ID   A0A268SFI7_9BACL        Unreviewed;       344 AA.
AC   A0A268SFI7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN   ORFNames=CHI14_12730 {ECO:0000313|EMBL:PAF31378.1};
OS   Paenibacillus sp. 7516.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2022549 {ECO:0000313|EMBL:PAF31378.1, ECO:0000313|Proteomes:UP000216732};
RN   [1] {ECO:0000313|EMBL:PAF31378.1, ECO:0000313|Proteomes:UP000216732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7516 {ECO:0000313|EMBL:PAF31378.1,
RC   ECO:0000313|Proteomes:UP000216732};
RA   Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA   Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT   "Isolation and whole genome analysis of endospore-forming bacteria from
RT   heroin.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Quinone oxidoreductase subfamily.
CC       {ECO:0000256|RuleBase:RU364000}.
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:PAF31378.1}.
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DR   EMBL; NPBI01000012; PAF31378.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A268SFI7; -.
DR   Proteomes; UP000216732; 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; cd08252; AL_MDR; 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; IPR013154; ADH-like_N.
DR   InterPro; IPR014182; ADH_Zn_typ-1.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   NCBIfam; TIGR02817; adh_fam_1; 1.
DR   PANTHER; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU364000};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364000};
KW   Zinc {ECO:0000256|RuleBase:RU364000}.
FT   DOMAIN          10..340
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   344 AA;  37762 MW;  5BE19004923965A1 CRC64;
     MSNQQMKAIG LLKYLPVEHP ESLLDVMMDV PEPTGRDLLI RVKAISVNPV DVKVRAPKNR
     TENTPKVLGW DVAGVVEQAG PESSLFKPGD EVYYAGSIDR PGGNSELHLV DERIVGFKPA
     TLEFAHAAAL PLTAITAWEG LFDRLGVSAA TERNEGKTIL IIGAAGGVSS IATQLAKHAG
     LTVIGTASRP ESAEWAKNMG ADHIINHYEA FLPQLKALGL EYVDYIFCLN STEKHWVNMA
     EAIAPQGKIC SIVETDEMLD LTLLKNKSVT FAWELMFTRP LFQTTDMIEQ HNLLNEVSRM
     IDEGRLRTTV AQILSPINAA NLRKAHAILE EGRMTGKIVI ENFE
//