ID A0A0M8X8V6_9ACTN Unreviewed; 339 AA. AC A0A0M8X8V6; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 08-MAY-2019, entry version 19. 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:KOV99183.1}; GN ORFNames=ADK65_19745 {ECO:0000313|EMBL:KOV99183.1}; OS Streptomyces sp. NRRL B-1140. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1415549 {ECO:0000313|EMBL:KOV99183.1, ECO:0000313|Proteomes:UP000037734}; RN [1] {ECO:0000313|EMBL:KOV99183.1, ECO:0000313|Proteomes:UP000037734} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL B-1140 {ECO:0000313|EMBL:KOV99183.1, RC ECO:0000313|Proteomes:UP000037734}; RA Noorani M.; 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: CC Reaction=L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) CC + NADH; Xref=Rhea:RHEA:13161, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57926, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:78948; EC=1.1.1.103; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00627, ECO:0000256|SAAS:SAAS01122051}; 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: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 -!- 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:KOV99183.1}. 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; LGEA01000099; KOV99183.1; -; Genomic_DNA. DR EnsemblBacteria; KOV99183; KOV99183; ADK65_19745. DR PATRIC; fig|1415549.3.peg.4108; -. DR UniPathway; UPA00046; UER00505. DR Proteomes; UP000037734; 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 InterPro; IPR020843; PKS_ER. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SMART; SM00829; PKS_ER; 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:UP000037734}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00627, KW 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:KOV99183.1}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00326562}. FT DOMAIN 9 335 PKS_ER. {ECO:0000259|SMART:SM00829}. FT NP_BIND 259 261 NAD. {ECO:0000256|HAMAP-Rule:MF_00627}. FT NP_BIND 283 284 NAD. {ECO:0000256|HAMAP-Rule:MF_00627}. FT ACT_SITE 37 37 Charge relay system. {ECO:0000256|HAMAP- FT Rule:MF_00627}. FT ACT_SITE 40 40 Charge relay system. {ECO:0000256|HAMAP- FT Rule:MF_00627}. FT METAL 35 35 Zinc 1; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00627}. FT METAL 60 60 Zinc 1; via tele nitrogen; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_00627}. FT METAL 61 61 Zinc 1; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00627}. FT METAL 90 90 Zinc 2. {ECO:0000256|HAMAP-Rule: FT 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 104 104 Zinc 2. {ECO:0000256|HAMAP-Rule: FT MF_00627}. FT BINDING 172 172 NAD; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00627}. FT BINDING 192 192 NAD. {ECO:0000256|HAMAP-Rule:MF_00627}. FT BINDING 197 197 NAD. {ECO:0000256|HAMAP-Rule:MF_00627}. FT SITE 145 145 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 339 AA; 36241 MW; 0C80869BA11E2284 CRC64; MVKQKAEPGL WLADVPEPTV GPKDVLIRVL RTGICGTDLH IRAWDGWARQ AISTPLVVGH EFVGEVVETG RDVTDISVGD RVSGEGHLVC GKCRNCLAGR RHLCRATVGL GVGRDGAFAE YVALPAGNVW VHRVPVDLDV AAIFDPFGNA VHTALSFPLV GEDVLVTGAG PIGLMAAAVA KHAGARNVVI TDVSEERLEL ARKIGVSLAL NVSEATIADG QRTLGLREGF DIGLEMSGRP EAMRDMIANM THGGRIAMLG LPAQEFPVDW ARVVTSMITI KGIYGREMFE TWYAMSVLLE AGLDLAPVIT GRYSHRDFEA AFEDAASGRG GKVILDWTA //