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Database: UniProt
Entry: B1MXD4_LEUCK
LinkDB: B1MXD4_LEUCK
Original site: B1MXD4_LEUCK 
ID   B1MXD4_LEUCK            Unreviewed;       338 AA.
AC   B1MXD4;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   SubName: Full=Threonine dehydrogenase {ECO:0000313|EMBL:ACA82186.1};
DE            EC=1.1.1.- {ECO:0000313|EMBL:ACA82186.1};
GN   OrderedLocusNames=LCK_00353 {ECO:0000313|EMBL:ACA82186.1};
OS   Leuconostoc citreum (strain KM20).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=349519 {ECO:0000313|EMBL:ACA82186.1, ECO:0000313|Proteomes:UP000002166};
RN   [1] {ECO:0000313|EMBL:ACA82186.1, ECO:0000313|Proteomes:UP000002166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KM20 {ECO:0000313|EMBL:ACA82186.1,
RC   ECO:0000313|Proteomes:UP000002166};
RX   PubMed=18281406; DOI=10.1128/JB.01862-07;
RA   Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA   Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT   "Complete genome sequence of Leuconostoc citreum KM20.";
RL   J. Bacteriol. 190:3093-3094(2008).
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; DQ489736; ACA82186.1; -; Genomic_DNA.
DR   RefSeq; WP_004900149.1; NC_010471.1.
DR   AlphaFoldDB; B1MXD4; -.
DR   STRING; 349519.LCK_00353; -.
DR   GeneID; 61102719; -.
DR   KEGG; lci:LCK_00353; -.
DR   eggNOG; COG1063; Bacteria.
DR   HOGENOM; CLU_026673_11_0_9; -.
DR   OMA; FETWYAM; -.
DR   OrthoDB; 9770238at2; -.
DR   Proteomes; UP000002166; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08234; threonine_DH_like; 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   ECO:0000313|EMBL:ACA82186.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          24..132
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          175..296
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   338 AA;  35918 MW;  ECB33903901DC7F4 CRC64;
     MDALVLTGIK SLELQDIAQP EVKPNEVKIH TAFAGICGTD HALYAGLPGS APAVPPIVLG
     HENSGVVAEV GSAVTNVKVG DRVTVDPNIY CGQCKFCRTG RPELCENLSA VGVTRDGGFE
     EYFTAPASVV YQIPDNVSLK SAAVVEPISC AVHGIKLLKV TPYQKALVIG DGFMGELFVQ
     ILQAYGIHQV DLAGIVDEKL AMNKEKFGVK NTFNTMKGDK IPEGEYDVII EAVGLPQTQE
     AAIEASARGA QVLMFGVGGP DAKFEMNTYE VFQKQLTIQG SFINPNAFED SLALLSSGKL
     NVEALMSHEL DYNTVDDFVN GKLGVVSKAV VKVGGEEA
//
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