ID   Q2T289_BURTA            Unreviewed;       354 AA.
AC   Q2T289;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   SubName: Full=Alcohol dehydrogenase, zinc-containing {ECO:0000313|EMBL:ABC38781.1};
GN   OrderedLocusNames=BTH_I0152 {ECO:0000313|EMBL:ABC38781.1};
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS   CIP 106301 / E264).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC38781.1, ECO:0000313|Proteomes:UP000001930};
RN   [1] {ECO:0000313|EMBL:ABC38781.1, ECO:0000313|Proteomes:UP000001930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC   {ECO:0000313|Proteomes:UP000001930};
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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; CP000086; ABC38781.1; -; Genomic_DNA.
DR   RefSeq; WP_009893586.1; NZ_CP008785.1.
DR   AlphaFoldDB; Q2T289; -.
DR   GeneID; 66548614; -.
DR   KEGG; bte:BTH_I0152; -.
DR   HOGENOM; CLU_026673_20_2_4; -.
DR   Proteomes; UP000001930; Chromosome I.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05283; CAD1; 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; IPR047109; CAD-like.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-RELATED; 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.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 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          9..343
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   354 AA;  38357 MW;  C4966248C6F904F1 CRC64;
     MSTTYAYAAT SATTPLAPFE FQRRALRDLD VQIEILYCGV CHSDLHQARN EWKNTTYPVV
     PGHEIVGRVT AVGPQVTRFK TGELVGVGCL VDSCRTCPSC EEGLEQYCEN GFVGTYNGRD
     RATGDVTFGG YSTQIVVDEA FVLRVPDTLD PAGAAPLLCA GITTYSPLRQ WGAGPGKKVG
     VVGLGGLGHM GVKLARAMGA HVVLFTTSPS KIDDGKRLGA HEVVISKDEA QMNAHLNSFD
     FILNTVAAQH DLNPFLHLLK RDGTMTLVGA PEHDHPSPQV FNLIFKRRRL AGSLIGGIAE
     TQEMLDFCAL HGITSDIEVI PMSQVNAAYE RMLKSDVKYR FVIDIGSIRP PRAA
//