BBMA_BACSU
ID BBMA_BACSU Reviewed; 588 AA.
AC O06988; Q795G7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Intracellular maltogenic amylase;
DE EC=3.2.1.-;
GN Name=bbmA; Synonyms=yvdF; OrderedLocusNames=BSU34620;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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 (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Monomer or homodimer; in equilibrium.
CC {ECO:0000250|UniProtKB:Q9R9H8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9R9H8}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. BbmA
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB08035.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB15467.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z94043; CAB08035.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB15467.1; ALT_INIT; Genomic_DNA.
DR PIR; F70033; F70033.
DR RefSeq; NP_391342.1; NC_000964.3.
DR AlphaFoldDB; O06988; -.
DR SMR; O06988; -.
DR STRING; 224308.BSU34620; -.
DR CAZy; CBM34; Carbohydrate-Binding Module Family 34.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; O06988; -.
DR PRIDE; O06988; -.
DR EnsemblBacteria; CAB15467; CAB15467; BSU_34620.
DR GeneID; 936514; -.
DR KEGG; bsu:BSU34620; -.
DR PATRIC; fig|224308.43.peg.3626; -.
DR eggNOG; COG0366; Bacteria.
DR InParanoid; O06988; -.
DR OMA; TPDWVKH; -.
DR BioCyc; BSUB:BSU34620-MON; -.
DR Proteomes; UP000001570; Chromosome.
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 3: Inferred from homology;
KW Calcium; Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW Metal-binding; Reference proteome.
FT CHAIN 1..588
FT /note="Intracellular maltogenic amylase"
FT /id="PRO_0000366977"
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; 68722 MW; 6132681370919DFE CRC64;
MEYAAIHHQP FSTDAYSYDG RTVHIKIRTK KGDADHIRFI WGDPYEYNDG KWSANEQPMR
KIAATEMHDY WFAEVVPPFR RLQYAFVVTD DHEDIFFGSS GVCPYNEKTL ETIHYYFKFP
FVHEADTFQA PEWVKSTVWY QIFPERFANG REDLSPKNAL PWGSKDPDVN DFFGGDLQGI
VDKLDYLEDL GVNGIYLTPI FSAPSNHKYD TLDYFSIDPH FGDPELFRTL VSQLHQRGMR
IMLDAVFNHI GSASPQWQDV VKNGDQSRYK DWFHIHSFPV TDDNYDRFAF TADMPKLNTA
NPEVQKYLLD IALYWIREFD IDGWRLDVAN EVDHVFWKTF RQAVSTEKPD VYILGEIWHS
AEPWLRGDEF HAAMNYPFTE PMIEYFADQT ISASRMAHRV NAHLMNGMKQ ANEVMFNLLD
SHDTKRLLTR CRNDEKKARA LLAFMFAQTG SPCIYYGTEI GLNGENDPLC RKCMVWEKEK
QNQDMLQFMK RLIALRKQEN TLLTEGHLEW NLLDDKNDFI SFSRTLDEKI LIYFFNQGNV
VQHVSLRELN IDRNKKICDA WTEQPLQHHD VIAVQPGEFL ILSAAAPV
