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Database: UniProt
Entry: G0EUU0_CUPNN
LinkDB: G0EUU0_CUPNN
Original site: G0EUU0_CUPNN 
ID   G0EUU0_CUPNN            Unreviewed;       297 AA.
AC   G0EUU0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=L-threonate dehydrogenase {ECO:0000256|ARBA:ARBA00039407};
DE            EC=1.1.1.411 {ECO:0000256|ARBA:ARBA00038870};
GN   Name=mmsB1 {ECO:0000313|EMBL:AEI76926.1};
GN   OrderedLocusNames=CNE_1c15830 {ECO:0000313|EMBL:AEI76926.1};
OS   Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453
OS   / N-1) (Ralstonia eutropha).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1042878 {ECO:0000313|EMBL:AEI76926.1, ECO:0000313|Proteomes:UP000006798};
RN   [1] {ECO:0000313|EMBL:AEI76926.1, ECO:0000313|Proteomes:UP000006798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1
RC   {ECO:0000313|Proteomes:UP000006798};
RX   PubMed=21742890; DOI=10.1128/JB.05660-11;
RA   Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.;
RT   "Complete genome sequence of the type strain Cupriavidus necator N-1.";
RL   J. Bacteriol. 193:5017-5017(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; CP002877; AEI76926.1; -; Genomic_DNA.
DR   RefSeq; WP_013956560.1; NC_015726.1.
DR   AlphaFoldDB; G0EUU0; -.
DR   KEGG; cnc:CNE_1c15830; -.
DR   HOGENOM; CLU_035117_1_2_4; -.
DR   Proteomes; UP000006798; Chromosome 1.
DR   GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; 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};
KW   Oxidoreductase {ECO:0000313|EMBL:AEI76926.1}.
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   297 AA;  30430 MW;  7E3E5AEF8BA13CB4 CRC64;
     MSRNIGVIGL GAMGFGVAQS LLRAGFNVHA CDLRPEVLQR FADAGGVPCA SPAELGSRCD
     VVLTLVVNAQ QTEAVLFGAN GAAAAMEPGK LVIASATVPP GFAQALGRRL AEQGLLMLDA
     PVSGGAARAA SGEMTMMTSG PAEAYSLAED VLAAIAGKVY RLGAAHGAGS KVKIINQLLA
     GVHIAAAAEA MALGLREGVD PDALYDVITH SAGNSWMFEN RVPHILKGDY TPLSAVDIFV
     KDLGMVLDTA RQSKFPLPLS AAAHQMFMMA STAGHGGEDD SAVIKIFPGI ELPGKAE
//
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