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Database: UniProt/TrEMBL
Entry: E3HNY6_ACHXA
LinkDB: E3HNY6_ACHXA
Original site: E3HNY6_ACHXA 
ID   E3HNY6_ACHXA            Unreviewed;       341 AA.
AC   E3HNY6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   07-JUN-2017, entry version 46.
DE   SubName: Full=Alcohol dehydrogenase 2 {ECO:0000313|EMBL:ADP18325.1};
DE            EC=1.1.1.1 {ECO:0000313|EMBL:ADP18325.1};
GN   Name=adh2 {ECO:0000313|EMBL:ADP18325.1};
GN   OrderedLocusNames=AXYL_05019 {ECO:0000313|EMBL:ADP18325.1};
OS   Achromobacter xylosoxidans (strain A8).
OC   Bacteria; Proteobacteria; 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
RT   bacterium Achromobacter xylosoxidans A8.";
RL   J. Bacteriol. 193:791-792(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; CP002287; ADP18325.1; -; Genomic_DNA.
DR   RefSeq; WP_013395629.1; NC_014640.1.
DR   STRING; 762376.AXYL_05019; -.
DR   EnsemblBacteria; ADP18325; ADP18325; AXYL_05019.
DR   KEGG; axy:AXYL_05019; -.
DR   PATRIC; fig|762376.5.peg.5022; -.
DR   eggNOG; ENOG4105DQ4; Bacteria.
DR   eggNOG; COG1064; LUCA.
DR   HOGENOM; HOG000294685; -.
DR   KO; K13953; -.
DR   OMA; YKGLKMT; -.
DR   OrthoDB; POG091H06JQ; -.
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   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006876};
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000313|EMBL:ADP18325.1};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN       14    338       PKS_ER. {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
//
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