ID B8L6X7_9GAMM Unreviewed; 342 AA.
AC B8L6X7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=SSKA14_2775 {ECO:0000313|EMBL:EED39757.1};
OS Stenotrophomonas sp. SKA14.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=391601 {ECO:0000313|EMBL:EED39757.1};
RN [1] {ECO:0000313|EMBL:EED39757.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA14 {ECO:0000313|EMBL:EED39757.1};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (DEC-2008) 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; DS999412; EED39757.1; -; Genomic_DNA.
DR RefSeq; WP_008267156.1; NZ_DS999412.1.
DR AlphaFoldDB; B8L6X7; -.
DR HOGENOM; CLU_026673_20_1_6; -.
DR Proteomes; UP000003991; Unassembled WGS sequence.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:EED39757.1}; Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..338
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 342 AA; 35749 MW; 8FFE6DF4D174E1CD CRC64;
MNPTMKAAVV REFGKPLVIE EVSVPRPGAG EVLVKIEACG VCHTDLHAAE GDWPVKPNPP
FIPGHEGVGH VVAVGGGVGH VREGDRVGIP WLYSACGHCE HCLGGWETLC ETQRNTGYSV
NGGFAEYALA DANYVGLLPK EVGFVEIAPV LCAGVTVYKG LKVTDTKPGD WVAISGIGGL
GHMAVQYARA MGLNVAAVDV DDNKLALARQ LGAQVTVNAR TTDPAAFLKR EIGGAHGALV
TAVSPKAFEQ ALGMVRRGGT VSLNGLPPGN FPLDIFGMVL NGITVRGSIV GTRLDLQESL
QFAAEGKVAA TVSTDRLENI NDVFARMHAG TIEGRVVLDF AA
//