ID A0A0L8M953_9ACTN Unreviewed; 342 AA. AC A0A0L8M953; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-NOV-2018, entry version 18. DE RecName: Full=L-threonine 3-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00321739}; 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:KOG46915.1}; GN ORFNames=ADK74_11460 {ECO:0000313|EMBL:KOG46915.1}; OS Streptomyces decoyicus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=249567 {ECO:0000313|EMBL:KOG46915.1, ECO:0000313|Proteomes:UP000037606}; RN [1] {ECO:0000313|Proteomes:UP000037606} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL 2666 {ECO:0000313|Proteomes:UP000037606}; RG Consortium for Microbial Forensics and Genomics (microFORGE); RA Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U., RA Blagden T., Winegar R.A.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. 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:SAAS00527196}. CC -!- CATALYTIC ACTIVITY: L-threonine + NAD(+) = L-2-amino-3- CC oxobutanoate + NADH. {ECO:0000256|HAMAP-Rule:MF_00627, CC ECO:0000256|SAAS:SAAS00321698}. 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:SAAS00368190}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00627, CC ECO:0000256|SAAS:SAAS00321708}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00627, CC ECO:0000256|SAAS:SAAS00321761}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {ECO:0000256|HAMAP-Rule:MF_00627, CC ECO:0000256|SAAS:SAAS00571236}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KOG46915.1}. 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; LGUU01000115; KOG46915.1; -; Genomic_DNA. DR RefSeq; WP_030083208.1; NZ_LGUU01000115.1. DR EnsemblBacteria; KOG46915; KOG46915; ADK74_11460. DR PATRIC; fig|249567.6.peg.2470; -. DR UniPathway; UPA00046; UER00505. DR Proteomes; UP000037606; Unassembled WGS sequence. 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 PROSITE; PS00059; ADH_ZINC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000037606}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00627, KW ECO:0000256|SAAS:SAAS00444222}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00627, KW ECO:0000256|SAAS:SAAS00460938}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00444455}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00627, KW ECO:0000256|SAAS:SAAS00460922, ECO:0000313|EMBL:KOG46915.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000037606}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00460926}. FT DOMAIN 25 133 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; 36452 MW; 5EBC59BEF056238A CRC64; MKALVKQKAE PGLWLMDVPE PAVGPGDVLI KVLRTGICGT DLHIRAWDGW AQQAVATPMT IGHEFVGEVV ETGRDVADIK AGDLVSGEGH LVCGKCRNCQ AGRRHLCRAT VGLGVGRDGA FAEYVALPAA NVWVHRVPVD LDIAAVFDPF GNAVHTALSF PLVGEDVLIT GAGPIGIMAA AVARHAGARN VVITDVSEPR LELARKVGVS LALNVAEAKI ADGQRELGLR EGFDIGLEMS GRPEAMRDMI ANMTHGGRIA VLGLPSEQFP VDWSRIVTSM ITIKGIYGRE MFETWYAMSV LLEGGLDLAP VITGRYSHQD FDAAFDDAAS GRSGKIILDW TA //