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Database: UniProt/TrEMBL
Entry: A0A1B2GLW2_STRNR
LinkDB: A0A1B2GLW2_STRNR
Original site: A0A1B2GLW2_STRNR 
ID   A0A1B2GLW2_STRNR        Unreviewed;       473 AA.
AC   A0A1B2GLW2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   31-JAN-2018, entry version 12.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=SNOUR_08095 {ECO:0000313|EMBL:ANZ14938.1};
OS   Streptomyces noursei ATCC 11455.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=316284 {ECO:0000313|EMBL:ANZ14938.1, ECO:0000313|Proteomes:UP000093521};
RN   [1] {ECO:0000313|EMBL:ANZ14938.1, ECO:0000313|Proteomes:UP000093521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11455 {ECO:0000313|EMBL:ANZ14938.1,
RC   ECO:0000313|Proteomes:UP000093521};
RA   Ruckert C., Albersmeier A., Winkler A., Zotchev S., Kalinowski J.;
RT   "Complete genome sequence of Streptomyces noursei ATCC 11455, a
RT   producer of the medically important antifungal antibiotic nystatin.";
RL   Submitted (APR-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:RU003615}.
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DR   EMBL; CP011533; ANZ14938.1; -; Genomic_DNA.
DR   EnsemblBacteria; ANZ14938; ANZ14938; SNOUR_08095.
DR   KEGG; snr:SNOUR_08095; -.
DR   PATRIC; fig|316284.13.peg.1803; -.
DR   KO; K01176; -.
DR   Proteomes; UP000093521; 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:UP000093521};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:ANZ14938.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:ANZ14938.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     47       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        48    473       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008537345.
FT   DOMAIN       54    382       Aamy. {ECO:0000259|SMART:SM00642}.
FT   DOMAIN      391    473       Aamy_C. {ECO:0000259|SMART:SM00632}.
SQ   SEQUENCE   473 AA;  50311 MW;  F83EE121B7625775 CRC64;
     MQRRRSRHRA VPKEPRGGHR SRMLGRTLTG ALAAAGLAAL APWPSQATPP GDRTVTATLF
     EWKYADVARA CTDQLGPAGY GYVEVSPASE HIQGDQWWTS YQPVSYKIAG RLGDRAAFAS
     MVGTCHAAGV KVIADAVINH MAAGSGTGTG GTQYTKYNYP GYYQDWDFHG CRRNISDYTN
     RDDVQNCELV GLADLDTGSD YVRTTLAKYL DDLRSLGVDG FRIDAAKHIA AADLAAIKGK
     MKDPGYWVQE VVYGAGEAVQ PDEYTGTGDI DEFRYGTHLK SAFQSGNLAQ LKSVADGKLG
     GDRARTFVDN WDTERNGSTL TYKDGAAYTL ANVFMLASPY GSPNVYSGYQ WSDKDAGPPA
     SGSSGWTDEH AKREITGMVG FRNAVGSAGL TNWWDNGGDA IAFGRGSAGF VALNAGDGAV
     NRTFATSLPA GTYCDVVAAV PTSCEGHTVT VGQDGSAQLT VPAHGAVALH IAR
//
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