LTND_ECOLI
ID LTND_ECOLI Reviewed; 302 AA.
AC Q46888; Q2MA93;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000250|UniProtKB:A0A0H2VA68};
DE EC=1.1.1.411 {ECO:0000250|UniProtKB:A0A0H2VA68};
GN Name=ltnD {ECO:0000250|UniProtKB:A0A0H2VA68}; Synonyms=ygbJ;
GN OrderedLocusNames=b2736, JW2706;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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:0000250|UniProtKB:A0A0H2VA68}.
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:0000250|UniProtKB:A0A0H2VA68};
CC -!- SIMILARITY: Belongs to the HIBADH-related family. L-threonate
CC dehydrogenase subfamily. {ECO:0000305}.
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DR EMBL; U29579; AAA69246.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75778.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76813.1; -; Genomic_DNA.
DR PIR; D65054; D65054.
DR RefSeq; NP_417216.1; NC_000913.3.
DR RefSeq; WP_000848004.1; NZ_LN832404.1.
DR AlphaFoldDB; Q46888; -.
DR SMR; Q46888; -.
DR BioGRID; 4261443; 17.
DR IntAct; Q46888; 3.
DR STRING; 511145.b2736; -.
DR PaxDb; Q46888; -.
DR PRIDE; Q46888; -.
DR EnsemblBacteria; AAC75778; AAC75778; b2736.
DR EnsemblBacteria; BAE76813; BAE76813; BAE76813.
DR GeneID; 947200; -.
DR KEGG; ecj:JW2706; -.
DR KEGG; eco:b2736; -.
DR PATRIC; fig|1411691.4.peg.4004; -.
DR EchoBASE; EB2907; -.
DR eggNOG; COG2084; Bacteria.
DR HOGENOM; CLU_035117_1_2_6; -.
DR InParanoid; Q46888; -.
DR OMA; QMFMQAS; -.
DR PhylomeDB; Q46888; -.
DR BioCyc; EcoCyc:G7417-MON; -.
DR PRO; PR:Q46888; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR015815; HIBADH-related.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029154; NADP-bd.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000103; HIBADH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..302
FT /note="L-threonate dehydrogenase"
FT /id="PRO_0000173062"
FT ACT_SITE 178
FT /evidence="ECO:0000250|UniProtKB:Q9I5I6"
FT BINDING 7..35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
FT BINDING 102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
FT BINDING 246
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
SQ SEQUENCE 302 AA; 30751 MW; 09E94256EDDFC26C CRC64;
MKTGSEFHVG IVGLGSMGMG AALSYVRAGL STWGADLNSN ACATLKEAGA CGVSDNAATF
AEKLDALLVL VVNAAQVKQV LFGETGVAQH LKPGTAVMVS STIASADAQE IATALAGFDL
EMLDAPVSGG AVKAANGEMT VMASGSDIAF ERLAPVLEAV AGKVYRIGAE PGLGSTVKII
HQLLAGVHIA AGAEAMALAA RAGIPLDVMY DVVTNAAGNS WMFENRMRHV VDGDYTPHSA
VDIFVKDLGL VADTAKALHF PLPLASTALN MFTSASNAGY GKEDDSAVIK IFSGITLPGA
KS
