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Database: UniProt/TrEMBL
Entry: A0A1D7XNN0_9CLOT
LinkDB: A0A1D7XNN0_9CLOT
Original site: A0A1D7XNN0_9CLOT 
ID   A0A1D7XNN0_9CLOT        Unreviewed;       524 AA.
AC   A0A1D7XNN0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   22-NOV-2017, entry version 10.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:AOR24941.1};
GN   ORFNames=BGI42_09125 {ECO:0000313|EMBL:AOR24941.1};
OS   Clostridium taeniosporum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=394958 {ECO:0000313|EMBL:AOR24941.1, ECO:0000313|Proteomes:UP000094652};
RN   [1] {ECO:0000313|EMBL:AOR24941.1, ECO:0000313|Proteomes:UP000094652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1/k {ECO:0000313|EMBL:AOR24941.1,
RC   ECO:0000313|Proteomes:UP000094652};
RA   Walker J.R.;
RT   "Genomics of Clostridium taeniosporum, an organism which forms
RT   endospores with ribbon-like appendages.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP017253; AOR24941.1; -; Genomic_DNA.
DR   RefSeq; WP_069681062.1; NZ_CP017253.1.
DR   EnsemblBacteria; AOR24941; AOR24941; BGI42_09125.
DR   KEGG; ctae:BGI42_09125; -.
DR   KO; K01176; -.
DR   Proteomes; UP000094652; 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:UP000094652};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094652}.
FT   DOMAIN       48    432       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    275    275       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR001021-1}.
FT   ACT_SITE    305    305       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001021-1}.
FT   METAL       148    148       Calcium 1. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       205    205       Calcium 2. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       238    238       Calcium 1. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       244    244       Calcium 1. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       246    246       Calcium 2. {ECO:0000256|PIRSR:
FT                                PIRSR001021-2}.
FT   METAL       279    279       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR001021-2}.
SQ   SEQUENCE   524 AA;  60884 MW;  D8E7E68C4F9F133B CRC64;
     MLCIILAIIL FVAIGGIMYL KLKQDQDIDE FYTEDKKISD RNVIQNNETM MQYFEWYYPN
     DGSLWIKVKE NSKELSEKGI TALWLPPAYK AVNGINDVGY GAYDLYDLGE FDQKGTIRTK
     YGTKAQYLDA INEAHNNNIK IYADTVFNHK AGADDSELVK AQLVDSNNRN NIISEEKDIK
     AFTVFNFPGR NEKYSSYKWS AKDFDGVDFD DSTKQNGIYK FVGKEWEQDV DNENGNFDFL
     MCADLDIDSR DVVEELKRWG IWCIDQCNVD GFRLDAIKHI KFDFFTEWIN YIRSKKGEHI
     FAVGEYWCGD INKLKYYISK SQNVMSLFDA PLHYKFFDAS NQEENFDLRT LMQNTLLEYD
     EKISVTFVDN HDTEPGQSLE SWVKPWFKLI AYTFILTRNE GYPCVFYGDY YGIPEKGFKG
     FKSQLDIILK VRKEYAYGEQ CDYFDDKNLI GWTRQGDLQH INSGIAVLIS NSNEGTKKMF
     VGANNVNTTF VDITGNYREE VIIDNDGNGI FKVNNRSYSI WIKK
//
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