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Database: UniProt/TrEMBL
Entry: Q64RC7_BACFR
LinkDB: Q64RC7_BACFR
Original site: Q64RC7_BACFR 
ID   Q64RC7_BACFR            Unreviewed;       481 AA.
AC   Q64RC7;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   28-FEB-2018, entry version 79.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:BAD49954.1};
GN   OrderedLocusNames=BF3209 {ECO:0000313|EMBL:BAD49954.1};
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405 {ECO:0000313|EMBL:BAD49954.1, ECO:0000313|Proteomes:UP000002197};
RN   [1] {ECO:0000313|EMBL:BAD49954.1, ECO:0000313|Proteomes:UP000002197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46 {ECO:0000313|EMBL:BAD49954.1,
RC   ECO:0000313|Proteomes:UP000002197};
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA
RT   inversions regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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DR   EMBL; AP006841; BAD49954.1; -; Genomic_DNA.
DR   RefSeq; WP_011203184.1; NC_006347.1.
DR   RefSeq; YP_100488.1; NC_006347.1.
DR   ProteinModelPortal; Q64RC7; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; BAD49954; BAD49954; BF3209.
DR   GeneID; 3083111; -.
DR   KEGG; bfr:BF3209; -.
DR   PATRIC; fig|295405.11.peg.3077; -.
DR   KO; K01176; -.
DR   OMA; VLNHKMG; -.
DR   OrthoDB; POG091H0HQ3; -.
DR   BioCyc; BFRA295405:G1301-3250-MONOMER; -.
DR   Proteomes; UP000002197; Chromosome.
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   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR013776; A-amylase_thermo.
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   PIRSF; PIRSF001021; Alph-amls_thrmst; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002197};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}.
FT   DOMAIN        4    388       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    232    232       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR001021-1}.
FT   ACT_SITE    262    262       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001021-1}.
FT   METAL       103    103       Calcium 1. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       182    182       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR001021-2}.
FT   METAL       195    195       Calcium 1. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       201    201       Calcium 1. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       203    203       Calcium 2. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       236    236       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR001021-2}.
SQ   SEQUENCE   481 AA;  55220 MW;  212A3767727131DB CRC64;
     MENGVMMQYF EWNLPNDGNL WKQLKEDASH LHEIGVTAVW IPPAYKADEQ QDEGYATYDL
     YDLGEFDQKG TVRTKYGTKE ELKEMIDELH KNHISVYLDV VLNHKAGGDF TEKFIVVEVD
     PNDRTQALGK PFEIQGWTGY SFHGRKDKCS DFKWHWYHFS GTGFDDAKKR SGIFQIQGEG
     KAWSEGVDNE NGNYDFLLCN DIDLDHPEVV TELNRWGKWV SKELNLDGMR LDAIKHMKDK
     FIAQFLDAVR SERGDKFYAV GEYWNGDLNT LDAYIKSVGH KVNLFDVPLH YNLFQASQEG
     KNYDLQNILK NTLVEHHCDL AVTFVDNHDS QSGSSLESQI EDWFKPLAYG LILLIKDGYP
     CLFYGDYYGV KGENSPHTQI INILLDARRK YAYGDQIEYF DHPSAIGFIR TGDEEHVGSG
     LVFLMSNDEA GSKKMDLGEE HKGEIWHEIT GNIQQEITLD EKGSGEFSVN TRNIAVWIKK
     N
//
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