ID A0A0S3F5R2_9SPHN Unreviewed; 341 AA.
AC A0A0S3F5R2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=ATN00_20945 {ECO:0000313|EMBL:ALR22957.1};
OS Sphingobium baderi.
OG Plasmid pDE1 {ECO:0000313|EMBL:ALR22957.1,
OG ECO:0000313|Proteomes:UP000056968}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1332080 {ECO:0000313|EMBL:ALR22957.1, ECO:0000313|Proteomes:UP000056968};
RN [1] {ECO:0000313|EMBL:ALR22957.1, ECO:0000313|Proteomes:UP000056968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DE-13 {ECO:0000313|EMBL:ALR22957.1,
RC ECO:0000313|Proteomes:UP000056968};
RC PLASMID=Plasmid pDE1 {ECO:0000313|Proteomes:UP000056968};
RA Cheng M., Meng Q., Yang Y., Chu C., Yan X., He J., Li S.;
RT "A Two-component Flavoprotein Monooxygenase System MeaXY Responsible for
RT para-Hydroxylation of 2-Methyl-6-ethylaniline and 2,6-Diethylaniline in
RT Sphingobium baderi DE-13.";
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013265; ALR22957.1; -; Genomic_DNA.
DR RefSeq; WP_062069264.1; NZ_CP013265.1.
DR AlphaFoldDB; A0A0S3F5R2; -.
DR KEGG; sbd:ATN00_20945; -.
DR OrthoDB; 9806940at2; -.
DR Proteomes; UP000056968; Plasmid pDE1.
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 Plasmid {ECO:0000313|EMBL:ALR22957.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000056968};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..338
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 341 AA; 35625 MW; 2B3910A56D3E80FB CRC64;
MAKTMKAAVV REFGKPLVIE DAPIPTVGPG QVLVKIAATG VCHTDLHAAE GDWPVKPNPP
FIPGHEGVGH VAAVGAGVTH VKEGDRVGVP WLYTACGHCV HCLGGWETLC HEQQNTGYSV
NGSFAEYVLA DPNYVGHLPD NVDFLDIAPI LCAGVTVYKG LKATEARPGE WVVVSGIGGL
GHMAVQYARA MGLNVAAVDI DDSKLDLATR LGATLTVNAR NEDPSAALKK AIGGAHGALV
TAVSPRAFQQ ALGMVRRGGT VALNGLPPGD FPLSIFDTVL NGITVRGSIV GTRLDLLEAL
AFAGEGKVKA TVHADKLENI NDVFSRMHHG DIEGRIVLDL A
//
