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Database: UniProt
Entry: A0A0F3RTM8_9LACO
LinkDB: A0A0F3RTM8_9LACO
Original site: A0A0F3RTM8_9LACO 
ID   A0A0F3RTM8_9LACO        Unreviewed;       363 AA.
AC   A0A0F3RTM8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Aryl-alcohol dehydrogenase {ECO:0000313|EMBL:KJW13326.1};
GN   ORFNames=VC81_02340 {ECO:0000313|EMBL:KJW13326.1};
OS   Levilactobacillus spicheri.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=216463 {ECO:0000313|EMBL:KJW13326.1, ECO:0000313|Proteomes:UP000033491};
RN   [1] {ECO:0000313|EMBL:KJW13326.1, ECO:0000313|Proteomes:UP000033491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LP38 {ECO:0000313|EMBL:KJW13326.1,
RC   ECO:0000313|Proteomes:UP000033491};
RA   Zheng J., Ganezle M.;
RL   Submitted (MAR-2015) 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:KJW13326.1}.
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DR   EMBL; JZCR01000006; KJW13326.1; -; Genomic_DNA.
DR   RefSeq; WP_045806553.1; NZ_JZCR01000006.1.
DR   AlphaFoldDB; A0A0F3RTM8; -.
DR   STRING; 216463.VC81_02340; -.
DR   PATRIC; fig|216463.3.peg.2280; -.
DR   OrthoDB; 9806940at2; -.
DR   Proteomes; UP000033491; 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; cd08278; benzyl_alcohol_DH; 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; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 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|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..360
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   363 AA;  37874 MW;  A71D110412875146 CRC64;
     MKIKTAYADG QSDQLKITAA ELDAPQANEV LVKMVATGIC HTDVAGRDGA TTPLPVALGH
     EGAGIVERVG DSVVGLTPGD HVVLSFSYCG HCANCLSGHP GLCTRFNDLN FGGHNYDGSH
     RLHLPDGQPL STFFGQSSFS TYTVVDQHGV VKVPQDLDLK MLAPLGCGIQ TGAGTVLNYL
     KPQFGESLVV FGTGTVGLAA MMAAKIAGVD HIVAVDIFDN RLALARELGA TETINSKTTD
     LATALQAILP AGADYTIDTT GVAPVVKSAV HALKPGGQCV AVGIGGDITF NLMGDLLAEA
     KSLAGVVEGD AIPQLFIPQL VTYYRQGRFP FDKLIKFFAF DDINAGFAAS KDGSVLKPVV
     TFD
//
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