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Database: UniProt
Entry: A0A2N7X084_9BURK
LinkDB: A0A2N7X084_9BURK
Original site: A0A2N7X084_9BURK 
ID   A0A2N7X084_9BURK        Unreviewed;       338 AA.
AC   A0A2N7X084;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
DE            EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN   ORFNames=C0Z20_21105 {ECO:0000313|EMBL:PMS34895.1};
OS   Trinickia symbiotica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Trinickia.
OX   NCBI_TaxID=863227 {ECO:0000313|EMBL:PMS34895.1, ECO:0000313|Proteomes:UP000235777};
RN   [1] {ECO:0000313|EMBL:PMS34895.1, ECO:0000313|Proteomes:UP000235777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPY 581 {ECO:0000313|EMBL:PMS34895.1,
RC   ECO:0000313|Proteomes:UP000235777};
RA   Estrada-de los Santos P., Palmer M., Chavez-Ramirez B., Beukes C.,
RA   Steenkamp E.T., Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M.,
RA   Gross E., Simon M.F., Bueno dos Reis Junior F., Poole P.S., Venter S.N.,
RA   James E.K.;
RT   "Whole genome analyses suggest that Burkholderia sensu lato contains two
RT   further novel genera in the rhizoxinica-symbiotica group Mycetohabitans
RT   gen. nov., and Trinickia gen. nov.: implications for the evolution of
RT   diazotrophy and nodulation in the Burkholderiaceae.";
RL   Submitted (JAN-2018) 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:PMS34895.1}.
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DR   EMBL; PNYC01000014; PMS34895.1; -; Genomic_DNA.
DR   RefSeq; WP_018443464.1; NZ_PTIR01000006.1.
DR   AlphaFoldDB; A0A2N7X084; -.
DR   STRING; 863227.GCA_000373005_04851; -.
DR   OrthoDB; 9796561at2; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000235777; 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; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR21708:SF42; 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   4: Predicted;
KW   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235777}.
FT   DOMAIN          15..179
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          208..329
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   338 AA;  35221 MW;  FCF6AE3A8BF51688 CRC64;
     MSEESEAPDR VSHTAVIGAG AIGGLMAAAL ARAGHEVSVL ARGRTLDAIR EHGVRVIDGN
     GQTSSIMLRA SDDAAELGAQ DFVVIALKAQ TLPAIAASLR PLVDERTTIV SAMNGLPWWF
     LDGTTTPLAG QRIDAVDPEG VVSRALPAPR ALGCVVHLSV STDAPGIVRR GLGNRLIVGA
     AYAAHAPIAR TFAAALGAGG FDVQAVDDIR TEIWAKLWGN MNMNPLSALT GSTADRLLDD
     PFTHALVLRM MEEAEAIGAC LGLSTGMSAA ERVAVTRKLG AFKTSMLQDM EAGRPLEIDP
     ILGVFPELGR KLGVPTPFCD AVLGLLRQRA ANSGLTIA
//
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