ID   A0A1I4KS78_9MICO        Unreviewed;       338 AA.
AC   A0A1I4KS78;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase {ECO:0000313|EMBL:SFL81644.1};
GN   ORFNames=SAMN04515692_11396 {ECO:0000313|EMBL:SFL81644.1};
OS   Leifsonia sp. CL147.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=1798215 {ECO:0000313|EMBL:SFL81644.1, ECO:0000313|Proteomes:UP000198997};
RN   [1] {ECO:0000313|Proteomes:UP000198997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL147 {ECO:0000313|Proteomes:UP000198997};
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; FOTM01000013; SFL81644.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4KS78; -.
DR   OrthoDB; 9797931at2; -.
DR   Proteomes; UP000198997; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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; 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   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:UP000198997};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          8..334
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   338 AA;  35911 MW;  4AACC57A6FEC9C26 CRC64;
     MLAANYTGDR TITIEEREPE PLRPGEARIA VAYVGICGTD LHIFHGDMDA RVARPATIGH
     EMSGTIVDLA PDVEGWSVGD AVTVMPLAWD GTCPACLAGN EHICQNLDFI GIDSPGALQE
     HWNVPASTLV RLPAGVSLRD AALVEPVAVA VHDVRRSELG PGDRAVVIGA GPIGVLIATV
     ATDFGAEVVI AEIDANRRAA AEEMGLRTLD PSAVDQVAWV EEWTGGAGAD VVFEVSGAAA
     AVLGATSLAK VRGTLVVVAI HSQPRPLDLH RLFWRELRIL GARVYERRDF ERAVELVAEG
     VIPADRLITR IVPLAETASA FEALEEGRAM KLLVEVGR
//