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Database: UniProt/TrEMBL
Entry: A0A0K2ARA6_STRAM
LinkDB: A0A0K2ARA6_STRAM
Original site: A0A0K2ARA6_STRAM 
ID   A0A0K2ARA6_STRAM        Unreviewed;       457 AA.
AC   A0A0K2ARA6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   20-DEC-2017, entry version 15.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   Name=amy {ECO:0000313|EMBL:AKZ55362.1};
GN   ORFNames=SAM23877_2313 {ECO:0000313|EMBL:AKZ55362.1};
OS   Streptomyces ambofaciens ATCC 23877.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=278992 {ECO:0000313|EMBL:AKZ55362.1, ECO:0000313|Proteomes:UP000061018};
RN   [1] {ECO:0000313|EMBL:AKZ55362.1, ECO:0000313|Proteomes:UP000061018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23877 {ECO:0000313|EMBL:AKZ55362.1,
RC   ECO:0000313|Proteomes:UP000061018};
RA   Thibessard A., Haas D., Gerbaud C., Aigle B., Lautru S.,
RA   Pernodet J.-L., Leblond P.;
RT   "Complete genome sequence of Streptomyces ambofaciens ATCC 23877, the
RT   spiramycin producer.";
RL   Submitted (JUL-2015) 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; CP012382; AKZ55362.1; -; Genomic_DNA.
DR   EnsemblBacteria; AKZ55362; AKZ55362; SAM23877_2313.
DR   KEGG; samb:SAM23877_2313; -.
DR   KO; K01176; -.
DR   Proteomes; UP000061018; 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:UP000061018};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:AKZ55362.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:AKZ55362.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061018};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     26       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        27    457       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5005473377.
FT   DOMAIN       33    370       Aamy. {ECO:0000259|SMART:SM00642}.
FT   DOMAIN      379    455       Aamy_C. {ECO:0000259|SMART:SM00632}.
SQ   SEQUENCE   457 AA;  48796 MW;  B19D905CBAEA18BC CRC64;
     MARRALTGAV ALAAAALVMT PTSAQASPPG AKDVTAVLFE WNFASVAREC TTTLGPAGYG
     YVQVSPPAEH IQGGQWWTSY QPVSYKIAGR LGDRAAFKNM VDTCHAAGVK VVADAVVNHM
     SAGSGTGTGG SSYGKYDYPG LYSSYDLDDC RSQIGNYQDR YNVQHCELVG LADLDTGEDY
     VRGKIAGYLN DLLSLGVDGF RIDAAKHIPA ADLAAVKSRL SNPGVYWKHE VIFGAGEAVQ
     PGEYTGSGDV QEFRYASDLK RVFTNENLAY LKNYGEGWGY LSSGSAGVFV DNHDTERNGS
     TLNYKSGANY TLANVFMLAW PYGAPDVNSG YEWSNHDAGP PNGGRVDACW QGGWKCQHAW
     PEIRSMVAFR NATRGQAVTN WWDNGNDAIA FGRGSKGYVV VNHESGALTR TYQTSLPAGT
     YCDVQSDKPV TVNGSGQFTA TLGADTALAL YAGKSAC
//
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