ID   D7M5N4_ARALL            Unreviewed;       542 AA.
AC   D7M5N4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Beta-amylase {ECO:0000256|ARBA:ARBA00012594, ECO:0000256|RuleBase:RU000509};
DE            EC=3.2.1.2 {ECO:0000256|ARBA:ARBA00012594, ECO:0000256|RuleBase:RU000509};
GN   Name=BMY9 {ECO:0000313|EMBL:EFH51283.1};
GN   ORFNames=ARALYDRAFT_490517 {ECO:0000313|EMBL:EFH51283.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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         ECO:0000256|RuleBase:RU000509};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family.
CC       {ECO:0000256|ARBA:ARBA00005652, ECO:0000256|RuleBase:RU000509}.
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DR   EMBL; GL348718; EFH51283.1; -; Genomic_DNA.
DR   RefSeq; XP_002875024.1; XM_002874978.1.
DR   AlphaFoldDB; D7M5N4; -.
DR   STRING; 81972.D7M5N4; -.
DR   EnsemblPlants; fgenesh2_kg.6__3651__AT4G00490.1; fgenesh2_kg.6__3651__AT4G00490.1; fgenesh2_kg.6__3651__AT4G00490.1.
DR   Gramene; fgenesh2_kg.6__3651__AT4G00490.1; fgenesh2_kg.6__3651__AT4G00490.1; fgenesh2_kg.6__3651__AT4G00490.1.
DR   eggNOG; ENOG502QTBX; Eukaryota.
DR   HOGENOM; CLU_016754_5_1_1; -.
DR   OrthoDB; 46229at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001554; Glyco_hydro_14.
DR   InterPro; IPR018238; Glyco_hydro_14_CS.
DR   InterPro; IPR001371; Glyco_hydro_14B_pln.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31352:SF47; BETA-AMYLASE 2, CHLOROPLASTIC; 1.
DR   Pfam; PF01373; Glyco_hydro_14; 1.
DR   PRINTS; PR00750; BETAAMYLASE.
DR   PRINTS; PR00842; GLHYDLASE14B.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00506; BETA_AMYLASE_1; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000509};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000509};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000509};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU000509};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT   ACT_SITE        269
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   ACT_SITE        465
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         377
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         382
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         424
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         466..467
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT   BINDING         501
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ   SEQUENCE   542 AA;  61392 MW;  82A54A208BE9C912 CRC64;
     MAIRLTHSVI PVSVKLGAPA RVSARSSLPF SVGDWRGVST FSGARPSLVS AKVKLRAEST
     EEDPVPIDDD DSTDQLVDEE IVHFEERDFS GTARVPVYVM LPLGVIDMNS QVVEPEELLD
     QLRTLKSVDV DGVMVDCWWG LVEAHTPQVY NWSGYKKLFQ MIRELGLKIQ VVMSFHECGG
     NVGDDVHIQL PEWVREIGQS NPDIYFTDRA GRRNTECLTW GIDKQRVLRG RTALEVYFDY
     MRSFRVEFDE FFEDKIIPEI EVGLGPCGEL RYPSYPAQFG WRYPGIGEFQ CYDKYLMKSL
     KEAAEVRGHS FWGRGPDNTE TYNSTPHGTG FFRDGGDYDS YYGRFFLNWY SRVLIDHGDR
     VLAMANLAFE GTCIAAKLSG IHWWYKTASH AAELTAGFYN SSNRDGYGPI AAMFKKHDAA
     LNFTCVELRT LDQHEDFPEA LADPEGLVWQ VLNAAWDASI PVASENALPC YDREGYNKIL
     ENAKPLTDPD GRHLSCFTYL RLNPTLMESQ NFKEFERFVK RMHGEAVPDL GLAPGTQETK
     PE
//