ID Q9RM92_PRIMG Unreviewed; 545 AA. AC Q9RM92; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 02-SEP-2026, entry version 119. DE RecName: Full=Beta-amylase {ECO:0000256|ARBA:ARBA00012594, ECO:0000256|PROSITE-ProRule:PRU10050}; DE EC=3.2.1.2 {ECO:0000256|ARBA:ARBA00012594, ECO:0000256|PROSITE-ProRule:PRU10050}; GN Name=bamM {ECO:0000313|EMBL:CAB61483.1}; OS Priestia megaterium (Bacillus megaterium). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Priestia. OX NCBI_TaxID=1404 {ECO:0000313|EMBL:CAB61483.1}; RN [1] {ECO:0000313|EMBL:CAB61483.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM319 {ECO:0000313|EMBL:CAB61483.1}; RX PubMed=11499932; DOI=10.1007/s002530100645; RA Wittchen K.D., Lee J.S., Stahl C., Strey J., Meinhardt F.; RT "Cloning, expression, and carbon catabolite repression of the bamM gene RT encoding beta-amylase of Bacillus megaterium DSM319."; RL Appl. Microbiol. Biotechnol. 56:205-211(2001). CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in CC polysaccharides so as to remove successive maltose units from the CC non-reducing ends of the chains.; EC=3.2.1.2; CC Evidence={ECO:0000256|ARBA:ARBA00000546, ECO:0000256|PROSITE- CC ProRule:PRU10050, ECO:0000256|RuleBase:RU000509}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|PIRSR:PIRSR600125-3}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR600125-3}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. CC {ECO:0000256|ARBA:ARBA00005652, ECO:0000256|RuleBase:RU000509}. 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; AJ250858; CAB61483.1; -; Genomic_DNA. DR RefSeq; WP_013081506.1; NZ_JARMWE010000025.1. DR AlphaFoldDB; Q9RM92; -. DR SMR; Q9RM92; -. DR CAZy; CBM20; Carbohydrate-Binding Module Family 20. DR CAZy; GH14; Glycoside Hydrolase Family 14. DR BRENDA; 3.2.1.2; 656. DR GO; GO:0016161; F:beta-amylase activity; IEA:UniProtKB-EC. DR GO; GO:2001070; F:starch binding; IEA:InterPro. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro. DR CDD; cd05809; CBM20_beta_amylase; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR002044; CBM20. DR InterPro; IPR034835; CBM20_beta_amylase. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR001554; Glyco_hydro_14. DR InterPro; IPR018238; Glyco_hydro_14_CS. DR InterPro; IPR000125; Glyco_hydro_14A_bac. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1. DR PANTHER; PTHR31352:SF1; BETA-AMYLASE 3, CHLOROPLASTIC; 1. DR Pfam; PF00686; CBM_20; 1. DR Pfam; PF01373; Glyco_hydro_14; 1. DR PRINTS; PR00750; BETAAMYLASE. DR PRINTS; PR00841; GLHYDLASE14A. DR SMART; SM01065; CBM_2; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS00506; BETA_AMYLASE_1; 1. DR PROSITE; PS00679; BETA_AMYLASE_2; 1. DR PROSITE; PS51166; CBM20; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR600125-3}; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, KW ECO:0000256|RuleBase:RU000509}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000509}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000509}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR600125-3}; KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326, KW ECO:0000256|RuleBase:RU000509}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..545 FT /note="Beta-amylase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5039023152" FT DOMAIN 444..545 FT /note="CBM20" FT /evidence="ECO:0000259|PROSITE:PS51166" FT ACT_SITE 202 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10050" FT ACT_SITE 202 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR600125-1" FT ACT_SITE 397 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600125-1" FT BINDING 79 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2" FT BINDING 86 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR600125-3" FT BINDING 90 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR600125-3" FT BINDING 91 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR600125-3" FT BINDING 119 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2" FT BINDING 127 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2" FT BINDING 174 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR600125-3" FT BINDING 317 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2" FT BINDING 322 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2" FT BINDING 360 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2" FT BINDING 398..399 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2" FT BINDING 427 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2" SQ SEQUENCE 545 AA; 60277 MW; 5CCC066A53132F7E CRC64; MKQLCKKGLA FVLMFIFVNA FILSPINGAA AVDGKSMNPG YKTYLMAPLK KVTDYTTWEA FENDLRKAKQ NGFYAVTVDF WWGDMEKNGD QQFDFSYAQR FAQAARNAGI KIVPIISTHQ CGGNVGDDCN VPLPSWVWNL KSDDSLYFKS ETGTTNKETL SPLATDVISK QYGELYTAFA QALAPYKDVI AKIYLSGGPA GEIRYPSYTA ADGTGYPSRG KFQVYTNFAK SKFQSYALTK YGSLAGINQA WGTNLTSASQ ILPPSDGYQF LKDGYSTAYG KDFLAWYQGA LEDHTKRIGQ LAHQAFDSTF NVPIGAKVAG IHWQYNNPTI PHAAEKPAGY NDYNALLDAF KTAKLDITFT CLEMTDSGNY PEYSMPKKLV RQVAGIANAK GVVLNGENAL TIGSEDQYTK AAEMAFNYNF AGFTLLRFYD VINNDTLMGQ FKNTLGVTPL AQTVVVKNAP TALGETVYIV GDRAELGQWD TSIYPIKLTY NSSTADWRGT VHFPASQNVQ FKAIVKRADG SLKAWQPSQQ YWSVPSTTTT YTDNW //