ID TDH_PHOLL Reviewed; 341 AA. AC Q7MY48; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 02-SEP-2026, entry version 140. 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}; OrderedLocusNames=plu4845; OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / OS TT01) (Photorhabdus luminescens subsp. laumondii). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Morganellaceae; Photorhabdus. OX NCBI_TaxID=243265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15139 / CIP 105565 / TT01; RX PubMed=14528314; DOI=10.1038/nbt886; RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C., RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M., RA Glaser P., Boemare N., Danchin A., Kunst F.; RT "The genome sequence of the entomopathogenic bacterium Photorhabdus RT luminescens."; RL Nat. Biotechnol. 21:1307-1313(2003). 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; BX571875; CAE17217.1; -; Genomic_DNA. DR RefSeq; WP_011148903.1; NC_005126.1. DR AlphaFoldDB; Q7MY48; -. DR SMR; Q7MY48; -. DR STRING; 243265.plu4845; -. DR GeneID; 48851073; -. DR KEGG; plu:plu4845; -. DR eggNOG; COG1063; Bacteria. DR HOGENOM; CLU_026673_11_0_6; -. DR OrthoDB; 9773078at2; -. DR UniPathway; UPA00046; UER00505. DR Proteomes; UP000002514; Chromosome. 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; Reference proteome; Zinc. FT CHAIN 1..341 FT /note="L-threonine 3-dehydrogenase" FT /id="PRO_0000160847" 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; 37375 MW; 82AF74B8587B875D CRC64; MKALSKLKAE EGIWMIDVPE PELGHNDVMI KIRKTAICGT DVHIYNWDDW SQKTIPVPMV VGHEYVGEVV AIGQEVKGFK IGDRVSGEGH ITCGYCRNCR GGRTHLCRNT IGVGVNRAGC FAQYLVIPAF NAFKIPDNIS DELAAIFDPF GNAVHTALSF DLVGEDVLVS GAGPIGIMAA AVCKHVGARH VVITDVNEYR LELARKMGVT RAVNVSQENL TDVMAELGMT EGFDVGLEMS GAPAAFRTLL NTMNHGGRVA LLGIPPSDMA IDWNQVIFKG LFIKGIYGRE MFETWYKMAT LIQSGLDLTP IITHRFSIDD FQKGFDIMRS GQSGKVILNW D //