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Database: UniProt/TrEMBL
Entry: M4KRF2_BACIU
LinkDB: M4KRF2_BACIU
Original site: M4KRF2_BACIU 
ID   M4KRF2_BACIU            Unreviewed;       659 AA.
AC   M4KRF2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   20-DEC-2017, entry version 31.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   Name=amyE {ECO:0000313|EMBL:AGE62151.1};
GN   ORFNames=C663_0294 {ECO:0000313|EMBL:AGE62151.1};
OS   Bacillus subtilis XF-1.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1233100 {ECO:0000313|EMBL:AGE62151.1, ECO:0000313|Proteomes:UP000011821};
RN   [1] {ECO:0000313|EMBL:AGE62151.1, ECO:0000313|Proteomes:UP000011821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XF-1 {ECO:0000313|EMBL:AGE62151.1};
RX   PubMed=23558530;
RA   Guo S., Mao Z., Wu Y., Hao K., He P., He Y.;
RT   "Genome Sequencing of Bacillus subtilis Strain XF-1 with High
RT   Efficiency in the Suppression of Plasmodiophora brassicae.";
RL   Genome Announc. 1:E0006613-E0006613(2013).
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; CP004019; AGE62151.1; -; Genomic_DNA.
DR   RefSeq; WP_015382700.1; NC_020244.1.
DR   EnsemblBacteria; AGE62151; AGE62151; C663_0294.
DR   KEGG; bsx:C663_0294; -.
DR   PATRIC; fig|1233100.3.peg.307; -.
DR   KO; K01176; -.
DR   Proteomes; UP000011821; 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; 2.60.40.10; -; 1.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR031965; CBM26.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16738; CBM26; 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:UP000011821};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:AGE62151.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:AGE62151.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     33       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        34    659       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004054759.
FT   DOMAIN       50    383       Aamy. {ECO:0000259|SMART:SM00642}.
FT   DOMAIN      393    468       Aamy_C. {ECO:0000259|SMART:SM00632}.
SQ   SEQUENCE   659 AA;  72428 MW;  7F72EE297347047A CRC64;
     MFAKRFKTSL LPLFAGFLLL FHLVLAGPTA ANAETANKSN ELTAPSIKSG TILHAWNWSF
     NTLKHNMKDI HDAGYTAIQT SPINQVKEGN QGNKSMSNWY WLYQPTSYQI GNRYLGTEQE
     FKEMCAAAEE YGIKVIVDAV INHTTSDYAA ISNEIKSIPN WTHGNTQIKN WSDRWDVTQN
     SLLGLYDWNT QNTQVQSYLK RFLERALNDG ADGFRFDAAK HIELPDDGSY GSQFWPNITN
     TSAEFQYGEI LQDSASRDAA YANYMNVTAS NYGHSIRSAL KNRNLGVSNI SHYASDVSAD
     KLVTWVESHD TYANDDEEST WMSDDDIRLG WAVIASRSGS TPLFFSRPEG GGNGVRFPGK
     SQIGDRGSAL FEDQAITAVN RFHNVMAGQP EELSNPNGNN QIFMNQRGSH GVVLANTGSS
     SVSINTPTKL PNGRYDNKAG AGSFQVNDGK LTGTINARSV AVLYPDDIAK APHVFLENYK
     TGVTHSFNDQ LTITLRADAN TTKAVYQINN GPETAFKDGD QFTIGKGDPF GKTYTIILKG
     TNSDGVTKTE EYSFVKRDPA SAKTIGYQNP NHWSQVNAYI YKHDGGRAIE LTGSWPGKPM
     TKNADGIYTL TLPADTDTTN AKVIFNNGSA QVPGQNQPGF DYVQNGLYND SGLSGSLPH
//
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