AC MF_00627; DC Protein; auto TR HAMAP; MF_00627; -; 1; level=0 XX Names: Thr_dehydrog XX ID TDH DE RecName: Full=L-threonine 3-dehydrogenase; DE Short=TDH; DE EC=1.1.1.103; GN Name=tdh; XX CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- CC amino-3-ketobutyrate. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) + CC NADH; Xref=Rhea:RHEA:13161, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57926, ChEBI:CHEBI:57945, ChEBI:CHEBI:78948; CC EC=1.1.1.103; case and CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 2 Zn(2+) ions per subunit.; end case case and not CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 Zn(2+) ion per subunit.; end case CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo- CC reductase pathway; glycine from L-threonine: step 1/2. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. XX DR Pfam; PF08240; ADH_N; 1; trigger=no DR Pfam; PF00107; ADH_zinc_N; 1; trigger=no DR NCBIfam; TIGR00692; tdh; 1; trigger=no DR PROSITE; PS00059; ADH_ZINC; 1; trigger=no XX KW Cytoplasm KW Oxidoreductase case or KW Zinc KW Metal-binding end case KW NAD XX GO GO:0008743; F:L-threonine 3-dehydrogenase activity case or GO GO:0008270; F:zinc ion binding end case GO GO:0006567; P:threonine catabolic process GO GO:0005737; C:cytoplasm XX FT From: TDH_PYRHO (O58389) FT BINDING 266..268 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: L-x-[LIT] FT BINDING 291..292 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: [IV]-[TY] FT ACT_SITE 44 FT /note="Charge relay system" FT Condition: T FT ACT_SITE 47 FT /note="Charge relay system" FT Condition: H FT BINDING 42 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT Group: 1; Condition: C FT BINDING 67 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 68 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT Group: 1; Condition: E FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Group: 2; Condition: C FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Group: 2; Condition: C FT BINDING 103 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Group: 2; Condition: C FT BINDING 111 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Group: 2; Condition: C FT BINDING 179 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: [LIV] FT BINDING 199 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: [ED] FT BINDING 204 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: R FT SITE 152 FT /note="Important for catalytic activity for the proton FT relay mechanism but does not participate directly in the FT coordination of zinc atom" FT Condition: [DE] XX Size: 340-361; Related: None; Template: P07913; O58389; Q5JI69; Q8U259; Q5SKS4; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.29 2023/06/01 //