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Database: UniProt/TrEMBL
Entry: D3ICN9_9BACT
LinkDB: D3ICN9_9BACT
Original site: D3ICN9_9BACT 
ID   D3ICN9_9BACT            Unreviewed;       473 AA.
AC   D3ICN9;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   28-FEB-2018, entry version 46.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=HMPREF0669_01193 {ECO:0000313|EMBL:EFC70738.1};
OS   Prevotella sp. oral taxon 299 str. F0039.
OG   Plasmid unnamed {ECO:0000313|EMBL:EFC70738.1}.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=575614 {ECO:0000313|EMBL:EFC70738.1, ECO:0000313|Proteomes:UP000015929};
RN   [1] {ECO:0000313|EMBL:EFC70738.1, ECO:0000313|Proteomes:UP000015929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0039 {ECO:0000313|EMBL:EFC70738.1,
RC   ECO:0000313|Proteomes:UP000015929};
RC   PLASMID=unnamed {ECO:0000313|EMBL:EFC70738.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T.,
RA   Walk T., White J., Yandava C., Izard J., Baranova O.V., Blanton J.M.,
RA   Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFC70738.1, ECO:0000313|Proteomes:UP000015929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0039 {ECO:0000313|EMBL:EFC70738.1,
RC   ECO:0000313|Proteomes:UP000015929};
RC   PLASMID=Plasmid {ECO:0000313|Proteomes:UP000015929};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA   Blanton J.M., Tanner A.C., Dewhirst F.E., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J.,
RA   McCowan C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella sp. Oral Taxon 299 strain F0039.";
RL   Submitted (JUN-2012) 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; CP003667; EFC70738.1; -; Genomic_DNA.
DR   RefSeq; WP_009228369.1; NC_022111.1.
DR   ProteinModelPortal; D3ICN9; -.
DR   STRING; 575614.HMPREF0669_01193; -.
DR   EnsemblBacteria; EFC70738; EFC70738; HMPREF0669_01193.
DR   KEGG; pro:HMPREF0669_01193; -.
DR   eggNOG; ENOG4105E54; Bacteria.
DR   eggNOG; COG0366; LUCA.
DR   KO; K01176; -.
DR   OrthoDB; POG091H0CDS; -.
DR   Proteomes; UP000015929; Plasmid.
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   Pfam; PF00128; Alpha-amylase; 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:UP000015929};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Plasmid {ECO:0000313|EMBL:EFC70738.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015929};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    473       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003046564.
FT   DOMAIN       31    392       Aamy. {ECO:0000259|SMART:SM00642}.
SQ   SEQUENCE   473 AA;  53087 MW;  8AD2AEB5C4EE182A CRC64;
     MIKMKKFFLI MALSCLVLQG IKAHKTVSND EVILHAWCWS FNTIRENLPK IAKAGYTIVQ
     TSPAQHCVTE VKGDKGGGNQ LYGHGKWYYQ YQPTDWKIGN YQMGTRDDLI ALCKEAKRYG
     IRIIVDVLPN HTAVNDCQVE DALDLAVGGH ENLYHANGLT EIKDYNDRLQ CTTGQMGGLP
     DVNTENPDFQ HYYLTYVNDL LSCGVRGFRY DTAKHIGLPS DPKDSKSPEN DFWDVVTGRK
     DVKGLRLALP NDSLFMYGEV LQDANVKEKE YADMIGGVTA STLGWCIRHA LEGHEWKIND
     ITNYCHPVEP QKLITWVESH DTYCNDHESA GLTDSQVRMG WVFITARQFG TPLFYSRPDG
     STLDNVWGNN IVGKKGNDAF LHPEVVAVNK FRKAMHGQKE TIIYANEGKV VEVMRGKKGT
     ALINISSAPQ NISIATMLPN GKYKDVVYQN TFVVSHGILK GTLKPLTSYI LSR
//
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