ID E3HNY6_ACHXA Unreviewed; 341 AA.
AC E3HNY6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN Name=adh2 {ECO:0000313|EMBL:ADP18325.1};
GN OrderedLocusNames=AXYL_05019 {ECO:0000313|EMBL:ADP18325.1};
OS Achromobacter xylosoxidans (strain A8).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP18325.1, ECO:0000313|Proteomes:UP000006876};
RN [1] {ECO:0000313|EMBL:ADP18325.1, ECO:0000313|Proteomes:UP000006876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|EMBL:ADP18325.1,
RC ECO:0000313|Proteomes:UP000006876};
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(2011).
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; CP002287; ADP18325.1; -; Genomic_DNA.
DR RefSeq; WP_013395629.1; NC_014640.1.
DR AlphaFoldDB; E3HNY6; -.
DR STRING; 762376.AXYL_05019; -.
DR KEGG; axy:AXYL_05019; -.
DR PATRIC; fig|762376.5.peg.5022; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_1_4; -.
DR OMA; GLKMTDT; -.
DR OrthoDB; 9771084at2; -.
DR Proteomes; UP000006876; Chromosome.
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:ADP18325.1}; Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..338
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 341 AA; 35973 MW; FD84D5D181FF83BC CRC64;
MDKTMKAAVA RAFGKPLAIE EVAVPRPGPG ELLVKIEACG VCHTDLHAVE GDWPVKPNPP
FIPGHEGVGH VVAVGAGVTH VKEGDRVGIP WLYSACGHCE HCLGGWETLC EQQQNAGYSV
NGGFAEYALA AADYVGLLPK NVSFVDIAPV LCAGVTVYKG LKMTDTRPGN WVVISGIGGL
GHMAVQYAKA MGLNVAAVDI DDAKLDFARR LGAEVTVNAK TTDPAAYLKR EIGGAHGALI
TAVSPKAFEQ ALGMVRRGGT VALNGLPPGD FPLSIFDMVL NGVTVRGSIV GSRLDLQESL
QFAEEGKVHA TVATESLENI NDVFDRMRRG QIEGRIVLDF A
//