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Database: UniProt/TrEMBL
Entry: A0A1B1M810_STRLN
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ID   A0A1B1M810_STRLN        Unreviewed;       461 AA.
AC   A0A1B1M810;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   18-JUL-2018, entry version 16.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=SLINC_2556 {ECO:0000313|EMBL:ANS64780.1};
OS   Streptomyces lincolnensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS64780.1, ECO:0000313|Proteomes:UP000092598};
RN   [1] {ECO:0000313|EMBL:ANS64780.1, ECO:0000313|Proteomes:UP000092598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS64780.1,
RC   ECO:0000313|Proteomes:UP000092598};
RA   Meng S.C.;
RT   "Enhancement of antibiotic productionsby engineered nitrateutilization
RT   in actinobacteria.";
RL   Submitted (JUL-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:RU003615}.
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DR   EMBL; CP016438; ANS64780.1; -; Genomic_DNA.
DR   EnsemblBacteria; ANS64780; ANS64780; SLINC_2556.
DR   KEGG; sls:SLINC_2556; -.
DR   PATRIC; fig|1915.4.peg.2828; -.
DR   KO; K01176; -.
DR   Proteomes; UP000092598; 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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Complete proteome {ECO:0000313|Proteomes:UP000092598};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092598};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31    461       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5008526736.
FT   DOMAIN       37    374       Aamy. {ECO:0000259|SMART:SM00642}.
FT   DOMAIN      383    459       Aamy_C. {ECO:0000259|SMART:SM00632}.
SQ   SEQUENCE   461 AA;  49510 MW;  9CD9B86CD93238FB CRC64;
     MISRWSATAT SVATALAAAA AVLAPGTAQA APPGTKDVTA VLFEWNFASV ARECTNTLGP
     AGYGYVQVSP PAEHIQGSQW WTSYQPVSYR IAGRLGDRTA FRNMVDTCHA AGVKVVVDTV
     VNHMSAGSGT GTGGSSYTKY TYPGLYSSPD FDDCTSRITN YQDRWNVQHC ELVGLADLDT
     GEEYVRGAVA GYMNDLLSLG VDGFRIDAAK HIDTADLANI RSRLANPSAY WKQEVIFGSG
     EAVQPTEYTG NGDVQEFRYA YDLKRVLTDE NLAYLKNYGE GWGYMSGSVA GVFVDNHDTE
     RNGSTLNYKD GADYTLANVF MLAHPYGAPD INSGYEFTDH DAGPPNGGQV NACWQDGWKC
     QHNWPEIRSM VAFRNATRGA AVTDWWDNGA DAIAFGRGGK GFVAINHESG PLSRTYQTSL
     PAGTYCNVQN NTSVTVNADG RFTATLGADT ALAIHAGKSA C
//
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