ID AMYB_BACCE Reviewed; 546 AA. AC P36924; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2002, sequence version 2. DT 27-MAR-2024, entry version 120. DE RecName: Full=Beta-amylase; DE EC=3.2.1.2; DE AltName: Full=1,4-alpha-D-glucan maltohydrolase; DE Flags: Precursor; GN Name=spoII; OS Bacillus cereus. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1396; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=BQ10-S1; RX PubMed=8434930; DOI=10.1128/aem.59.2.623-627.1993; RA Nanmori T., Nagai M., Shimizu Y., Shinke R., Mikami B.; RT "Cloning of the beta-amylase gene from Bacillus cereus and characteristics RT of the primary structure of the enzyme."; RL Appl. Environ. Microbiol. 59:623-627(1993). RN [2] RP SEQUENCE REVISION. RA Nanmori T., Mikami B., Shimizu Y.; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), ACTIVE SITE, SUBSTRATE-BINDING, RP METAL-BINDING, AND COFACTOR. RX PubMed=10353816; DOI=10.1021/bi9829377; RA Mikami B., Adachi M., Kage T., Sarikaya E., Nanmori T., Shinke R., RA Utsumi S.; RT "Structure of raw starch-digesting Bacillus cereus beta-amylase complexed RT with maltose."; RL Biochemistry 38:7050-7061(1999). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 31-546 IN COMPLEXES WITH SUBSTRATE RP ANALOGS, ACTIVE SITE, AND SUBSTRATE-BINDING. RX PubMed=12761294; DOI=10.1093/jb/mvg061; RA Oyama T., Miyake H., Kusunoki M., Nitta Y.; RT "Crystal structures of beta-amylase from Bacillus cereus var mycoides in RT complexes with substrate analogs and affinity-labeling reagents."; RL J. Biochem. 133:467-474(2003). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 31-546 IN COMPLEX WITH CALCIUM RP IONS AND MALTOSE, MUTAGENESIS OF TYR-194, AND DISULFIDE BOND. RX PubMed=15449941; DOI=10.1021/bi049173h; RA Hirata A., Adachi M., Utsumi S., Mikami B.; RT "Engineering of the pH optimum of Bacillus cereus beta-amylase: conversion RT of the pH optimum from a bacterial type to a higher-plant type."; RL Biochemistry 43:12523-12531(2004). 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 -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:10353816}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:10353816}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}. 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; AB024519; BAA75890.1; -; Genomic_DNA. DR PDB; 1B90; X-ray; 2.50 A; A=31-546. DR PDB; 1B9Z; X-ray; 2.10 A; A=31-546. DR PDB; 1CQY; X-ray; 1.95 A; A=448-546. DR PDB; 1ITC; X-ray; 2.10 A; A=31-546. DR PDB; 1J0Y; X-ray; 2.10 A; A/B/C/D=31-546. DR PDB; 1J0Z; X-ray; 2.20 A; A/B/C/D=31-546. DR PDB; 1J10; X-ray; 2.10 A; A/B/C/D=31-546. DR PDB; 1J11; X-ray; 2.00 A; A/B/C/D=31-546. DR PDB; 1J12; X-ray; 2.10 A; A/B/C/D=31-546. DR PDB; 1J18; X-ray; 2.00 A; A=31-546. DR PDB; 1VEM; X-ray; 1.85 A; A=31-546. DR PDB; 1VEN; X-ray; 2.02 A; A=31-546. DR PDB; 1VEO; X-ray; 2.12 A; A=31-546. DR PDB; 1VEP; X-ray; 2.06 A; A=31-546. DR PDB; 5BCA; X-ray; 2.20 A; A/B/C/D=31-546. DR PDBsum; 1B90; -. DR PDBsum; 1B9Z; -. DR PDBsum; 1CQY; -. DR PDBsum; 1ITC; -. DR PDBsum; 1J0Y; -. DR PDBsum; 1J0Z; -. DR PDBsum; 1J10; -. DR PDBsum; 1J11; -. DR PDBsum; 1J12; -. DR PDBsum; 1J18; -. DR PDBsum; 1VEM; -. DR PDBsum; 1VEN; -. DR PDBsum; 1VEO; -. DR PDBsum; 1VEP; -. DR PDBsum; 5BCA; -. DR AlphaFoldDB; P36924; -. DR SMR; P36924; -. DR DrugBank; DB02645; 3,4-Epoxybutyl-Alpha-D-Glucopyranoside. DR DrugBank; DB03389; alpha-D-Xylopyranose. DR DrugBank; DB02379; Beta-D-Glucose. DR DrugBank; DB03323; Maltose. DR CAZy; CBM20; Carbohydrate-Binding Module Family 20. DR CAZy; GH14; Glycoside Hydrolase Family 14. DR BRENDA; 3.2.1.2; 648. DR EvolutionaryTrace; P36924; -. DR GO; GO:0102229; F:amylopectin maltohydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0016161; F:beta-amylase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:2001070; F:starch binding; IEA:InterPro. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW. 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; IPR034835; CBM20_beta_amylase. DR InterPro; IPR002044; CBM_fam20. DR InterPro; IPR001554; Glyco_hydro_14. DR InterPro; IPR018238; Glyco_hydro_14_CS. DR InterPro; IPR000125; Glyco_hydro_14A_bac. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR013783; Ig-like_fold. DR PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1. DR PANTHER; PTHR31352:SF40; BETA-AMYLASE 5; 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 1: Evidence at protein level; KW 3D-structure; Calcium; Carbohydrate metabolism; Direct protein sequencing; KW Disulfide bond; Glycosidase; Hydrolase; Metal-binding; KW Polysaccharide degradation; Signal. FT SIGNAL 1..30 FT CHAIN 31..546 FT /note="Beta-amylase" FT /id="PRO_0000001453" FT DOMAIN 444..546 FT /note="CBM20" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594" FT ACT_SITE 202 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10050, FT ECO:0000269|PubMed:10353816, ECO:0000269|PubMed:12761294" FT ACT_SITE 397 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:10353816, FT ECO:0000269|PubMed:12761294" FT BINDING 79 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:10353816, FT ECO:0000269|PubMed:12761294" FT BINDING 86 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10353816" FT