ID B1KZG7_CLOBM Unreviewed; 542 AA.
AC B1KZG7;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Beta-amylase {ECO:0000256|RuleBase:RU000509};
DE EC=3.2.1.2 {ECO:0000256|RuleBase:RU000509};
GN OrderedLocusNames=CLK_0646 {ECO:0000313|EMBL:ACA57155.1};
OS Clostridium botulinum (strain Loch Maree / Type A3).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498214 {ECO:0000313|EMBL:ACA57155.1, ECO:0000313|Proteomes:UP000000722};
RN [1] {ECO:0000313|EMBL:ACA57155.1, ECO:0000313|Proteomes:UP000000722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Loch Maree / Type A3 {ECO:0000313|Proteomes:UP000000722};
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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|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|RuleBase:RU000509}.
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DR EMBL; CP000962; ACA57155.1; -; Genomic_DNA.
DR RefSeq; WP_012344936.1; NC_010520.1.
DR AlphaFoldDB; B1KZG7; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR KEGG; cbl:CLK_0646; -.
DR HOGENOM; CLU_016754_6_0_9; -.
DR Proteomes; UP000000722; Chromosome.
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; 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; 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|RuleBase:RU000509, ECO:0000313|EMBL:ACA57155.1};
KW Hydrolase {ECO:0000256|RuleBase:RU000509, ECO:0000313|EMBL:ACA57155.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR600125-3};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU000509}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..542
FT /note="Beta-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002765043"
FT DOMAIN 443..542
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT ACT_SITE 198
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600125-1"
FT ACT_SITE 391
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600125-1"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR600125-3"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR600125-3"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR600125-3"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT BINDING 392..393
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT BINDING 422
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
SQ SEQUENCE 542 AA; 61993 MW; ED94312F62A9E400 CRC64;
MYYGNKILKK YGNFILSLVL AFALSLCFTF KAFAANMSPD YKCCVMGPLE RVDNWSDFKK
QLITLKNNGV YAITTDVWWG YVESEGDNKF DWSYYKTYGD TVRAAGLKWI PIISTHECGS
NVGDSVNIPL PSWLWEKDTA DNMKFKDENG VYNKETLSPW WSDTVKQYDE LYESFASNFS
SYKDIIAKIY LSSGPAGELR FPSYNPSTGW SRGFLQCYTK AAKLDFQNAM KNKYDTISRL
NSEWGTSLKS FEQVSPPTDG DNFFVNGYKT TYGNDFLTWY QGVLIKHLSN IATKAHNRFD
PVFGSTIGAK VSGVHWLMNS PNMPHAAEYC TGYYNYSTLL DQFKKSNLDL TFTCLEKEDS
NPYNYPYSAP KSLVINIANL AREKGIKYFG ENASDIYNNK KAYENCAEML FNYDFSGFTL
LRLKNIVNYD GTPNAEMAHF GNLLAIKPVP VTFTVNNVNL ESDENLYLTG SRWEMANWST
EFYPLQFKNN NGSYTITTHL AEGHNYEFKA IKKNNNGNVI WQGGYNQFYN VPKGGDSYTW
SW
//
