ID A0A0L8M953_9ACTN Unreviewed; 342 AA. AC A0A0L8M953; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 09-DEC-2015, 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: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}; RN [1] {ECO:0000313|EMBL:KOG46915.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL 2666 {ECO:0000313|EMBL:KOG46915.1}; RA Tran T., Druce J.; RT "MeaNS - Measles Nucleotide Surveillance Program."; 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: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 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 PANTHER; PTHR11695; PTHR11695; 1. 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 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:KOG46915.1}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00326562}. FT METAL 38 38 Zinc 1; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00627}. FT METAL 63 63 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 METAL 148 148 Zinc 1; catalytic. {ECO:0000256|HAMAP- FT Rule: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 //