ID A0A0G3AC55_9ACTN Unreviewed; 342 AA. AC A0A0G3AC55; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 27-MAR-2024, entry version 41. DE RecName: Full=L-threonine 3-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00627}; DE Short=TDH {ECO:0000256|HAMAP-Rule:MF_00627}; DE EC=1.1.1.103 {ECO:0000256|HAMAP-Rule:MF_00627}; GN Name=tdh {ECO:0000256|HAMAP-Rule:MF_00627, GN ECO:0000313|EMBL:AKJ09365.1}; GN ORFNames=ABB07_04830 {ECO:0000313|EMBL:AKJ09365.1}; OS Streptomyces incarnatus. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ09365.1, ECO:0000313|Proteomes:UP000035366}; RN [1] {ECO:0000313|EMBL:AKJ09365.1, ECO:0000313|Proteomes:UP000035366} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366}; RX PubMed=26159526; RA Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K., RA Tamura T.; RT "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces RT the Nucleoside Antibiotic Sinefungin."; RL Genome Announc. 3:e00715-e00715(2015). CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- CC amino-3-ketobutyrate. {ECO:0000256|HAMAP-Rule:MF_00627}. CC -!- FUNCTION: Catalyzes the oxidation of 2-deoxy-scyllo-inosamine (DOIA) CC with NAD(+) or NADP(+), forming 3-amino-2,3-dideoxy-scyllo-inosose CC (amino-DOI). {ECO:0000256|ARBA:ARBA00037678}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-deoxy-scyllo-inosamine + NAD(+) = 3-amino-2,3-dideoxy- CC scyllo-inosose + H(+) + NADH; Xref=Rhea:RHEA:33883, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:65002, ChEBI:CHEBI:65003; EC=1.1.1.329; CC Evidence={ECO:0000256|ARBA:ARBA00036792}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-deoxy-scyllo-inosamine + NADP(+) = 3-amino-2,3-dideoxy- CC scyllo-inosose + H(+) + NADPH; Xref=Rhea:RHEA:33879, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:65002, ChEBI:CHEBI:65003; EC=1.1.1.329; CC Evidence={ECO:0000256|ARBA:ARBA00036830}; 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; Evidence={ECO:0000256|HAMAP-Rule:MF_00627}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00627}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00627}. CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; 2-deoxystreptamine CC biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 3/4. CC {ECO:0000256|ARBA:ARBA00037908}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00627}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00627}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. DOIA dehydrogenase subfamily. {ECO:0000256|ARBA:ARBA00038004}. 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; CP011497; AKJ09365.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0G3AC55; -. DR STRING; 665007.ABB07_04830; -. DR PATRIC; fig|665007.5.peg.1052; -. DR UniPathway; UPA00046; UER00505. DR Proteomes; UP000035366; 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:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniPathway. 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; IPR011032; GroES-like_sf. DR InterPro; IPR004627; L-Threonine_3-DHase. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. 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 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00627}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00627}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00627}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00627}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00627}. FT DOMAIN 26..133 FT /note="Alcohol dehydrogenase-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF08240" FT DOMAIN 174..300 FT /note="Alcohol dehydrogenase-like C-terminal" FT /evidence="ECO:0000259|Pfam:PF00107" FT ACT_SITE 40 FT /note="Charge relay system" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT ACT_SITE 43 FT /note="Charge relay system" FT /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00627" FT BINDING 93 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 96 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 99 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 107 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 175 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 195 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 200 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 262..264 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 286..287 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_00627" SQ SEQUENCE 342 AA; 36746 MW; A8083FD262CA2DD9 CRC64; MKALVKEKAE PGLWLTDVPE PEIGPADVLI KVIRTGICGT DLHIRAWDGW AQQAIRTPLV LGHEFVGQVV ETGRDVTEIR IGDRVSGEGH LVCGKCRNCL AGRRHLCRAT VGLGVGRDGA FAEYVALPAS NVWVHRVPVD LDVAAIFDPF GNAVHTALSF PLVGEDVLIT GAGPIGLMAA AVARHAGARN VVVTDVSEER LELARKIGVS LALNVAETTI ADGQRELGLR EGFDIGLEMS GRPEAMRDMI ANMTHGGRIA MLGLPAQEFP VDWARIVTSM ITIKGIYGRE MYETWYAMSV LLEGGLDLAP VITGRYGYRD FEAAFADAAS GKGGKVILDW TV //