ID   A0A1H0V1D5_9ACTN        Unreviewed;       350 AA.
AC   A0A1H0V1D5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Threonine dehydrogenase {ECO:0000313|EMBL:SDP72161.1};
GN   ORFNames=SAMN04487981_13511 {ECO:0000313|EMBL:SDP72161.1};
OS   Streptomyces sp. cf386.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1761904 {ECO:0000313|EMBL:SDP72161.1, ECO:0000313|Proteomes:UP000198720};
RN   [1] {ECO:0000313|Proteomes:UP000198720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF386 {ECO:0000313|Proteomes:UP000198720};
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; FNHV01000035; SDP72161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0V1D5; -.
DR   STRING; 1761904.SAMN04487981_13511; -.
DR   OrthoDB; 241504at2; -.
DR   Proteomes; UP000198720; 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   InterPro; IPR020843; PKS_ER.
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   SMART; SM00829; PKS_ER; 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   Reference proteome {ECO:0000313|Proteomes:UP000198720};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..346
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   350 AA;  36573 MW;  18EAAF5D9D516EC5 CRC64;
     MKALTYHGRH DIRYGDAPDP AVTSPTDAVV QVTAAGICGS DLHIYGGSPF SPELGYTPGH
     ECVGVVVETG GQVTRFKPGD RVLVPASVGC AHCRSCAAGF TARCERAKSS TELCYGVSPQ
     LPGSQAQALA VPYADVNLVH LPEDISDEAA VVLTDNAPTA WYGCRRARIQ PGETVLVIGL
     GPVGLMAAQS AFAMGAARVL GADLVAERRA FAATLGVEPV EGEDVRAAIR DMTGGRGPDA
     VVEAVGSDST IELALKAVRQ AGRVSVIGVS QNKAFPFHMG LAQIKELEFA IGLCSVHYEL
     PPLIALTRAG RIKPEVAVSH RFALSEGPAA YELFAGRADG VRKILLDPTH
//