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Database: UniProt/TrEMBL
Entry: F7Z707_BACC6
LinkDB: F7Z707_BACC6
Original site: F7Z707_BACC6 
ID   F7Z707_BACC6            Unreviewed;       480 AA.
AC   F7Z707;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   07-JUN-2017, entry version 30.
DE   SubName: Full=Alpha amylase catalytic region {ECO:0000313|EMBL:AEH54976.1};
GN   OrderedLocusNames=BCO26_2920 {ECO:0000313|EMBL:AEH54976.1};
OS   Bacillus coagulans (strain 2-6).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=941639 {ECO:0000313|EMBL:AEH54976.1, ECO:0000313|Proteomes:UP000005637};
RN   [1] {ECO:0000313|EMBL:AEH54976.1, ECO:0000313|Proteomes:UP000005637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-6 {ECO:0000313|EMBL:AEH54976.1,
RC   ECO:0000313|Proteomes:UP000005637};
RX   PubMed=21705584; DOI=10.1128/JB.05378-11;
RA   Su F., Yu B., Sun J., Ou H.Y., Zhao B., Wang L., Qin J., Tang H.,
RA   Tao F., Jarek M., Scharfe M., Ma C., Ma Y., Xu P.;
RT   "Genome sequence of the thermophilic strain Bacillus coagulans 2-6, an
RT   efficient producer of high-optical-purity L-lactic acid.";
RL   J. Bacteriol. 193:4563-4564(2011).
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DR   EMBL; CP002472; AEH54976.1; -; Genomic_DNA.
DR   EnsemblBacteria; AEH54976; AEH54976; BCO26_2920.
DR   KEGG; bck:BCO26_2920; -.
DR   KO; K01176; -.
DR   OMA; GEFWKDS; -.
DR   OrthoDB; POG091H0HQ3; -.
DR   Proteomes; UP000005637; 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:UP000005637};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}.
FT   DOMAIN        1    384       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    226    226       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR001021-1}.
FT   ACT_SITE    256    256       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001021-1}.
FT   METAL        97     97       Calcium 1. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       178    178       Calcium 2. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       189    189       Calcium 1. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       195    195       Calcium 1. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       197    197       Calcium 2. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       230    230       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR001021-2}.
SQ   SEQUENCE   480 AA;  55157 MW;  C3BE7EA4464B77D9 CRC64;
     MQFFEWNTPA DGSHWNRLKE MAPELKKTGI DAVWLPPVTK GQSDMDNGYG VYDHYDLGEF
     DQKGTVRTKY GTKQQLHEAI NACHEHDIQV YIDVVMNHKA GADETEAFQV VEVDPMDRTK
     EISEPFEIEG WTKFNFTNRK DKYSDFTWNH THFSGVDYDN RTGRNGIFRI VGENKHWDEH
     VDNEFGNFDY LMYADIDYNH PDVKKEMIEW GKWLADTTGC DGYRLDAIKH INHDFIRDFA
     AALMEHRGDH FYFVGEFWNP QLEACQKYLD HVQFKIDLFD VALHYKLHEA SKKGRAFDLT
     TIFHDTLVQT HPLNAVTFVD NHDSQPNESL ESWVDDWFKQ SAYALILLRK DGYPCVFYGD
     MYGIGGDHPI PGKKGALSPL LSVRREKAYG EQDDYFDHPN TIGWVRRGVP EMPHSGCAVV
     ISNGENGEKR MLAGKERAGE VWVDATGNRQ EKITIGEDGY AAFPVNGGSV SVWVQETGEN
//
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