LTND_CUPNH
ID LTND_CUPNH Reviewed; 297 AA.
AC Q0KBC7;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 OrderedLocusNames=H16_A1562 {ECO:0000312|EMBL:CAJ92694.1};
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
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=0.35 mM for NAD(+) {ECO:0000269|PubMed:27402745};
CC KM=0.30 mM for NADP(+) {ECO:0000269|PubMed:27402745};
CC Note=kcat is 29 sec(-1) with NAD(+) as cosubstrate. kcat is 2.2 sec(-
CC 1) with NADP(+) as cosubstrate. {ECO:0000269|PubMed:27402745};
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is unable to use L-threonate as a
CC carbon source. {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; AM260479; CAJ92694.1; -; Genomic_DNA.
DR RefSeq; WP_011615152.1; NZ_CP039287.1.
DR AlphaFoldDB; Q0KBC7; -.
DR SMR; Q0KBC7; -.
DR STRING; 381666.H16_A1562; -.
DR EnsemblBacteria; CAJ92694; CAJ92694; H16_A1562.
DR GeneID; 57643661; -.
DR KEGG; reh:H16_A1562; -.
DR PATRIC; fig|381666.6.peg.1947; -.
DR eggNOG; COG2084; Bacteria.
DR HOGENOM; CLU_035117_1_2_4; -.
DR OMA; QMFMQAS; -.
DR OrthoDB; 1194694at2; -.
DR BRENDA; 1.1.1.411; 231.
DR Proteomes; UP000008210; Chromosome 1.
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:UniProtKB-KW.
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; 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.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..297
FT /note="L-threonate dehydrogenase"
FT /id="PRO_0000439747"
FT ACT_SITE 173
FT /evidence="ECO:0000250|UniProtKB:Q9I5I6"
FT BINDING 3..31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
FT BINDING 241
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
SQ SEQUENCE 297 AA; 30439 MW; 83078DF65FB9B09D CRC64;
MSRNIGVIGL GAMGFGVAQS LLRAGFNVHA CDLRPEVLQR FADAGGVPCA SPAELGSRCD
VVLTLVVNAQ QTEAVLFGAN GAAAAMQPGK LVIASATVPP GFAEALGRRL AEQGLLMLDA
PVSGGAARAA SGEMTMMTSG PAEAYSLAED VLAAIAGKVY RLGAAHGAGS KVKIINQLLA
GVHIAAAAEA MALGLREGVD PDALYDVITH SAGNSWMFEN RVPHILKGDY TPLSAVDIFV
KDLGMVLDTA RHSKFPLPLS AAAHQMFMMA STAGHGGEDD SAVIKIFPGI ELPGKAE
