ID LTND_ECOL6 Reviewed; 302 AA.
AC A0A0H2VA68;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=L-threonate dehydrogenase {ECO:0000303|PubMed:27402745};
DE EC=1.1.1.411 {ECO:0000269|PubMed:27402745};
GN Name=ltnD {ECO:0000303|PubMed:27402745};
GN Synonyms=ygbJ {ECO:0000312|EMBL:AAN81746.1};
GN OrderedLocusNames=c3297 {ECO:0000312|EMBL:AAN81746.1};
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=27402745; DOI=10.1073/pnas.1605546113;
RA Zhang X., Carter M.S., Vetting M.W., San Francisco B., Zhao S.,
RA Al-Obaidi N.F., Solbiati J.O., Thiaville J.J., de Crecy-Lagard V.,
RA Jacobson M.P., Almo S.C., Gerlt J.A.;
RT "Assignment of function to a domain of unknown function: DUF1537 is a new
RT kinase family in catabolic pathways for acid sugars.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E4161-E4169(2016).
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:0000269|PubMed:27402745}.
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:0000269|PubMed:27402745};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.16 mM for NAD(+) {ECO:0000269|PubMed:27402745};
CC KM=0.59 mM for NADP(+) {ECO:0000269|PubMed:27402745};
CC Note=kcat is 28 sec(-1) with NAD(+) as cosubstrate. kcat is 3.5 sec(-
CC 1) with NADP(+) as cosubstrate. {ECO:0000269|PubMed:27402745};
CC -!- SIMILARITY: Belongs to the HIBADH-related family. L-threonate
CC dehydrogenase subfamily. {ECO:0000305}.
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DR EMBL; AE014075; AAN81746.1; -; Genomic_DNA.
DR RefSeq; WP_000847998.1; NZ_CP051263.1.
DR AlphaFoldDB; A0A0H2VA68; -.
DR SMR; A0A0H2VA68; -.
DR STRING; 199310.c3297; -.
DR KEGG; ecc:c3297; -.
DR eggNOG; COG2084; Bacteria.
DR HOGENOM; CLU_035117_1_2_6; -.
DR Proteomes; UP000001410; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; 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.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..302
FT /note="L-threonate dehydrogenase"
FT /id="PRO_0000439748"
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; 30706 MW; 536848758AC4FF4C CRC64;
MKTGSEFHVG IVGLGSMGMG AALSCVRAGL STWGADLNSN ACATLKEAGA CGVSDNAATF
AEKLDALLVL VVNATQVKQV LFGEKGVAQH LKPGTAVMVS STIASADAQE IATALAGFGL
EMLDAPVSGG AVKAANGEMT VMASGSDIAF ERLAPVLEAV AGKVYRIGSE PGLGSTVKII
HQLLAGVHIA AGAEAMALAA RAGIPLDVMY DVVTNAAGNS WMFENRMRHV VDGDYTPHSA
VDIFVKDLGL VADTAKALHF PLPLASTALN MFTSASNAGY GKEDDSAVIK IFSGITLPGA
KS
//
