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Entry: A0A1B1S8F8_9BACT
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Original site: A0A1B1S8F8_9BACT 
ID   A0A1B1S8F8_9BACT        Unreviewed;       478 AA.
AC   A0A1B1S8F8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 2.
DT   20-DEC-2017, entry version 13.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=A4V02_04735 {ECO:0000313|EMBL:ANU63086.2};
OS   Parabacteroides sp. YL27.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=1834200 {ECO:0000313|EMBL:ANU63086.2, ECO:0000313|Proteomes:UP000186351};
RN   [1] {ECO:0000313|Proteomes:UP000186351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YL27 {ECO:0000313|Proteomes:UP000186351};
RA   Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA   McCoy K.D., Macpherson A.J.;
RT   "Complete Genome Sequences of Twelve Strains of a Stable Defined
RT   Moderately Diverse Mouse Microbiota 2 (sDMDMm2).";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic
CC       linkages in polysaccharides containing three or more (1->4)-alpha-
CC       linked D-glucose units. {ECO:0000256|RuleBase:RU361134}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|RuleBase:RU361134}.
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DR   EMBL; CP015402; ANU63086.2; -; Genomic_DNA.
DR   KEGG; pary:A4V02_04735; -.
DR   KO; K01176; -.
DR   Proteomes; UP000186351; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0103025; F:alpha-amylase activity (releasing maltohexaose); IEA:UniProtKB-EC.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Complete proteome {ECO:0000313|Proteomes:UP000186351};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Lyase {ECO:0000313|EMBL:ANU63086.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186351}.
FT   DOMAIN       34    379       Aamy. {ECO:0000259|SMART:SM00642}.
FT   DOMAIN      410    478       Aamy_C. {ECO:0000259|SMART:SM00632}.
SQ   SEQUENCE   478 AA;  52769 MW;  FE0C9C1DA8CA5520 CRC64;
     MMKNFLLFPT VGIMIAGSVI GCKPETNEVP TCDGAILHAW SWSFDTIAAN MKAIADAGFD
     YVQTSPANTC FIGEQGGMAL FSEEGDSVKG KWYYYYQPID WKIGNHLLGT RQQFKNMCDS
     AAKYGVKVIV DVLPNHTAVD HSAVTADLDS AAGGHDKLFH ANGFNNIHQW NDRYECTTGM
     MGGLPDVNTE NPGFQHYYLQ YVNDLLACGA RGFRYDTAKH IGLPDDPRDS LSERNNFWDI
     ATGRESVQGL SLAMPADSLF IYGEVLQDKN VREADYAEYM GVTASNYGHA LRHVLSEGNY
     FADSLAQWMN PAPPARLVTW VESHDTYANE HESADLEDDQ IRQGYVFLVA RQYGTPLFFS
     RPMGSTRQNY WGNNRIGARG NDEFFNPEVV AANHFRHAMH GQSEQISATD NGAVIAVERG
     NKGIILINIS DEPQQVNLPT SLAKGTYTDN VHGLGFNVSD GLISGTILSM SSCIIYGN
//
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