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Database: UniProt
Entry: A0A1B9YL97_9BRAD
LinkDB: A0A1B9YL97_9BRAD
Original site: A0A1B9YL97_9BRAD 
ID   A0A1B9YL97_9BRAD        Unreviewed;       337 AA.
AC   A0A1B9YL97;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Zinc-type alcohol dehydrogenase-like protein {ECO:0000256|RuleBase:RU364000};
GN   ORFNames=LMTR3_11935 {ECO:0000313|EMBL:OCK55504.1};
OS   Bradyrhizobium sp. LMTR 3.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=189873 {ECO:0000313|EMBL:OCK55504.1, ECO:0000313|Proteomes:UP000093220};
RN   [1] {ECO:0000313|EMBL:OCK55504.1, ECO:0000313|Proteomes:UP000093220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMTR 3 {ECO:0000313|EMBL:OCK55504.1,
RC   ECO:0000313|Proteomes:UP000093220};
RA   Ormeno-Orrillo E., Duran D., Rey L., Ruiz Argueso T., Imperial J.,
RA   Martinez E.;
RL   Submitted (JUL-2016) 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:OCK55504.1}.
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DR   EMBL; MAXC01000046; OCK55504.1; -; Genomic_DNA.
DR   RefSeq; WP_065748173.1; NZ_MAXC01000046.1.
DR   AlphaFoldDB; A0A1B9YL97; -.
DR   STRING; 189873.LMTR3_11935; -.
DR   OrthoDB; 9785812at2; -.
DR   Proteomes; UP000093220; 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   Reference proteome {ECO:0000313|Proteomes:UP000093220};
KW   Zinc {ECO:0000256|RuleBase:RU364000}.
FT   DOMAIN          15..334
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   337 AA;  36366 MW;  4A1EC735C03D93DA CRC64;
     MKAVGYKKSL PIEDANALID FEAAKPEPTG RDIRVAVKAI SANPVDYKVR KRAAPPEGET
     KILGYDAAGI VDAVGPDVTL FKPGDEVFYA GSILRQGTNA EFHLVDERIV GKKPKSLSFA
     QAAALPLTSI TAWELLFDRL GALPGKSLDP RTLLITGGAG GVGSILIQLA RRLTGLTVVA
     TATRPESQKW CLDLGAHAVI DHSKPMKEQI EKLKVPPVAL VASLTFTDQH YKAIADFIAP
     QGKFGLIDDP PEFTVSAFKG KAVSIHWESM FTRSSFQTPD MIAQHHLLND VSDLLDKGVL
     RTTLDQTFGT INAANLKRAH ALLESGKSRG KIVLEGW
//
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