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Database: UniProt/TrEMBL
Entry: G2NH71_STREK
LinkDB: G2NH71_STREK
Original site: G2NH71_STREK 
ID   G2NH71_STREK            Unreviewed;       574 AA.
AC   G2NH71;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   20-JUN-2018, entry version 51.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=SACTE_1640 {ECO:0000313|EMBL:AEN09556.1};
OS   Streptomyces sp. (strain SirexAA-E / ActE).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN09556.1, ECO:0000313|Proteomes:UP000001397};
RN   [1] {ECO:0000313|EMBL:AEN09556.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C.,
RA   Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I.,
RA   Adams A., Raffa K., Adams S., Book A., Currie C., Woyke T.;
RT   "Complete sequence of Streptomyces sp. SirexAA-E.";
RL   Submitted (AUG-2011) 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; CP002993; AEN09556.1; -; Genomic_DNA.
DR   RefSeq; WP_014045543.1; NC_015953.1.
DR   ProteinModelPortal; G2NH71; -.
DR   STRING; 862751.SACTE_1640; -.
DR   EnsemblBacteria; AEN09556; AEN09556; SACTE_1640.
DR   KEGG; ssx:SACTE_1640; -.
DR   PATRIC; fig|862751.12.peg.1711; -.
DR   eggNOG; ENOG4105E54; Bacteria.
DR   eggNOG; COG0366; LUCA.
DR   KO; K01176; -.
DR   OrthoDB; POG091H0CDS; -.
DR   BioCyc; SSP862751:G1GPM-1650-MONOMER; -.
DR   Proteomes; UP000001397; 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:UP000001397};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001397};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     33       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        34    574       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003433798.
FT   DOMAIN      472    574       CBM20. {ECO:0000259|PROSITE:PS51166}.
SQ   SEQUENCE   574 AA;  60253 MW;  C82854F8E25EB68F CRC64;
     MARRSLSASL ALVTGAAVLA LPAGLGTAGT AQAAPPGEKD VTAVMFEWKF DSVAKACTDS
     LGPAGYGYVQ VSPPQEHIQG GQWWTSYQPV SYKIAGRLGD RTAFANMVGT CHGAGVKVVA
     DAVVNHMSSG SGTGTGGSSY TKYDYPGLYS VNDMNDCQSE INNYGDRANV QNCELVGLAD
     LDTGEEYVRG KIAGYLNDLL SLGVDGFRID AAKHMPAGDL ANIKSRLSNP NVYWKQEAIY
     GANEAVSPTE YLGTGDVQEF RYARGLKQSF LGGNLADLKN FGEGWGFMES GRSAVFVDNH
     DTERNGETLN YKNGADYTLA SVFMLAYPYG SPDVHSGYEW SDKDAGPPSG GQVNACYSDG
     WKCQHAWTEI SSMVGFRNAA RGQAVTNWWD NGGDQIAFGR GSKAYVAINH EGSSLTRTFQ
     TSLPAGDYCD VQSGKGVTVN GSGQFTATLG SNTAVALHTG ARTCTGGGTT PDPGTGGSGA
     SFGVAATTVL GQNIYVTGDQ ATLGDWNPGG ALKLDPAAYP VWKLDVALPA GTSFAYKYLR
     KDAAGNVTWE SGANRTATVP SSGKVALTSD VWRG
//
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