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Database: UniProt/TrEMBL
Entry: D6EDP6_STRLI
LinkDB: D6EDP6_STRLI
Original site: D6EDP6_STRLI 
ID   D6EDP6_STRLI            Unreviewed;       573 AA.
AC   D6EDP6;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   31-JAN-2018, entry version 49.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   Name=aml {ECO:0000313|EMBL:AIJ11852.1};
GN   ORFNames=SLIV_04145 {ECO:0000313|EMBL:AIJ11852.1};
OS   Streptomyces lividans TK24.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=457428 {ECO:0000313|EMBL:AIJ11852.1, ECO:0000313|Proteomes:UP000028682};
RN   [1] {ECO:0000313|EMBL:AIJ11852.1, ECO:0000313|Proteomes:UP000028682}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TK24 {ECO:0000313|EMBL:AIJ11852.1,
RC   ECO:0000313|Proteomes:UP000028682};
RG   StrepSynth;
RA   Ruckert C., Fridjonson O.H., Lambert C., van Wezel G.P., Bernaerts K.,
RA   Anne J., Economou A., Kalinowski J.;
RT   "Complete genome sequence of Streptomyces lividans TK24.";
RL   Submitted (AUG-2014) 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; CP009124; AIJ11852.1; -; Genomic_DNA.
DR   RefSeq; WP_003972124.1; NZ_GG657756.1.
DR   ProteinModelPortal; D6EDP6; -.
DR   EnsemblBacteria; AIJ11852; AIJ11852; SLIV_04145.
DR   GeneID; 29658851; -.
DR   KEGG; slv:SLIV_04145; -.
DR   PATRIC; fig|457428.16.peg.889; -.
DR   KO; K01176; -.
DR   Proteomes; UP000028682; 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:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF49452; SSF49452; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51166; CBM20; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028682};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:AIJ11852.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:AIJ11852.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     35       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        36    573       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003083587.
FT   DOMAIN      473    573       CBM20. {ECO:0000259|PROSITE:PS51166}.
SQ   SEQUENCE   573 AA;  61467 MW;  B2A565830F135362 CRC64;
     MHGNTSPARR ITATALALTA GVAGSLLATT APAQASPPGD KDVTAVMFEW KFTSVAQACT
     DTLGPAGYGY VQVSPPQEHI QGGQWWTSYQ PVSYRIAGRL GDRAQFKSMV DTCHAAGVKV
     VADSVVNHMS AGNGTGTGGS SYTKYDYPGL YSSNDLDNCT SQINNYGDRF NVQECELVGL
     ADLDTGEDYV RGKIAGYLND LLSLGVDGFR IDAAKHMAAA DLAAIKSRLS NPNVYWKHEA
     IYGAGEAVSP TEYVGSGDVQ EFRYARDLKR VFNGENLAYL KNFGEAWGHL PSDEAAVFVT
     NHDTERNGET LTYKDGATYT LAHVFMLAWP YGSPDVHSGY EFTDHDAGPP NGGQVNACYS
     DGWKCQHAWR EISSMVAFRN TARGQGVTDW WDNGGDQIAF GRGSKAYVAI NHEGTSLTRT
     FQTSLPAGDY CDVQTGKGVT VDGAGRFTAT LGAGTAVALH VGARTCDGGD PGDPDPVSSG
     VSFAVDATTS WGQNIYVTGN RPELGNWNPG GALQLDPAAY PVWKRDVELP EGTTFEYKYL
     RKDDAGNVTW ESGANRTATV NTTKTTLNDT WRN
//
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