ID   A0A1C6VUG7_9ACTN        Unreviewed;       392 AA.
AC   A0A1C6VUG7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Threonine dehydrogenase {ECO:0000313|EMBL:SCL69945.1};
GN   ORFNames=GA0070603_5330 {ECO:0000313|EMBL:SCL69945.1};
OS   Micromonospora chersina.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=47854 {ECO:0000313|EMBL:SCL69945.1, ECO:0000313|Proteomes:UP000198605};
RN   [1] {ECO:0000313|EMBL:SCL69945.1, ECO:0000313|Proteomes:UP000198605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44151 {ECO:0000313|EMBL:SCL69945.1,
RC   ECO:0000313|Proteomes:UP000198605};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; FMIB01000002; SCL69945.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6VUG7; -.
DR   STRING; 47854.GA0070603_5330; -.
DR   OrthoDB; 3399630at2; -.
DR   Proteomes; UP000198605; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08283; FDH_like_1; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          26..146
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          196..264
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   392 AA;  41881 MW;  7B5BE25983BBEBF8 CRC64;
     MRALCWEGVG RLAVRDVPEP TIRSAGDIIV KVRASSVCGS DLHLINGYLP AMREGDILGH
     EFMGEVVETG PDVQRIKVGD RVVVGSVVAC GGCWYCRTEQ YSLCDNSNPQ PVFTEKLWGH
     SPAGILGYSH AAGGYSGSHA EYIRVPFGDV GAFTVPDGVP DDSVVFASDA MPTGWMAADF
     CGLKGGEVVA VWGAGGVGLM AARSAQILGA ERVIVIDRLP ERLATATQRL GVETINYAET
     DVLEALREMT AGRGPDACIE AVGMESHDVG PTYAYDKAKQ TARLQSDRPT SVRQAIMACR
     KGGTVSIVGV YGGLVDKFPL GAAMNKALVL RMGQMHAQRY IPMLLDRLAI GEIDPGFLAT
     HPMSLEDGAR GYEVFQKKEE GCLRTVLHPQ VA
//