ID A0A0M8X8V6_9ACTN Unreviewed; 339 AA. AC A0A0M8X8V6; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 17-JUN-2020, 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, ECO:0000256|SAAS:SAAS00322204}; 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 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:SAAS00322494}. 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 EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00322287}; 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:SAAS00322183}; 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 FT /note="PKS_ER" FT /evidence="ECO:0000259|SMART:SM00829" FT NP_BIND 259..261 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT NP_BIND 283..284 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT ACT_SITE 37 FT /note="Charge relay system" 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 METAL 35 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 60 FT /note="Zinc 1; via tele nitrogen; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 61 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT METAL 90 FT /note="Zinc 2" 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 104 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 172 FT /note="NAD; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 192 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT BINDING 197 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00627" FT SITE 145 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 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 //