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Database: UniProt/TrEMBL
Entry: G2TIS7_BACCO
LinkDB: G2TIS7_BACCO
Original site: G2TIS7_BACCO 
ID   G2TIS7_BACCO            Unreviewed;       487 AA.
AC   G2TIS7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   07-JUN-2017, entry version 38.
DE   SubName: Full=Alpha amylase catalytic region {ECO:0000313|EMBL:AEP00550.1};
GN   ORFNames=Bcoa_1344 {ECO:0000313|EMBL:AEP00550.1};
OS   Bacillus coagulans 36D1.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=345219 {ECO:0000313|EMBL:AEP00550.1, ECO:0000313|Proteomes:UP000009283};
RN   [1] {ECO:0000313|EMBL:AEP00550.1, ECO:0000313|Proteomes:UP000009283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=36D1 {ECO:0000313|EMBL:AEP00550.1,
RC   ECO:0000313|Proteomes:UP000009283};
RX   PubMed=22675583; DOI=10.4056/sigs.2365342;
RA   Rhee M.S., Moritz B.E., Xie G., Glavina Del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Chertkov O., Brettin T., Han C., Detter C.,
RA   Pitluck S., Land M.L., Patel M., Ou M., Harbrucker R., Ingram L.O.,
RA   Shanmugam K.T.;
RT   "Complete Genome Sequence of a thermotolerant sporogenic lactic acid
RT   bacterium, Bacillus coagulans strain 36D1.";
RL   Stand. Genomic Sci. 5:331-340(2011).
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DR   EMBL; CP003056; AEP00550.1; -; Genomic_DNA.
DR   RefSeq; WP_014096659.1; NC_016023.1.
DR   ProteinModelPortal; G2TIS7; -.
DR   STRING; 345219.Bcoa_1344; -.
DR   EnsemblBacteria; AEP00550; AEP00550; Bcoa_1344.
DR   KEGG; bag:Bcoa_1344; -.
DR   eggNOG; ENOG4105E5K; Bacteria.
DR   eggNOG; COG0366; LUCA.
DR   KO; K01176; -.
DR   OrthoDB; POG091H0HQ3; -.
DR   Proteomes; UP000009283; 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; IPR006047; Glyco_hydro_13_cat_dom.
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:UP000009283};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009283}.
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       202    202       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   487 AA;  56053 MW;  19244E7372EB736A CRC64;
     MERNHTILQF FEWNTPADGS HWNRLKEMAP ELKKTGIDAV WLPPVTKGQS DMDNGYGVYD
     HYDLGEFDQK GTVRTKYGTK QQLHEAINAC HEHDIQVYID VVMNHKAGAD ETESFQVVEV
     DPMDRNKEIS EPFEIEGWTK FNFTNRKGKY SDFTWNHTHF SGVDYDNRTG RNGIFRIVGE
     NKHWSEHVDN EFGNFDYLMY ADIDYNHPDV KKEMIEWGKW LADTTGCDGY RLDAIKHINH
     DFIRDFAAAL MEHRGDHFYF VGEFWNPQLE ACQKYLDHVQ FKIDLFDVAL HYKLHEASKK
     GRAFDLPTIF HDTLVQTHPL NAVTFVDNHD SQPNESLESW VDDWFKQSAY ALILLRKDGY
     PCVFYGDMYG IGGDNPIPGK KDALSPLLSV RREKAYGEQD DYFDHPNTIG WVRRGVPEMP
     HSGCAVVISN GENGEKRMLV GKERAGEVWV DATGNRQEKV TIGEDGYAGF PVNGGSVSVW
     VQETDEN
//
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