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Database: UniProt
Entry: F2LJS0_BURGS
LinkDB: F2LJS0_BURGS
Original site: F2LJS0_BURGS 
ID   F2LJS0_BURGS            Unreviewed;       296 AA.
AC   F2LJS0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE            EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN   OrderedLocusNames=bgla_2g06410 {ECO:0000313|EMBL:AEA63114.1};
OS   Burkholderia gladioli (strain BSR3).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA63114.1, ECO:0000313|Proteomes:UP000008316};
RN   [1] {ECO:0000313|EMBL:AEA63114.1, ECO:0000313|Proteomes:UP000008316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSR3 {ECO:0000313|EMBL:AEA63114.1,
RC   ECO:0000313|Proteomes:UP000008316};
RX   PubMed=21478339; DOI=10.1128/JB.00420-11;
RA   Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA   Moon J.S., Kim J., Hwang I.;
RT   "Complete genome sequence of Burkholderia gladioli BSR3.";
RL   J. Bacteriol. 193:3149-3149(2011).
CC   -!- FUNCTION: Catalyzes oxidation of L-threonate to 2-oxo-tetronate. Can
CC       use either NAD(+) or NADP(+) as cosubstrate, with a preference for
CC       NAD(+). {ECO:0000256|ARBA:ARBA00037062}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonate + NAD(+) = 2-dehydro-L-erythronate + H(+) + NADH;
CC         Xref=Rhea:RHEA:52548, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57561, ChEBI:CHEBI:57945, ChEBI:CHEBI:136669;
CC         EC=1.1.1.411; Evidence={ECO:0000256|ARBA:ARBA00036958};
CC   -!- SIMILARITY: Belongs to the HIBADH-related family. L-threonate
CC       dehydrogenase subfamily. {ECO:0000256|ARBA:ARBA00037979}.
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DR   EMBL; CP002600; AEA63114.1; -; Genomic_DNA.
DR   RefSeq; WP_013689446.1; NC_015376.1.
DR   AlphaFoldDB; F2LJS0; -.
DR   STRING; 999541.bgla_2g06410; -.
DR   KEGG; bgd:bgla_2g06410; -.
DR   eggNOG; COG2084; Bacteria.
DR   HOGENOM; CLU_035117_1_2_4; -.
DR   Proteomes; UP000008316; Chromosome 2.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
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; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR029154; HIBADH-like_NADP-bd.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43060:SF17; L-THREONATE DEHYDROGENASE; 1.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000103; HIBADH; 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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          4..161
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          167..286
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   296 AA;  30133 MW;  A297D1014CA2C0A1 CRC64;
     MSRQVGVIGL GAMGLGVARS LLRAGFRVHA CDLREDVLAA FAAEGGVPCA TPAELGARCE
     VLITLVVNAA QTEAVLFGEQ GAVPAMRAGS VVISSATVAP DFAVQLGARV EAAGLSMLDA
     PVSGGAARAA SGEMTVMSSG PAEAYAACED VLAAIAGKVY RLGAEHGAGS KVKIINQLLA
     GVHIAAAAEA MALGLREGVD ADALYEVITH SAGNSWMFEN RVPHILDGDY TPLSAVDIFV
     KDLGLVLDTA RRSKFPLPLS ATAHQMFMSA SSAGHGGEDD SAVIKTFPGI TLPPAR
//
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