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
//
