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Database: UniProt/TrEMBL
Entry: A0A1B1FWR8_9BACT
LinkDB: A0A1B1FWR8_9BACT
Original site: A0A1B1FWR8_9BACT 
ID   A0A1B1FWR8_9BACT        Unreviewed;       439 AA.
AC   A0A1B1FWR8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   07-JUN-2017, entry version 6.
DE   SubName: Full=Putative alpha amylase, Glycoside hydrolase family 13 {ECO:0000313|EMBL:ANQ50613.1};
GN   ORFNames=MY04_3248 {ECO:0000313|EMBL:ANQ50613.1};
OS   Flammeovirga sp. MY04.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Flammeovirgaceae;
OC   Flammeovirga.
OX   NCBI_TaxID=1191459 {ECO:0000313|EMBL:ANQ50613.1, ECO:0000313|Proteomes:UP000092715};
RN   [1] {ECO:0000313|EMBL:ANQ50613.1, ECO:0000313|Proteomes:UP000092715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MY04 {ECO:0000313|EMBL:ANQ50613.1,
RC   ECO:0000313|Proteomes:UP000092715};
RA   Han W., Gu J., Liu H., Li Z., Han K., Li Y.;
RT   "The genome sequence and the agarase system of a polysaccharide-
RT   degrading marine bacterium, Flammeovirga sp. MY04.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; CP003560; ANQ50613.1; -; Genomic_DNA.
DR   EnsemblBacteria; ANQ50613; ANQ50613; MY04_3248.
DR   KEGG; flm:MY04_3248; -.
DR   PATRIC; fig|1191459.5.peg.3295; -.
DR   KO; K01176; -.
DR   Proteomes; UP000092715; Chromosome 1.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR013776; A-amylase_thermo.
DR   InterPro; IPR015237; Alpha-amylase_C_pro.
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; PF09154; DUF1939; 1.
DR   PIRSF; PIRSF001021; Alph-amls_thrmst; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000092715};
KW   Hydrolase {ECO:0000313|EMBL:ANQ50613.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092715}.
FT   DOMAIN       30    359       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    218    218       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR001021-1}.
FT   ACT_SITE    242    242       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001021-1}.
FT   METAL       130    130       Calcium 1. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       193    193       Calcium 1. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       366    366       Calcium 3. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
SQ   SEQUENCE   439 AA;  50556 MW;  5CCE5C5D0B021905 CRC64;
     MEMQVTTHDG APFTTDESSN KRYYDSPGGP VMMQAFYWDV PAGGTWWNTV KGKLNNWSNQ
     GIGSIWLPPA SKAQNGPFSM GYDPMDYFDF GDYNQNGSTE TRFGSGAELR SLIGEAHNQN
     MQVYADIVIN HNSGGQLEAN PYTGTDTWTK FQPASGKFNR TYNDFHPNLD ANNDEGIFGG
     YPDLSHVKGY VQDWLWKSNE SVGKYYKNNV GFDGWRFDYV KGFGGWVVKD WVNHVGGFAV
     GEMWDGNANT LKWWVDNTDR KASAFDFAAY YAMDRAFDGN NLNELNSDML WKKDSYRAVT
     FVANHDTDEI WRKNLAYAYI LTHEGYPCVF YKDYEDWLDR GMMNNLLWIH KSYATGNTSI
     LHVDNDEYIM RRNGYNGNPG LVLYINNSDN WQERWIPTNW SSRQIKDYTG HSNWEPWTQG
     GTWVKIQCPP RSYSIWSTK
//
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