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Database: UniProt/TrEMBL
Entry: E3EBZ3_PAEPS
LinkDB: E3EBZ3_PAEPS
Original site: E3EBZ3_PAEPS 
ID   E3EBZ3_PAEPS            Unreviewed;       497 AA.
AC   E3EBZ3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:ADO59117.1};
GN   Name=amyL {ECO:0000313|EMBL:ADO59117.1};
GN   ORFNames=PPSC2_24270 {ECO:0000313|EMBL:ADO59117.1};
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO59117.1, ECO:0000313|Proteomes:UP000006868};
RN   [1] {ECO:0000313|EMBL:ADO59117.1, ECO:0000313|Proteomes:UP000006868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:ADO59117.1,
RC   ECO:0000313|Proteomes:UP000006868};
RX   PubMed=21037012; DOI=10.1128/JB.01234-10;
RA   Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA   Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT   "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT   growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT   activity.";
RL   J. Bacteriol. 193:311-312(2011).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; CP002213; ADO59117.1; -; Genomic_DNA.
DR   RefSeq; WP_013373652.1; NC_014622.2.
DR   AlphaFoldDB; E3EBZ3; -.
DR   SMR; E3EBZ3; -.
DR   STRING; 1406.LK13_11790; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; ppm:PPSC2_24270; -.
DR   PATRIC; fig|886882.15.peg.5139; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_024572_2_0_9; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000006868; 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   CDD; cd11318; AmyAc_bac_fung_AmyA; 1.
DR   Gene3D; 2.40.30.140; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013776; A-amylase_thermo.
DR   InterPro; IPR015237; Alpha-amylase_C_pro.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF09154; Alpha-amy_C_pro; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PIRSF; PIRSF001021; Alph-amls_thrmst; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006868}.
FT   DOMAIN          5..391
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        233
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   ACT_SITE        263
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   BINDING         104
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         196
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         204
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         237
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ   SEQUENCE   497 AA;  57151 MW;  89B4CDF2DB1A97FA CRC64;
     MKRNHTMMQF FEWNVKADGS HWKKLARLAP ELKAKGIDAI WIPPVTKGQS PEDTGYGVYD
     LYDLGEFDQK GAVRTKYGTR EDLLEAVASC VRHGVAVYVD LVMNHKAGAD ETEVFKVVEV
     NPDNRNEVIS EPFDIEGWTK FTFPGRQGKY STFQWNFEHF NGTDYDASQD RTGIYRILGK
     NKNWSDNVDD EFGNYDYLMF ANIDYNHQDV RKEMIRWGKW LVDTLQCNGF RLDAIKHINH
     EFVREFATEM IKKRGQDFYM VGEFWKPDLE SCQKFLDTID YKIDLFDVSL HYKLHSASLG
     GKDFDLSTIF EDTLVHTHPL NSVTFVDNHD SQPHEALESW VEDWFKPSAY ALILLRKDGY
     PCVFYGDYYG IQGQTPVEGK QAELDPLLYA RYHKAYGEQK DYFDDPHTIG WVRQGIPELH
     GSGCAVVITN ANDGEKRMFV GKQRAGEKWT DLTGHHDHTI KIEQDGYGIF PVRAGSVSVW
     ALPTEEDSLD AEDTASA
//
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