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Database: UniProt
Entry: A0A0V8HQ32_9BACI
LinkDB: A0A0V8HQ32_9BACI
Original site: A0A0V8HQ32_9BACI 
ID   A0A0V8HQ32_9BACI        Unreviewed;       338 AA.
AC   A0A0V8HQ32;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Threonine dehydrogenase {ECO:0000313|EMBL:SCB78089.1};
GN   ORFNames=GA0061094_0454 {ECO:0000313|EMBL:SCB78089.1};
OS   [Bacillus] enclensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX   NCBI_TaxID=1402860 {ECO:0000313|EMBL:SCB78089.1, ECO:0000313|Proteomes:UP000181997};
RN   [1] {ECO:0000313|EMBL:SCB78089.1, ECO:0000313|Proteomes:UP000181997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SGD-1123 {ECO:0000313|EMBL:SCB78089.1,
RC   ECO:0000313|Proteomes:UP000181997};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={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; FMAU01000001; SCB78089.1; -; Genomic_DNA.
DR   RefSeq; WP_058297349.1; NZ_KQ758482.1.
DR   AlphaFoldDB; A0A0V8HQ32; -.
DR   OrthoDB; 9770238at2; -.
DR   Proteomes; UP000181997; 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; cd08236; sugar_DH; 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; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 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          25..130
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          172..299
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   338 AA;  36744 MW;  5B55185B4068D3D6 CRC64;
     MKVLSWNGPK QIDVEERPMP ECKKDEVLIR VDVVGICGSE IEGFLGHNSL RVPPLIMGHE
     FSGYIEEMGD EVQNVLIGSK VVVNPLISCG SCPKCRRGLE NLCDNRQIIG VHRPGAFAEY
     VVVPASSVIE VPKSLDSYTA SLSEPLACCL RAVRRALAQH PFSNVLIYGA GAIGVLSGFV
     ADILGARKVV IADINNDRLN TLNNVGFNHT LNPNEESFEE KLSEMAGPEG IDVVIDAAGF
     LPTRTQAASI VNTGGVIMNI GLGIDETPLP VNVFIRSEIT VLGSFCYTKQ DFHDAVNLLV
     DSKIDIKGWT QERELNEGQQ AFLDLIGNRV ENSKIFLS
//
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