ID   A0A1H7DY17_9ACTN        Unreviewed;       391 AA.
AC   A0A1H7DY17;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Threonine dehydrogenase {ECO:0000313|EMBL:SEK06616.1};
GN   ORFNames=SAMN05443287_1224 {ECO:0000313|EMBL:SEK06616.1};
OS   Micromonospora phaseoli.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1144548 {ECO:0000313|EMBL:SEK06616.1, ECO:0000313|Proteomes:UP000198707};
RN   [1] {ECO:0000313|Proteomes:UP000198707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7038 {ECO:0000313|Proteomes:UP000198707};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FNYV01000022; SEK06616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7DY17; -.
DR   STRING; 1144548.SAMN05443287_1224; -.
DR   OrthoDB; 3399630at2; -.
DR   Proteomes; UP000198707; 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..150
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          198..267
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   391 AA;  42441 MW;  2CB370E543A88D96 CRC64;
     MRANTWTGRN KVKVRDVPDP RLLNDRDAIV RITSTAICGS DLHLVDGYVP TMQDGDVLGH
     EFMGEVIEVG RGVDSGRLRV GDRVVVPFPI ACGACGACAA ELYSCCENSN PNAGIAEKMF
     GHPVAGIFGY SHLTGGFAGG QAQYARVPFA DVGPLKIESD LTDEQVLFLS DILPTGYMGA
     EMCDIQPTDV VAVWGAGPVG QFAMDSARVL GAAKVIAIDK EPYRLQMAER AGHTPVNFEE
     VDVRSRLLEL TGGRGPDKCI DAVGMEASHG STPLYAYDRV KQAVRSETER PHALRQAILS
     CRSGGIVSVI GVYGGLLDKF PAGAWMNRSL TLRTGQCHVQ RYMKPLLQRI ERGEIDPTRV
     ITHTLPLDDA ERGFEIFKNK QDNCEKVVLK P
//