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Database: UniProt/TrEMBL
Entry: A0A0S2FM85_9GAMM
LinkDB: A0A0S2FM85_9GAMM
Original site: A0A0S2FM85_9GAMM 
ID   A0A0S2FM85_9GAMM        Unreviewed;       345 AA.
AC   A0A0S2FM85;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   07-JUN-2017, entry version 9.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:ALN84779.1};
DE            EC=1.1.1.1 {ECO:0000313|EMBL:ALN84779.1};
GN   Name=adhT {ECO:0000313|EMBL:ALN84779.1};
GN   ORFNames=LC55x_1488 {ECO:0000313|EMBL:ALN84779.1};
OS   Lysobacter capsici.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=435897 {ECO:0000313|EMBL:ALN84779.1};
RN   [1] {ECO:0000313|EMBL:ALN84779.1, ECO:0000313|Proteomes:UP000059881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55 {ECO:0000313|EMBL:ALN84779.1,
RC   ECO:0000313|Proteomes:UP000059881};
RX   PubMed=26597042; DOI=10.1186/s12864-015-2191-z;
RA   de Bruijn I., Cheng X., de Jager V., Exposito R.G., Watrous J.,
RA   Patel N., Postma J., Dorrestein P.C., Kobayashi D., Raaijmakers J.M.;
RT   "Comparative genomics and metabolic profiling of the genus
RT   Lysobacter.";
RL   BMC Genomics 16:991-991(2015).
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; CP011130; ALN84779.1; -; Genomic_DNA.
DR   RefSeq; WP_046658854.1; NZ_KQ061217.1.
DR   EnsemblBacteria; ALN84779; ALN84779; LC55x_1488.
DR   KEGG; lcp:LC55x_1488; -.
DR   PATRIC; fig|435897.5.peg.1480; -.
DR   KO; K13953; -.
DR   Proteomes; UP000059881; 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; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000059881};
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000313|EMBL:ALN84779.1};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN       14    339       PKS_ER. {ECO:0000259|SMART:SM00829}.
SQ   SEQUENCE   345 AA;  36189 MW;  9CFC2B0E4BE23EB8 CRC64;
     MKGTMRAAVA HRLGIPLSIE HLPIPSPGPG EVLVKIRASG VCHTDLHAVQ GDWPIQPVLP
     FIPGHEGAGV VTEVGAGVKH LRSGDPVGIA WLHDACGHCE YCISGWETLC ERQRNSGYSV
     NGTFSDYAIA DAAYVARLPD NCDFIALAPI LCAGVTSYKG IRETEARPGE WIAISGIGGL
     GHLAIQYAKT MGLHVAAIDV SESKLALARS LGAEIVVNAN DASALEDIRR ATGGGAQGVL
     VTAVSPSAFT QALGMVRRKG TISLVGLPPG EFATPIFDVV LKRITLRGSI VGNRQDLAEA
     VAMAAYGKVR AQVEPFPLSQ VNMVLDRLRV GGIEGRAVLD MSLVA
//
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