ID A0A0G3AC55_9ACTN Unreviewed; 342 AA. AC A0A0G3AC55; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 22-NOV-2017, entry version 17. DE RecName: Full=L-threonine 3-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00678662}; 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; Actinobacteria; Streptomycetales; Streptomycetaceae; OC 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 RT Produces the Nucleoside Antibiotic Sinefungin."; RL Genome Announc. 3:e00715-15(2015). CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine CC to 2-amino-3-ketobutyrate. {ECO:0000256|HAMAP-Rule:MF_00627, CC ECO:0000256|SAAS:SAAS00678731}. CC -!- CATALYTIC ACTIVITY: L-threonine + NAD(+) = L-2-amino-3- CC oxobutanoate + NADH. {ECO:0000256|HAMAP-Rule:MF_00627, CC ECO:0000256|SAAS:SAAS00678774}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC 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 CC oxydo-reductase pathway; glycine from L-threonine: step 1/2. CC {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00678706}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00627, CC ECO:0000256|SAAS:SAAS00678730}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00627, CC ECO:0000256|SAAS:SAAS00678758}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {ECO:0000256|HAMAP-Rule:MF_00627, CC ECO:0000256|SAAS:SAAS00682228}. 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 EnsemblBacteria; AKJ09365; AKJ09365; 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 HAMAP; MF_00627; Thr_dehydrog; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_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 Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; SSF50129; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00692; tdh; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000035366}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00627, KW ECO:0000256|SAAS:SAAS00678797}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00627, KW ECO:0000256|SAAS:SAAS00682216}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00678712}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00627, KW ECO:0000256|SAAS:SAAS00682222, ECO:0000313|EMBL:AKJ09365.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000035366}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00682217}. FT DOMAIN 26 133 ADH_N. {ECO:0000259|Pfam:PF08240}. FT DOMAIN 174 301 ADH_zinc_N. {ECO:0000259|Pfam:PF00107}. FT NP_BIND 262 264 NAD. {ECO:0000256|HAMAP-Rule:MF_00627}. FT NP_BIND 286 287 NAD. {ECO:0000256|HAMAP-Rule:MF_00627}. FT ACT_SITE 40 40 Charge relay system. {ECO:0000256|HAMAP- FT Rule:MF_00627}. FT ACT_SITE 43 43 Charge relay system. {ECO:0000256|HAMAP- FT Rule:MF_00627}. FT METAL 38 38 Zinc 1; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00627}. FT METAL 63 63 Zinc 1; via tele nitrogen; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_00627}. FT METAL 64 64 Zinc 1; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00627}. FT METAL 93 93 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_00627}. FT METAL 96 96 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_00627}. FT METAL 99 99 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_00627}. FT METAL 107 107 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_00627}. FT BINDING 175 175 NAD; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00627}. FT BINDING 195 195 NAD. {ECO:0000256|HAMAP-Rule:MF_00627}. FT BINDING 200 200 NAD. {ECO:0000256|HAMAP-Rule:MF_00627}. FT SITE 148 148 Important for catalytic activity for the FT proton relay mechanism but does not FT participate directly in the coordination FT of zinc atom. {ECO:0000256|HAMAP-Rule: FT 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 //