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Database: UniProt/TrEMBL
Entry: A0A1D8FZE4_9ACTN
LinkDB: A0A1D8FZE4_9ACTN
Original site: A0A1D8FZE4_9ACTN 
ID   A0A1D8FZE4_9ACTN        Unreviewed;       569 AA.
AC   A0A1D8FZE4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   18-JUL-2018, entry version 15.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   Name=aml_1 {ECO:0000313|EMBL:AOT58579.1};
GN   ORFNames=A4G23_01392 {ECO:0000313|EMBL:AOT58579.1};
OS   Streptomyces rubrolavendulae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=285473 {ECO:0000313|EMBL:AOT58579.1, ECO:0000313|Proteomes:UP000095349};
RN   [1] {ECO:0000313|EMBL:AOT58579.1, ECO:0000313|Proteomes:UP000095349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJM4426 {ECO:0000313|EMBL:AOT58579.1,
RC   ECO:0000313|Proteomes:UP000095349};
RA   Kim J.-G.;
RT   "Streptomyces rubrolavendulae MJM4426 Genome sequencing and
RT   assembly.";
RL   Submitted (SEP-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; CP017316; AOT58579.1; -; Genomic_DNA.
DR   RefSeq; WP_069976098.1; NZ_CP017316.1.
DR   EnsemblBacteria; AOT58579; AOT58579; A4G23_01392.
DR   KEGG; srn:A4G23_01392; -.
DR   PATRIC; fig|285473.5.peg.1446; -.
DR   KO; K01176; -.
DR   Proteomes; UP000095349; 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   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; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
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:UP000095349};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:AOT58579.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:AOT58579.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095349};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     29       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        30    569       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5009106939.
FT   DOMAIN      468    569       CBM20. {ECO:0000259|PROSITE:PS51166}.
SQ   SEQUENCE   569 AA;  60735 MW;  34E988C4C12606DE CRC64;
     MARRTVAAAL ALVAGAAVGV TAPSQTAQAA APGDKDVTAV MFEWKFSSIA KACTDTLGPA
     GYGYVQVSPP QERIQGSTWW TAYQPVSYRI AGPLGDRAAF KSMIDTCHSA GVKVVADTVI
     NHMSAGSGTG TGGSSYTKYN YPGIYSASDF DNCTSEVNNY RDRWNVQNCE LVGLSDLDTG
     EEYVRGRIAA YMNDLLSLGV DGFRVDAAKH MPAADLANIK SRLSNPNVYW KQEVIHGAGE
     AVSPDEYLGN GDVQEFRYAR ELKRMFTGDK LAYLKNFGEA WGFMSSGQSG VFVDNHDTER
     VGDTLNYKSG AAYTLANVFM LAWPYGSPDV HSGYEWSNKD AGAPNGNQVN ACYQDGWKCQ
     HDWREIKSMV GFRNVARGQG VTNWWDNGNN AIAFGRGTKA YVAINHEGGS LTRTFQTSLP
     AGTYCDVQSN TPVTVDGSGR FTATLGARTA LALHVGATSC GGGGPVTPPP ADGSGASFNV
     DATTSLGQNI HVTGNHAALG NWNPAAAPKL DPSAYPVWKL DLTLPAGTTF EYKYVRKDAA
     GNVTWESGAN RVATVPASGK VTLTDTWRN
//
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