ID TDH_ECOLU Reviewed; 341 AA. AC B7NES3; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 02-SEP-2026, entry version 91. DE RecName: Full=L-threonine 3-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00627}; DE Short=TDH {ECO:0000255|HAMAP-Rule:MF_00627}; DE EC=1.1.1.103 {ECO:0000255|HAMAP-Rule:MF_00627}; GN Name=tdh {ECO:0000255|HAMAP-Rule:MF_00627}; GN OrderedLocusNames=ECUMN_4133; OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585056; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UMN026 / ExPEC; RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E., RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- CC amino-3-ketobutyrate. {ECO:0000255|HAMAP-Rule:MF_00627}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + NADH + CC H(+); 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; Evidence={ECO:0000255|HAMAP-Rule:MF_00627}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00627}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00627}; CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo- CC reductase pathway; glycine from L-threonine: step 1/2. CC {ECO:0000255|HAMAP-Rule:MF_00627}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00627}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00627}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {ECO:0000255|HAMAP-Rule:MF_00627}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU928163; CAR15274.1; -; Genomic_DNA. DR RefSeq; WP_000646019.1; NC_011751.1. DR AlphaFoldDB; B7NES3; -. DR SMR; B7NES3; -. DR STRING; 585056.ECUMN_4133; -. DR KEGG; eum:ECUMN_4133; -. DR PATRIC; fig|585056.7.peg.4308; -. DR HOGENOM; CLU_026673_11_0_6; -. DR UniPathway; UPA00046; UER00505. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006567; P:L-threonine catabolic process; IEA:UniProtKB-UniRule. DR FunFam; 3.40.50.720:FF:000059; L-threonine 3-dehydrogenase; 1. DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00627; Thr_dehydrog; 1. DR InterPro; IPR013149; ADH-like_C. DR InterPro; IPR013154; ADH-like_N. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR020843; ER. DR InterPro; IPR011032; GroES-like_sf. DR InterPro; IPR004627; L-Threonine_3-DHase. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR050129; Zn_alcohol_dh. DR NCBIfam; NF003808; PRK05396.1; 1. DR NCBIfam; TIGR00692; tdh; 1. DR PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1. DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SMART; SM00829; PKS_ER; 1. DR SUPFAM; SSF50129; GroES-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 3: Inferred from homology; KW Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc. FT CHAIN 1..341 FT /note="L-threonine 3-dehydrogenase" FT /id="PRO_1000130549" FT ACT_SITE 40 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT ACT_SITE 43 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 38 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 63 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 64 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 93 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 96 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 99 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 107 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 175 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 195 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 200 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 262..264 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 286..287 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT SITE 148 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 /evidence="ECO:0000255|HAMAP-Rule:MF_00627" SQ SEQUENCE 341 AA; 37241 MW; AAB29FDEC279BE8E CRC64; MKALSKLKAE EGIWMTDVPV PELGHNDLLI KIRKTAICGT DVHIYNWDEW SQKTIPVPMV VGHEYVGEVV GIGQEVKGFK IGDRVSGEGH ITCGHCRNCR GGRTHLCRNT IGVGVNRPGC FAEYLVIPAF NAFKIPDNIS DDLASIFDPF GNAVHTALSF DLVGEDVLVS GAGPIGIMAA AVAKHVGARN VVITDVNEYR LELARKMGVT RAVNVAKENL NDVMAELGMT EGFDVGLEMS GAPPAFRTML DTMNHGGRIA MLGIPPSDMS IDWTKVIFKG LFIKGIYGRE MFETWYKMAA LIQSGLDLSP IITHRFSIDD FQKGFDAMRS GQSGKVILSW D //