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Database: UniProt/TrEMBL
Entry: A0A1Q2GYY0_9GAMM
LinkDB: A0A1Q2GYY0_9GAMM
Original site: A0A1Q2GYY0_9GAMM 
ID   A0A1Q2GYY0_9GAMM        Unreviewed;       669 AA.
AC   A0A1Q2GYY0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   28-FEB-2018, entry version 9.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=B0W48_11090 {ECO:0000313|EMBL:AQQ00297.1};
OS   Pseudoalteromonas aliena.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=247523 {ECO:0000313|EMBL:AQQ00297.1, ECO:0000313|Proteomes:UP000188243};
RN   [1] {ECO:0000313|EMBL:AQQ00297.1, ECO:0000313|Proteomes:UP000188243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EH1 {ECO:0000313|EMBL:AQQ00297.1,
RC   ECO:0000313|Proteomes:UP000188243};
RA   Kim E., Heo E., Kim H., Kim D.;
RT   "Complete genome sequence of the cold-active Pseudoalteromonas aliena
RT   strain EH1 isolated from Arctic seawater.";
RL   Submitted (FEB-2017) 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; CP019628; AQQ00297.1; -; Genomic_DNA.
DR   KEGG; paln:B0W48_11090; -.
DR   KO; K01176; -.
DR   Proteomes; UP000188243; 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   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:UP000188243};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    669       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012975852.
FT   DOMAIN       27    373       Aamy. {ECO:0000259|SMART:SM00642}.
FT   DOMAIN      383    470       Aamy_C. {ECO:0000259|SMART:SM00632}.
SQ   SEQUENCE   669 AA;  73204 MW;  16ECD9B5F664B7F9 CRC64;
     MTLNKIITTA GLSLGLLLPS IATATPTTFV HLFEWNWQDV AQECEQYLGP KGYAAVQVSP
     PNEHITGSQW WTRYQPVSYE LKSRGGNRAQ FIDMVNRCSA AGVDIYVDTL INHMAAGSGT
     GTAGNSFGNK SYPIYSPQDF HQSCTINNSD YGNNRYRVQN CELVGLADLD TASNYVQNTL
     AAYINDLQAI GVKGFRFDAA KHVAASDIQS LKTKINGSPV IFHEVIDQGV EAVSASEYLS
     SGLVTEFKYS TQLGNTFRKG SLAWLSNFGE GWGFMPSSSA VVFVDNHDNQ RGHGGAGNVI
     TFEDGRLYDL ANVFMLAYPY GYPKVMSSYD FHGNTDAGGP SVPVHNNGNL ECFGSNWKCE
     HRWSYIAGGV DFRNNTADNW AVTNWWDNTN NQIAFGRGSS GHMAINKEDS TLNATVQTDM
     ASGQYCNVLK GALSADGKRC SGEVIAVNAN GTINLNVAAW DAMAIHKNSK LNTSSAPNTG
     SDWQRTVIFI NAQTQSGQDM FLRGGVDHAY ANANLGRNCQ TSNFECAMPI RHNNLKNVTT
     SPWKTNDNYL DWYGIENGQS GEAEGSATDW TTNVWPAGWG AEKTLSADGF GVTPLNIWGE
     HYWMLDVDMD CSKAVNGWFE LKAFIKNGQG WETAIAQNNT PYASTNHMAQ CGKINKFEFN
     NSSVAIRSF
//
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