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Database: UniProt/TrEMBL
Entry: A0A0F7N4M1_9ACTN
LinkDB: A0A0F7N4M1_9ACTN
Original site: A0A0F7N4M1_9ACTN 
ID   A0A0F7N4M1_9ACTN        Unreviewed;       477 AA.
AC   A0A0F7N4M1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   20-JUN-2018, entry version 18.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=AA958_08825 {ECO:0000313|EMBL:AKH82314.1};
OS   Streptomyces sp. CNQ-509.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH82314.1, ECO:0000313|Proteomes:UP000034283};
RN   [1] {ECO:0000313|EMBL:AKH82314.1, ECO:0000313|Proteomes:UP000034283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH82314.1,
RC   ECO:0000313|Proteomes:UP000034283};
RA   Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA   Kalinowski J., Heide L., Kaysser L.;
RT   "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific
RT   Producer of Meroterpenoid Chemistry.";
RL   Submitted (MAY-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; CP011492; AKH82314.1; -; Genomic_DNA.
DR   RefSeq; WP_047015661.1; NZ_CP011492.1.
DR   EnsemblBacteria; AKH82314; AKH82314; AA958_08825.
DR   KEGG; strc:AA958_08825; -.
DR   PATRIC; fig|444103.5.peg.1859; -.
DR   KO; K01176; -.
DR   Proteomes; UP000034283; 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   Gene3D; 2.60.40.1180; -; 1.
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; IPR013780; Glyco_hydro_b.
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:UP000034283};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034283};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     35       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        36    477       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002519182.
FT   DOMAIN       49    394       Aamy. {ECO:0000259|SMART:SM00642}.
FT   DOMAIN      403    477       Aamy_C. {ECO:0000259|SMART:SM00632}.
SQ   SEQUENCE   477 AA;  50421 MW;  CE252E84FB1B27B0 CRC64;
     MAQSVRRRRR GSRLLPGTAL AALVLGLLPA ATAHANTEAV ARDTAAGNDV IANLWSWNWK
     SVAAECTDVL GPAGYGAVWV APPAESLSHP RHHWWDVYQP YSYGLSGRFG TEADFTAMTA
     ACNGAGVAVY TDAVVNHTAA QTGTGYAGTA LGDKYAPPMY SRADYNVDVC NREISNWDDK
     WEVQNCELLG LPDLKTGSDS VRDKIAGYLN SQIARGVSGF RVDAAKHIPA ADLEAIAGRL
     DDTADGSRPF VFHEVFPGGT PAPDEYYGSG RVLDFAFGDR VKAAFQSDIA QLENLGPGQG
     LLPAGNSVSF VTNHDTERNG RHLTYKDGDT AVLANVFQLG WTEAPPTVYA GFAFAGNDDS
     PPADADGFVT GTDCAAGWSC LDRDPRITGM VGWRNAAGDA EVTDWQSPRG NVVGFGRGDR
     GFAALNNTGE PVTQEFGTAV PDGVYCNVLD DCAGKVTVAG GRVTLDLPAR GAVAFHP
//
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