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Database: UniProt
Entry: A0A0K0GAN1_9FIRM
LinkDB: A0A0K0GAN1_9FIRM
Original site: A0A0K0GAN1_9FIRM 
ID   A0A0K0GAN1_9FIRM        Unreviewed;       556 AA.
AC   A0A0K0GAN1;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   28-FEB-2018, entry version 17.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=WH51_08610 {ECO:0000313|EMBL:KKE79125.1};
OS   Bacilli bacterium VT-13-104.
OC   Bacteria; Firmicutes; Bacilli.
OX   NCBI_TaxID=1637974 {ECO:0000313|EMBL:KKE79125.1, ECO:0000313|Proteomes:UP000034981};
RN   [1] {ECO:0000313|EMBL:KKE79125.1, ECO:0000313|Proteomes:UP000034981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VT-13-104 {ECO:0000313|EMBL:KKE79125.1,
RC   ECO:0000313|Proteomes:UP000034981};
RA   Tetz V., Tetz G.;
RT   "Bacilli bacterium VT-13-104.";
RL   Submitted (APR-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:RU003615}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKE79125.1}.
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DR   EMBL; LAZH01000034; KKE79125.1; -; Genomic_DNA.
DR   RefSeq; WP_047185232.1; NZ_LAZH01000034.1.
DR   EnsemblBacteria; KKE79125; KKE79125; WH51_08610.
DR   PATRIC; fig|1637974.4.peg.1812; -.
DR   Proteomes; UP000034981; Unassembled WGS sequence.
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; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034981};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034981}.
FT   DOMAIN       13    415       Aamy. {ECO:0000259|SMART:SM00642}.
SQ   SEQUENCE   556 AA;  64603 MW;  81A98E05886C2A95 CRC64;
     MTSQWWKEAV AYQIYPRSFM DSNGDGVGDI QGIISKLDYL QDLGIDVIWI SPIYPSPNID
     NGYDISDYQG ISAEYGTMED FDELLEEVHA RGMKLIMDLV INHTSDKHEW FIESRSSRDN
     PYRDYYIWHP GIDGKAPNNW ESIFGGSVWE YDEKTGEYYM HVFASKQPDL NWENPEVRHD
     LYKMVNWWLD KGIDGFRVDA ISHIKKVPGF PDMPNPDNQK YVPSYEGHMN RPGIEVFLEE
     LRKETFDKYD IMTVGEANGV KIQQADAWVG EENGFFNMIF QFEHLDLWGK SATGGLDMQG
     LKKALSKWQK GLDGIGWNAL FLENHDQPRS VSTWGNDTDL REKSAKSFAT MYFLMQGTPF
     IYQGQEIGMT NVKFDSIDDY NDVAIKTLYK EERVAGKSHE EVMKIIWKSG RDNSRTPMQW
     NSKENGGFTT GTPWMKVNPN VKEINVEAEL ENPDSIYHYY KKLIELRRGN ETLIYGSYEL
     ILEEHEQIYA YVRTLGEQQY VILTNLLDGT ADFEFPENLL GKQAELRLSN YQVQEAHETL
     DTMTFRPYEA RVYQIK
//
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