BINDING 90 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10353816" FT BINDING 91 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10353816" FT BINDING 119 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:10353816, FT ECO:0000269|PubMed:12761294" FT BINDING 127 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:10353816, FT ECO:0000269|PubMed:12761294" FT BINDING 171 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10353816" FT BINDING 174 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10353816" FT BINDING 317 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:10353816, FT ECO:0000269|PubMed:12761294" FT BINDING 322 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:10353816, FT ECO:0000269|PubMed:12761294" FT BINDING 360 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:10353816, FT ECO:0000269|PubMed:12761294" FT BINDING 398..399 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:10353816" FT BINDING 427 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:10353816, FT ECO:0000269|PubMed:12761294" FT DISULFID 121..129 FT /evidence="ECO:0000269|PubMed:15449941" FT MUTAGEN 194 FT /note="Y->E: Reduces activity by 60%." FT /evidence="ECO:0000269|PubMed:15449941" FT MUTAGEN 194 FT /note="Y->F: Reduces activity by 64%." FT /evidence="ECO:0000269|PubMed:15449941" FT MUTAGEN 194 FT /note="Y->H: Reduces activity by 97%." FT /evidence="ECO:0000269|PubMed:15449941" FT MUTAGEN 194 FT /note="Y->Q: Reduces activity by 80%." FT /evidence="ECO:0000269|PubMed:15449941" FT HELIX 32..34 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 42..46 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 52..54 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 58..70 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 73..81 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 82..85 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 96..107 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 111..117 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 121..124 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 135..140 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 146..149 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 165..182 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 184..189 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 199..201 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 202..204 FT /evidence="ECO:0007829|PDB:1VEM" FT TURN 210..213 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 227..241 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 244..251 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 258..260 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 267..272 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 274..276 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 278..306 FT /evidence="ECO:0007829|PDB:1VEM" FT TURN 307..310 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 314..318 FT /evidence="ECO:0007829|PDB:1VEM" FT TURN 323..326 FT /evidence="ECO:0007829|PDB:1VEN" FT STRAND 328..330 FT /evidence="ECO:0007829|PDB:1VEM" FT TURN 331..334 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 335..338 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 343..353 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 356..360 FT /evidence="ECO:0007829|PDB:1VEM" FT TURN 370..372 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 376..390 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 394..397 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 405..417 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 421..426 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 428..432 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 435..444 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 449..458 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 466..473 FT /evidence="ECO:0007829|PDB:1VEM" FT HELIX 474..476 FT /evidence="ECO:0007829|PDB:1VEM" FT TURN 477..479 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 481..484 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 489..491 FT /evidence="ECO:0007829|PDB:1VEM" FT TURN 492..495 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 496..504 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 509..516 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 522..525 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 530..534 FT /evidence="ECO:0007829|PDB:1VEM" FT STRAND 541..545 FT /evidence="ECO:0007829|PDB:1VEM" SQ SEQUENCE 546 AA; 61629 MW; A8F7CFC96ED6979B CRC64; MKNQFQYCCI VILSVVMLFV SLLIPQASSA AVNGKGMNPD YKAYLMAPLK KIPEVTNWET FENDLRWAKQ NGFYAITVDF WWGDMEKNGD QQFDFSYAQR FAQSVKNAGM KMIPIISTHQ CGGNVGDDCN VPIPSWVWNQ KSDDSLYFKS ETGTVNKETL NPLASDVIRK EYGELYTAFA AAMKPYKDVI AKIYLSGGPA GELRYPSYTT SDGTGYPSRG KFQAYTEFAK SKFRLWVLNK YGSLNEVNKA WGTKLISELA ILPPSDGEQF LMNGYLSMYG KDYLEWYQGI LENHTKLIGE LAHNAFDTTF QVPIGAKIAG VHWQYNNPTI PHGAEKPAGY NDYSHLLDAF KSAKLDVTFT CLEMTDKGSY PEYSMPKTLV QNIATLANEK GIVLNGENAL SIGNEEEYKR VAEMAFNYNF AGFTLLRYQD VMYNNSLMGK FKDLLGVTPV MQTIVVKNVP TTIGDTVYIT GNRAELGSWD TKQYPIQLYY DSHSNDWRGN VVLPAERNIE FKAFIKSKDG TVKSWQTIQQ SWNPVPLKTT SHTSSW //