ID A0A1B4BZJ5_9BURK Unreviewed; 342 AA.
AC A0A1B4BZJ5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=WI26_20920 {ECO:0000313|EMBL:AOI60061.1};
OS Burkholderia diffusa.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=488732 {ECO:0000313|EMBL:AOI60061.1, ECO:0000313|Proteomes:UP000094588};
RN [1] {ECO:0000313|EMBL:AOI60061.1, ECO:0000313|Proteomes:UP000094588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RF2-non-BP9 {ECO:0000313|EMBL:AOI60061.1,
RC ECO:0000313|Proteomes:UP000094588};
RA Sahl J., Wagner D., Keim P.;
RT "Diversity of Burkholderia near neighbor genomes.";
RL Submitted (DEC-2015) 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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; CP013363; AOI60061.1; -; Genomic_DNA.
DR RefSeq; WP_069227039.1; NZ_CP013363.1.
DR AlphaFoldDB; A0A1B4BZJ5; -.
DR KEGG; bdf:WI26_20920; -.
DR Proteomes; UP000094588; Chromosome 2.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08297; CAD3; 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; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR42940:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11; 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 14..338
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 342 AA; 36131 MW; 5E718AD9CC7DCD3F CRC64;
MTQTMKAAVV HAFGEPLRIE EVPVPTPGPG QILVNIKASG VCHTDLHAAD GDWPVKPTLP
FIPGHEGVGV VAAVGAGVTH VREGDRVGVP WLYTACGYCE YCHTGWETLC HGQQNTGYSV
NGSYAEYVLA DPDYVGHLPA QVAFDEIAPI LCAGVTVYKG IRVTDTRPGQ WIAISGIGGL
GHVAVQYARA MGLHVAAIDV SAPKLELARQ LGAQLTIDAS ADDPAKVIQK EIGGAHGVLV
TAVSRSAFAQ ALGMVRRGGT VALNGLPPGD FPLPIFSTVL NGITVRGSIV GTRRDLQESL
DFAADGLVRA HIHRDRLGNI NDIFARLREG KVDGRIVLTD MH
//