ID A0A0G3AC55_9ACTN Unreviewed; 342 AA. AC A0A0G3AC55; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 11-DEC-2019, entry version 22. DE RecName: Full=L-threonine 3-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00368434}; 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 Produces RT the Nucleoside Antibiotic Sinefungin."; RL Genome Announc. 3:e00715-15(2015). CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- CC amino-3-ketobutyrate. {ECO:0000256|HAMAP-Rule:MF_00627, CC ECO:0000256|SAAS:SAAS00527196}. 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 ECO:0000256|SAAS:SAAS01122051}; 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, ECO:0000256|SAAS:SAAS00321706}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00627, CC ECO:0000256|SAAS:SAAS00367962}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00627, CC ECO:0000256|SAAS:SAAS00322478}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {ECO:0000256|HAMAP-Rule:MF_00627, CC ECO:0000256|SAAS:SAAS00571236}. 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00321720}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00627, KW ECO:0000256|SAAS:SAAS00326561}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00321751}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00627, KW ECO:0000256|SAAS:SAAS00326557, ECO:0000313|EMBL:AKJ09365.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000035366}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00326562}. FT DOMAIN 26..133 FT /note="ADH_N" FT /evidence="ECO:0000259|Pfam:PF08240" FT DOMAIN 174..298 FT /note="ADH_zinc_N" FT /evidence="ECO:0000259|Pfam:PF00107" FT NP_BIND 262..264 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT NP_BIND 286..287 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" 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 METAL 38 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 63 FT /note="Zinc 1; via tele nitrogen; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 64 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 93 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 96 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 99 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 107 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 175 FT /note="NAD; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 195 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 200 FT /note="NAD" 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 //