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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //