ID D7LD98_ARALL Unreviewed; 677 AA.
AC D7LD98;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
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 ORFNames=ARALYDRAFT_346398 {ECO:0000313|EMBL:EFH58297.1};
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; GL348716; EFH58297.1; -; Genomic_DNA.
DR RefSeq; XP_002882038.1; XM_002881992.1.
DR AlphaFoldDB; D7LD98; -.
DR STRING; 81972.D7LD98; -.
DR EnsemblPlants; fgenesh1_pg.C_scaffold_4002740; fgenesh1_pg.C_scaffold_4002740; fgenesh1_pg.C_scaffold_4002740.
DR GeneID; 9316272; -.
DR Gramene; fgenesh1_pg.C_scaffold_4002740; fgenesh1_pg.C_scaffold_4002740; fgenesh1_pg.C_scaffold_4002740.
DR KEGG; aly:9316272; -.
DR eggNOG; ENOG502QTBX; Eukaryota.
DR HOGENOM; CLU_016754_4_0_1; -.
DR OrthoDB; 46229at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; 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:0003700; F:DNA-binding transcription factor activity; IEA:EnsemblPlants.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048831; P:regulation of shoot system development; IEA:EnsemblPlants.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR008540; BES1_N.
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:SF62; BETA-AMYLASE 7; 1.
DR Pfam; PF05687; BES1_N; 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 DOMAIN 65..200
FT /note="BES1/BZR1 plant transcription factor N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05687"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 421
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 617
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
SQ SEQUENCE 677 AA; 75580 MW; 4AB4CF914DE829A4 CRC64;
MATDMQKLLG TSEEDDDEEM DMDVKEEDDG DRRNRDTRAA SGSSNDEFMF QQSMQDQVGT
PGGGGSRRSR PLEEKERTKL RERHRRAITA RILGGLRRHG NYNLRVRADI NDVIAALARE
AGWVVLPDGT TFPAKSQGTK PTGGSSAVAA GSSASHIASQ QTSTPALRVV SSGRRSPVEL
SACRMKGVFT PASSPYDKFP TQSPELVGSV NKAEGLVGCS VDVINSKQIL DIPPNLTEQD
FSGTPYVPVY VMLPLGVINM KCELADRDGL VKHLRILKSI HVDGVKVDCW WGIVEAHSPQ
EYNWTGYRQL FQMVRDLNLK IQVLMSFHEC GGNVGDDVCI PLPHWVAEIG RTNPDIYFTD
REGRRNPECL SWGIDKERIL RGRTALEVYF DYMRSFRIEL AEFLEDGVIS MVEIGLGPCG
ELRYPSCPIK HGWRYPGVGE FQCYDKYLSK SLRKAAESRG HLFWARGPDN TGSYNSQPQG
TGFFCDGGDY DGLYGRFFLK WYSQVLIDHA DQILSLAKLV FDSSCIAAKL PDVHWWYRTA
SHAAELTAGF YNPSNRDGYA AIASTLKKHG ATLSFVSGEV QVLNRPDDFS GALGEPEAVA
WQVLNAAWDS DTPVARENSL PCHDRVGYNK MLESVKFRND PDRRHLSSFA YSRLVPALME
EHNIVEFERF VKKLHGN
//
