ID TDH_ANADF Reviewed; 343 AA. AC A7HEI5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 04-NOV-2026, entry version 104. 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=Anae109_2931; OS Anaeromyxobacter sp. (strain Fw109-5). OC Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=404589; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fw109-5; RX PubMed=25614562; DOI=10.1128/genomea.01449-14; RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T., RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C., RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J., RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A., RA Loeffler F.E., Fields M.W.; RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic, RT metal-reducing bacterium isolated from a contaminated subsurface RT environment."; RL Genome Announc. 3:0-0(2015). 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; CP000769; ABS27131.1; -; Genomic_DNA. DR RefSeq; WP_012097735.1; NC_009675.1. DR AlphaFoldDB; A7HEI5; -. DR SMR; A7HEI5; -. DR STRING; 404589.Anae109_2931; -. DR KEGG; afw:Anae109_2931; -. DR eggNOG; COG1063; Bacteria. DR HOGENOM; CLU_026673_11_0_7; -. DR OMA; AADCIGN; -. DR OrthoDB; 5484143at2; -. 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 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; tdh; 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..343 FT /note="L-threonine 3-dehydrogenase" FT /id="PRO_1000051615" FT ACT_SITE 41 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT ACT_SITE 44 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 39 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 65 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 94 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 108 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 176 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 196 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 201 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 263..265 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT BINDING 287..288 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00627" FT SITE 149 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 343 AA; 37693 MW; 254FD650E370FB10 CRC64; MKALVKSRRA EGIWMVHDAP VPEVGVHDVR IRVRKSAICG TDVHIYNWDE WSQRTIPVPM IVGHEYVGVV DAVGGEVEAF HPGDRVSGEG HVTCGFCRNC RAGRRHLCRH TIGVGVNRPG SFAEYVVIPA DNVYRIPDDI PDEVAAIFDP YGNATHTALS FELVGEDVLV TGAGPIGVMA VSIARHVGAR HVVVTDVNDY RLGLARRMGA TRAVNVARED LRAVMKDLGM KEGFDVGLEM SGNGRAFRQM LEAMNHGAKV ALLGIMPGEE AIDWSQVVFK GLVLKGIYGR EMYETWYKMV AMLQSGLDIS PVITHRFPID EFQQGFDVMR SGQSGKVVLD WGT //