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Database: UniProt/TrEMBL
Entry: S5UQ17_STRC3
LinkDB: S5UQ17_STRC3
Original site: S5UQ17_STRC3 
ID   S5UQ17_STRC3            Unreviewed;       458 AA.
AC   S5UQ17;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   20-DEC-2017, entry version 31.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=B446_11680 {ECO:0000313|EMBL:AGS69158.1};
OS   Streptomyces collinus (strain DSM 40733 / Tu 365).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS69158.1, ECO:0000313|Proteomes:UP000015423};
RN   [1] {ECO:0000313|Proteomes:UP000015423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40733 / Tu 365 {ECO:0000313|Proteomes:UP000015423};
RA   Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA   Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT   "The complete genome sequence of Streptomyces collinus Tu 365.";
RL   Submitted (OCT-2012) 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; CP006259; AGS69158.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGS69158; AGS69158; B446_11680.
DR   KEGG; sci:B446_11680; -.
DR   PATRIC; fig|1214242.5.peg.2398; -.
DR   KO; K01176; -.
DR   OrthoDB; POG091H0CDS; -.
DR   BioCyc; SCOL1214242:G13G0-2331-MONOMER; -.
DR   Proteomes; UP000015423; 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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006048; A-amylase/branching_C.
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   Pfam; PF02806; Alpha-amylase_C; 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:UP000015423};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015423};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     27       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        28    458       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004532791.
FT   DOMAIN       34    371       Aamy. {ECO:0000259|SMART:SM00642}.
FT   DOMAIN      380    456       Aamy_C. {ECO:0000259|SMART:SM00632}.
SQ   SEQUENCE   458 AA;  49567 MW;  59D11099B0FEE7E6 CRC64;
     MARSTLPMAL AVAAAFTIGM YPTTAAASPP GTKDVTAVLF EWNYASVAKE CTATLGPAGY
     GYVQVSPPAE HIQGSQWWTS YQPVSYRIAG RLGDRTAFQN MVNTCHAAGV KVVVDTVVNH
     MAAGSGTGTG GSSYTKYNYP GLYSSPDFDD CTSQVTNYQD RWNVQHCELV GLADLDTGEE
     YVRKTIAGYM NDLLTLGVDG FRIDAAKHIP ADDLANIKSR LTKPAAYWKQ EVIYGAGEAV
     QPTEYTGNGD VQEFRYAYDL KRVFNNEKLA YLNNYGEGWG YLSSSVAGVF VDNHDTERNG
     STLNYKDGAK YTLANVFMLA WPYGAPDINS GYEWSDADAG PPNGGKVNAC WQDGWKCQHA
     WPEIKSMVAF RNATRGQSVT NWWDDGNNAI GFGRGSKGYV AINHESSSLT RTYQTSLAAG
     TYCNVQNNTT VTVNSNGQFT ATLGADTALA IYAGKSGC
//
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