ID A0A0M8X8V6_9ACTN Unreviewed; 339 AA. AC A0A0M8X8V6; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 20-JAN-2016, entry version 2. DE RecName: Full=L-threonine 3-dehydrogenase {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 -!- CATALYTIC ACTIVITY: L-threonine + NAD(+) = L-2-amino-3- CC oxobutanoate + NADH. {ECO:0000256|HAMAP-Rule:MF_00627, CC ECO:0000256|SAAS:SAAS00368609}. 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00627, CC ECO:0000256|SAAS:SAAS00368516}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {ECO:0000256|HAMAP-Rule:MF_00627}. 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 UniPathway; UPA00046; UER00505. DR Proteomes; UP000037734; Unassembled WGS sequence. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.180.10; -; 1. DR HAMAP; MF_00627; Thr_dehydrog; 1. DR InterPro; IPR013149; ADH_C. DR InterPro; IPR013154; ADH_N. DR InterPro; IPR002085; ADH_SF_Zn-type. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like. DR InterPro; IPR004627; L-Threonine_3-DHase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020843; PKS_ER. DR PANTHER; PTHR11695; PTHR11695; 1. 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 METAL 35 35 Zinc 1; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00627}. FT METAL 60 60 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 METAL 145 145 Zinc 1; catalytic. {ECO:0000256|HAMAP- FT 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 //