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Database: UniProt/TrEMBL
Entry: A0A0G3BKD2_9BURK
LinkDB: A0A0G3BKD2_9BURK
Original site: A0A0G3BKD2_9BURK 
ID   A0A0G3BKD2_9BURK        Unreviewed;       510 AA.
AC   A0A0G3BKD2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   20-DEC-2017, entry version 15.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=AAW51_1762 {ECO:0000313|EMBL:AKJ28453.1};
OS   [Polyangium] brachysporum.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ28453.1, ECO:0000313|Proteomes:UP000035352};
RN   [1] {ECO:0000313|EMBL:AKJ28453.1, ECO:0000313|Proteomes:UP000035352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ28453.1,
RC   ECO:0000313|Proteomes:UP000035352};
RA   Tang B., Yu Y.;
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; CP011371; AKJ28453.1; -; Genomic_DNA.
DR   EnsemblBacteria; AKJ28453; AKJ28453; AAW51_1762.
DR   KEGG; pbh:AAW51_1762; -.
DR   PATRIC; fig|413882.6.peg.1853; -.
DR   KO; K01176; -.
DR   Proteomes; UP000035352; 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   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; 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:UP000035352};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035352};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31    510       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5005183595.
FT   DOMAIN       36    413       Aamy. {ECO:0000259|SMART:SM00642}.
FT   DOMAIN      423    508       Aamy_C. {ECO:0000259|SMART:SM00632}.
SQ   SEQUENCE   510 AA;  55092 MW;  0449DBBCB50AB7B6 CRC64;
     MPRSFARAAV ALGVASLLGA APWAASTAHA QASARTAFVH LFEWKWTDVA KECETYLGPK
     GFAGVQVSPP NEHNWVTSGN GAPYPWWMRY QPVSYNLDRS RSGTRAEFQD MVNRCNAVGV
     GIYVDAVINH MSGGSSGTSS AGRSWSYHHY PGLYSGYDFH SPVCAVNNYS NADNVQLCEL
     SGLQDLHTGT PYVRGKIADY LVGLANMGVK GFRVDAAKHI SPGDLGAIID NVNSRVATRP
     YWFLEVIGAP GEAVQPEQYF GLGGGQVNVT EFNYGKQLYG KFANGRLADL ETFGPTWGLM
     PSHKAVAFVD NHDKQRGHGG GGSYLTYHAG STYNLANVFM LAWPYGYPSV MSSYAFNRAS
     EYDTSFGPPH HSGGATKGPW DGNVSSPACF NQQIGGWVCE HRWRPIGNMV GFRNATLGTW
     AVTDWWDNDH NQIAFGRGDK GFVVINKEGA ALTRNFKTSL PAGRYCDVIS GDYLNGSCTG
     QVVTVDAGGY ATLTAPPYGA AAIHVGARMR
//
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