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Database: UniProt/TrEMBL
Entry: A0A0B6A9S1_BACMB
LinkDB: A0A0B6A9S1_BACMB
Original site: A0A0B6A9S1_BACMB 
ID   A0A0B6A9S1_BACMB        Unreviewed;       483 AA.
AC   A0A0B6A9S1;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-SEP-2017, entry version 14.
DE   SubName: Full=Alpha amylase, catalytic domain protein {ECO:0000313|EMBL:AJI21715.1};
GN   ORFNames=BG04_2237 {ECO:0000313|EMBL:AJI21715.1};
OS   Bacillus megaterium (strain ATCC 14581 / DSM 32 / JCM 2506 / NBRC
OS   15308 / NCIMB 9376 / NCTC 10342 / VKM B-512).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1348623 {ECO:0000313|EMBL:AJI21715.1, ECO:0000313|Proteomes:UP000031829};
RN   [1] {ECO:0000313|EMBL:AJI21715.1, ECO:0000313|Proteomes:UP000031829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14581 / DSM 32 / JCM 2506 / NBRC 15308 / NCIMB 9376 /
RC   NCTC 10342 / VKM B-512 {ECO:0000313|Proteomes:UP000031829};
RX   PubMed=25931591;
RA   Johnson S.L., Daligault H.E., Davenport K.W., Jaissle J., Frey K.G.,
RA   Ladner J.T., Broomall S.M., Bishop-Lilly K.A., Bruce D.C.,
RA   Gibbons H.S., Coyne S.R., Lo C.C., Meincke L., Munk A.C.,
RA   Koroleva G.I., Rosenzweig C.N., Palacios G.F., Redden C.L.,
RA   Minogue T.D., Chain P.S.;
RT   "Complete genome sequences for 35 biothreat assay-relevant bacillus
RT   species.";
RL   Genome Announc. 3:0-0(2015).
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DR   EMBL; CP009920; AJI21715.1; -; Genomic_DNA.
DR   RefSeq; WP_034648190.1; NZ_JJMH01000011.1.
DR   EnsemblBacteria; AJI21715; AJI21715; BG04_2237.
DR   GeneID; 29908438; -.
DR   KEGG; bmeg:BG04_2237; -.
DR   KO; K01176; -.
DR   Proteomes; UP000031829; 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   InterPro; IPR013776; A-amylase_thermo.
DR   InterPro; IPR015237; Alpha-amylase_C_pro.
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   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:UP000031829};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}.
FT   DOMAIN        5    391       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    233    233       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR001021-1}.
FT   ACT_SITE    263    263       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001021-1}.
FT   METAL       104    104       Calcium 1. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       196    196       Calcium 1. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       204    204       Calcium 2. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       237    237       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR001021-2}.
SQ   SEQUENCE   483 AA;  56110 MW;  94AE23504387D40C CRC64;
     MERNHTIMQF FEWHVPADGE HWQRLKELAP QLKEQGIDSV WIPPVTKGVS SEDNGYGVYD
     LYDLGEFDQK GTVRTKYGTK QELHEAIDAC HNHGINVYVD IVMNHKAAAD EKETFHVIEV
     DPMNRTEEIS EPFEIEGWTK FTFEGRGDKY SSFKWNFNHF NGTDYDDKNG KEGVFRIAGE
     NKSWNENVDQ EFGNYDYLMF ANIDYDHPEV REEMIKWGKW LADTLQCDGY RLDAIKHINH
     DFIKEFAHEL SSSQEKPFYF VGEFWNPELT ACQEFLDVID YQIDLFDVSL HYKLHEASQQ
     GRDFDLTTIF DDTLVKTHPL NVVTFVDNHD SQPNESLESW VEDWFKQSAY ALILLREDGY
     PCVFYGDYFG IGGEHPIEGK EKDISALLHV RYDKAYGQQD DYFDHPNTIG WVRHGVEEFE
     KSGCAVVMSN GEDGEKRMFV GEHRSGQTWI DFTNNREDQV VIEEDGYGQF PVNGGSVSVW
     AEA
//
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