRLA AAGRDVTFLV RDGRAAALAR DGLVIRSPRG DLTLRDVQTV
     RAGDSAAPFD LVLLSCKAYS LDDAIASFAP FVGPSTLILP MLNGMRHLDV LRERFGAARV
     LGGLCVIAAT LDREQHIVHL NDTHGLSFGE PGGGDSPRMR ALADVLGNAG FDATLSDDIV
     ARMWDKWVFL ATLAASTSLF RGSVGDILSA PDGRRLLETM LDECSAIAAH NGYRPEPAAI
     ARMRQMVLTP SPLTASMLRD IENRARVEAD HVIGDLLARR DPDAGDALSL LRIAYNHLKT
     YEARVARERA AA
//
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