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Database: UniProt/TrEMBL
Entry: A0A167TP08_9BACI
LinkDB: A0A167TP08_9BACI
Original site: A0A167TP08_9BACI 
ID   A0A167TP08_9BACI        Unreviewed;       336 AA.
AC   A0A167TP08;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   22-NOV-2017, entry version 12.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:ANB61690.1};
DE            EC=1.1.1.1 {ECO:0000313|EMBL:ANB61690.1};
GN   Name=adh {ECO:0000313|EMBL:ANB61690.1};
GN   ORFNames=GFC30_353 {ECO:0000313|EMBL:ANB61690.1};
OS   Anoxybacillus amylolyticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB61690.1, ECO:0000313|Proteomes:UP000076865};
RN   [1] {ECO:0000313|EMBL:ANB61690.1, ECO:0000313|Proteomes:UP000076865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB61690.1,
RC   ECO:0000313|Proteomes:UP000076865};
RX   PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003;
RA   Poli A., Esposito E., Lama L., Orlando P., Nicolaus G.,
RA   de Appolonia F., Gambacorta A., Nicolaus B.;
RT   "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing
RT   bacterium isolated from Mount Rittmann (Antarctica).";
RL   Syst. Appl. Microbiol. 29:300-307(2006).
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; CP015438; ANB61690.1; -; Genomic_DNA.
DR   RefSeq; WP_066322596.1; NZ_CP015438.1.
DR   EnsemblBacteria; ANB61690; ANB61690; GFC30_353.
DR   KEGG; aamy:GFC30_353; -.
DR   PATRIC; fig|294699.3.peg.336; -.
DR   KO; K13953; -.
DR   Proteomes; UP000076865; 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_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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:UP000076865};
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000313|EMBL:ANB61690.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076865};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN       10    334       PKS_ER. {ECO:0000259|SMART:SM00829}.
SQ   SEQUENCE   336 AA;  35908 MW;  05BAA135C310E887 CRC64;
     MKAAVVHEFK QKLRIEEVEK PTLEYGEVLV KIEACGVCHT DLHAAHGDWP VKPKLPLIPG
     HEGVGVVVEV GEGVKSLKVG DRVGIPWLYS ACGECEYCLS GQETLCPHQL NGGYSVDGGY
     AEYCKAPADY VARIPENLDP VEVAPILCAG VTTYKALKVS NAKPGDWVAI YGIGGLGHIA
     LQYAKAMGFN VVAVDISDDK AELATKLGAD IAINGLKEDP VATIQEKVGG VQAAISVAVT
     KKAFEQAYRS VKRGGCLVVV GLPHDELPIP IFDTVLNGVT VKGSIVGTRK DMQEALDFAA
     RGKVRPIVEA VPLEKINDVF EKMEKGQING RIVLTM
//
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