BBMA_BACIU
ID BBMA_BACIU Reviewed; 588 AA.
AC Q9R9H8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Intracellular maltogenic amylase;
DE EC=3.2.1.-;
GN Name=bbmA;
OS Bacillus subtilis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=SUH4-2;
RX PubMed=10825545; DOI=10.1016/s0167-4838(00)00037-6;
RA Cho H.-Y., Kim Y.-W., Kim T.-J., Lee H.-S., Kim D.-Y., Kim J.-W.,
RA Lee Y.-W., Leed S.-B., Park K.-H.;
RT "Molecular characterization of a dimeric intracellular maltogenic amylase
RT of Bacillus subtilis SUH4-2.";
RL Biochim. Biophys. Acta 1478:333-340(2000).
CC -!- FUNCTION: Hydrolyzes beta-cyclodextrin to maltose and glucose, soluble
CC starch to maltose and glucose, and pullulan to panose with trace
CC amounts of maltose and glucose. It is also able to hydrolyze acarbose.
CC Can also exhibit a transglycosylation activity transferring glucose or
CC maltose to another moiety of sugars by forming alpha-(1,6)- and alpha-
CC (1,3)-glycosidic linkages upon the hydrolysis of substrate at
CC concentrations of 5% or higher. {ECO:0000269|PubMed:10825545}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P38940};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P38940};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. Stable at pH 6.0 and about 80% of the enzyme
CC activity remained between pH 7.0 and pH 8.0.
CC {ECO:0000269|PubMed:10825545};
CC Temperature dependence:
CC Optimum temperature is 40-45 degrees Celsius.
CC {ECO:0000269|PubMed:10825545};
CC -!- SUBUNIT: Monomer or homodimer; in equilibrium.
CC {ECO:0000269|PubMed:10825545}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10825545}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. BbmA
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF23874.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF115340; AAF23874.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_032729161.1; NZ_PISO01000015.1.
DR AlphaFoldDB; Q9R9H8; -.
DR SMR; Q9R9H8; -.
DR STRING; 483913.AN935_17415; -.
DR CAZy; CBM34; Carbohydrate-Binding Module Family 34.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd02857; E_set_CDase_PDE_N; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.90.400.10; -; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004185; Glyco_hydro_13_lg-like_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR045857; O16G_dom_2.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02903; Alpha-amylase_N; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW Metal-binding.
FT CHAIN 1..588
FT /note="Intracellular maltogenic amylase"
FT /id="PRO_0000366978"
FT ACT_SITE 327
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT ACT_SITE 356
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 422..423
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 467
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT BINDING 471
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P38940"
FT SITE 423
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 588 AA; 68700 MW; 00EE31A2A54BE14F CRC64;
MEYAAIHHQP FSTDAYSYDG RTVHIKIRTK KGDADHIRFI WGDPYEYNDG KWSANEQPMR
KIAATEMHDY WFAEVVPPFR RLQYAFVVTD DHEDIFFGSS GVCPYNEKTL ETIHYYFKFP
FVHEADTFQA PEWVKSTVWY QIFPERFANG REDLSPKNAL PWGSKDPGVN DFFGGDLQGI
VDKLDYLEDL GVNGIYLTPI FSAPSNHKYD TLDYFSIDPH FGDPEIFRTL VSQLHQRGMR
IMLDAVFNHI GSASPQWQDV VKNGDQSRYK DWFHIHSFPV TDDNYDRFAF TADMPKLNTA
NPEVQKYLLD IALYWIREFD IDGWRLDVAN EVDHVFWKTF RQAVSTEKPD VYILGEIWHS
AEPWLRGDEF HAAMNYPFTE PMIEYFADQT ISASRMAHRV NAHLMNGMKQ ANEVMFNLLD
SHDTKRLLTR CRNDEKKARA LLAFMFAQTG SPCIYYGTEI GLDGENDPLC RKCMVWEKEK
QNQDMLQFMK RLIALRKQEN TLLTEGHLEW NLLDDKNDFI SFSRTLDEKI LIYFFNQGNV
VQHISLRELN IDRNNKICDA WTEQPLHYHD VIAVQPGEFL ILSAAAPV
