ID   A0A0G1Y1V7_9BACT        Unreviewed;       455 AA.
AC   A0A0G1Y1V7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Threonine 3-dehydrogenase {ECO:0000313|EMBL:KKW08902.1};
GN   ORFNames=UY45_C0003G0109 {ECO:0000313|EMBL:KKW08902.1};
OS   Parcubacteria group bacterium GW2011_GWA1_49_26.
OC   Bacteria.
OX   NCBI_TaxID=1618797 {ECO:0000313|EMBL:KKW08902.1, ECO:0000313|Proteomes:UP000034066};
RN   [1] {ECO:0000313|EMBL:KKW08902.1, ECO:0000313|Proteomes:UP000034066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKW08902.1}.
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DR   EMBL; LCQA01000003; KKW08902.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1Y1V7; -.
DR   Proteomes; UP000034066; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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          114..230
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          271..406
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   455 AA;  50795 MW;  F3112EED92416CE2 CRC64;
     MGEEFSVLQG GCGKQACLRR RAEYPAQKFY GQRHAITGRL VVLFVLRTTC PELHEGQFYL
     RLIYDNLKKT MNSISALTYD VKEDGWETST GFIKREVTMP ALDEKANPKD VLAVLLEIQY
     AGVCGTDRGI WNRQVFKELI HQTLERENKS TRILGHEFVG RVVEAGSQVE NLYGIRVGDN
     VSGDSHVTCG RCFQCRVGEE EVCQDQAILG ISTDGIFSKY AKISAKNLWQ VDFSRIRPEI
     CAMLDPFGNA VHSCSKVELR GKRVAVLGCG PIGMFTVLLA RAFGAVKIVA VDILEANLNT
     AKELGAHEVV LLRKRDDIEA DPGLLQRIRE LTYDKGVDVT FEMAGPNASV NNALAITRGG
     GEVVLFGLKD GDFVIPEFKD AIVKGLTLYG VIGRQIFQTW QTSQRMLSDK TNGIQEKVWK
     HILKEGRDTI IPLDSYSKEL FEQKMAEHAK ILIKF
//