ID TDH_SHEB5 Reviewed; 341 AA. AC A3CYN0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 1. DT 04-NOV-2026, entry version 106. 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=Sbal_0057; OS Shewanella baltica (strain OS155 / ATCC BAA-1091). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Alteromonadales; Shewanellaceae; Shewanella. OX NCBI_TaxID=325240; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OS155 / ATCC BAA-1091; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I., RA Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.; RT "Complete sequence of chromosome of Shewanella baltica OS155."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. 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; CP000563; ABN59593.1; -; Genomic_DNA. DR RefSeq; WP_006079369.1; NC_009052.1. DR SMR; A3CYN0; -. DR STRING; 325240.Sbal_0057; -. DR GeneID; 11775065; -. DR KEGG; sbl:Sbal_0057; -. DR HOGENOM; CLU_026673_11_0_6; -. DR OMA; AADCIGN; -. DR OrthoDB; 9773078at2; -. DR UniPathway; UPA00046; UER00505. 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 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 NCBIfam; NF003808; tdh; 1. DR NCBIfam; TIGR00692; tdh; 1. DR PROSITE; PS00059; ADH_ZINC; 1. 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 Proteomes; UP000001557; Chromosome. DR AlphaFoldDB; A3CYN0; -. PE 3: Inferred from homology; KW Cytoplasm; Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1..341 FT /note="L-threonine 3-dehydrogenase" FT /id="PRO_1000051652" 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; 37179 MW; 50217051CF41145E CRC64; MKALSKLKAE KGIWLVDAPK PVMGHNDLLI KIKKTAICGT DMHIYNWDEW SQKTIPVPMV VGHEYVGEVV DIGQEVRGFK IGDRVSGEGH ITCGHCRNCR AGRTHLCRNT SGVGVNREGS FAEYLVIPAF NAFKIPDDIS DDLASIFDPF GNAVHTALSF DLVGEDVLIT GAGPIGIMAA AVCRHVGARH VVITDVNEYR LELARKMGAT RAVNVSKESL KDVMKELGMT EGFDVGLEMS GVPSAFHAML DTMNHGGKVA MLGIPGGEMA IDWSKVIFKG LVIKGIYGRE MFETWYKMAS LIQSGLDISP IITHHFKIDD FQQGFDAMGS GQSGKVILSW D //