AMYB_BACCE
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 03-AUG-2022, entry version 116.
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; Firmicutes; 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}.
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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; 2.60.40.10; -; 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; PTHR31352; 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; SSF51445; 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
