ID   A0A419TCA1_9FIRM        Unreviewed;       340 AA.
AC   A0A419TCA1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Zn-dependent alcohol dehydrogenase {ECO:0000313|EMBL:RKD35134.1};
GN   ORFNames=BET01_01965 {ECO:0000313|EMBL:RKD35134.1};
OS   Lacrimispora algidixylanolytica.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lacrimispora.
OX   NCBI_TaxID=94868 {ECO:0000313|EMBL:RKD35134.1, ECO:0000313|Proteomes:UP000284277};
RN   [1] {ECO:0000313|EMBL:RKD35134.1, ECO:0000313|Proteomes:UP000284277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPL73 {ECO:0000313|EMBL:RKD35134.1,
RC   ECO:0000313|Proteomes:UP000284277};
RA   Poppleton D.I., Gribaldo S.;
RT   "A new outlook on sporulation: Clostridium algidixylanolyticum.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00008072, 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:RKD35134.1}.
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DR   EMBL; MCIA01000001; RKD35134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A419TCA1; -.
DR   OrthoDB; 9769198at2; -.
DR   Proteomes; UP000284277; 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   CDD; cd08261; Zn_ADH7; 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   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:UP000284277};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..336
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   340 AA;  36602 MW;  94D918CAE127E8C9 CRC64;
     MKAVQIVKPG QLTIIDIEKP ELSGPDQVLV KMTAAGICGS DVGIYHGSNA AATYPRIIGH
     EMVGKVVETG SGVTHIKVGE RVIVNQVTSC GHCYPCRIGR GNVCDHLAVR GVHIDGGYRE
     YIAVPESDCY LLPDSISDED AVMIEPTTIG IQACTRAELN KDDMLLIYGS GALGSSILKT
     ASLICEHIIV ADVQESKLEA ARRNGAVYTI NTREEDLVSK VKEYTNGHGA TVSIDAVCNK
     DSLSQLLDAT GNAGRVITMG FSTSPTEISQ FAITSKELDV RGSRLQNKMF GKAIDLIREG
     KLDLLGSVSH TFPLTKAQEA FDFVDSRDPS IRKVVLTFDF
//