ID   I0BEP8_9BACL            Unreviewed;      1129 AA.
AC   I0BEP8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=beta-amylase {ECO:0000256|ARBA:ARBA00012594};
DE            EC=3.2.1.2 {ECO:0000256|ARBA:ARBA00012594};
GN   ORFNames=B2K_08955 {ECO:0000313|EMBL:AFH60845.1};
OS   Paenibacillus mucilaginosus K02.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=997761 {ECO:0000313|EMBL:AFH60845.1, ECO:0000313|Proteomes:UP000007392};
RN   [1] {ECO:0000313|EMBL:AFH60845.1, ECO:0000313|Proteomes:UP000007392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K02 {ECO:0000313|EMBL:AFH60845.1,
RC   ECO:0000313|Proteomes:UP000007392};
RA   Xiao B., Sun L., Xiao L., Lian B.;
RT   "Complete genome sequence of Paenibacillus mucilaginosus K02.";
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
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};
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};
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DR   EMBL; CP003422; AFH60845.1; -; Genomic_DNA.
DR   RefSeq; WP_014650037.1; NC_017672.3.
DR   AlphaFoldDB; I0BEP8; -.
DR   KEGG; pmw:B2K_08955; -.
DR   PATRIC; fig|997761.3.peg.1740; -.
DR   HOGENOM; CLU_279379_0_0_9; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000007392; 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; cd11339; AmyAc_bac_CMD_like_2; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR005085; CBM25.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR001554; Glyco_hydro_14.
DR   InterPro; IPR018238; Glyco_hydro_14_CS.
DR   InterPro; IPR000125; Glyco_hydro_14A_bac.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF03423; CBM_25; 2.
DR   Pfam; PF01373; Glyco_hydro_14; 1.
DR   PRINTS; PR00750; BETAAMYLASE.
DR   PRINTS; PR00841; GLHYDLASE14A.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM01066; CBM_25; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR   PROSITE; PS00679; BETA_AMYLASE_2; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR600125-3};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR600125-3};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          456..534
FT                   /note="Carbohydrate binding module family 25"
FT                   /evidence="ECO:0000259|SMART:SM01066"
FT   DOMAIN          561..639
FT                   /note="Carbohydrate binding module family 25"
FT                   /evidence="ECO:0000259|SMART:SM01066"
FT   DOMAIN          684..1040
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          1052..1129
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
FT   ACT_SITE        198
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-1"
FT   ACT_SITE        394
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         314
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT   BINDING         357
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT   BINDING         395..396
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
FT   BINDING         424
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600125-2"
SQ   SEQUENCE   1129 AA;  122831 MW;  4A7DCA9B8DC032A4 CRC64;
     MSSARFLMKK ASMLLLSLVM LLTTVIGLGP SRTEAAVAND FQASVMGPLA QVTDWNAFKN
     QLRTLKSNGV YAITTDVWWG LVESAGDNQF NWSYYQTYAS AVREAGLKWV PILSTHKCGG
     NVGDDCNIPL PAWLWNKGTA DEMQFKSETG YVNNEAVSPF WSGIGTQYSE LYASFASTFA
     GYKDIIPKIY LSGGPSGELR YPSYYPAAGW SYPSRGKFQV YTETAKNAFR TAMTTKYGSL
     SGINSAWGTN LTSVSQINPP TDGDGFYTSG GYNSTYGKDF LRWYQSVLEN HLGVIGTAAH
     QKFDSVFGVP IGAKVSGVHW QMSNPTMPHS AEQAAGYYDY NTLLQKFKDT NLDLTFTCLE
     MFDNAAAPNY SQPSTLVDTV SAIANAKGVR LNGENALPAS GTSAFGKIQE KLTRFSYNGF
     TLLRLANVVN ADGSVTGEMA NFKNYVVSLA KPADTHNLIT IYYKKGFATP YLHYRPAGGT
     WTTAPGLKMA DSEVSGYAKA TVDIGAATQL EAAFNDGNNT WDSNATKNYF FGVGTFTYTP
     GSNGAAGTIT QGAPSGGGGT TNTVTVYYKK GFTTPYIHYR PAGGTWTTAP GVRMADAEVS
     GYAKATVEIG TATQLEAAFN DGNNTWDSNA QKNYFFGTGT FTYTPGANGA AGTITQGAPT
     GSGGGDGGGG IVTPVDWSTR SIYFIMTDRF VNGDTSNDNY GGFAANKSDP GKWHGGDFQG
     IINNLDYIKN MGFNAIWITP VTMQKSVNAY HGYHTYDFYA VDGHLGTMEK FQELVKTAHA
     KNIAVMLDVV LNHTGDFQPS NGYAKAPFDK YDWYHHNGEI TSTDYNQNNQ WKIENGDVAG
     LDDLNHENTA VMAELNNWIQ WLIAQSGVDG LRVDTAKHVP KSYLKSFDTA ANTFTFAEVF
     HGDPAYVGDY SNYLDAALDF PMYYTIRDVF GKDGSPTLIR DRYTSDSKYR DARLNGLFLD
     NHDVKRFLNE ASGNPSNTSD KWPQLKAALG FLFTSRGIPI VYQGTELGYS GGDDPANRED
     VVPNANHDLY KYIAKLNGVR NSHPALQNGT QKEKWADSTV YGFQRSKNGD EAVVLINNSW
     SSQTRTVGSL DNLTSGTTLR NQLGTDSVTV NNGSVTVTLA PKEVKIFTK
//