ID A0A059C078_EUCGR Unreviewed; 546 AA.
AC A0A059C078;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=EUGRSUZ_E00138 {ECO:0000313|EMBL:KCW71611.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW71611.1};
RN [1] {ECO:0000313|EMBL:KCW71611.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW71611.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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; KK198757; KCW71611.1; -; Genomic_DNA.
DR RefSeq; XP_010055131.1; XM_010056829.2.
DR AlphaFoldDB; A0A059C078; -.
DR STRING; 71139.A0A059C078; -.
DR EnsemblPlants; KCW71611; KCW71611; EUGRSUZ_E00138.
DR GeneID; 104443441; -.
DR Gramene; KCW71611; KCW71611; EUGRSUZ_E00138.
DR KEGG; egr:104443441; -.
DR eggNOG; ENOG502QTBX; Eukaryota.
DR InParanoid; A0A059C078; -.
DR OMA; YKRLFHM; -.
DR OrthoDB; 46229at2759; -.
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}.
FT ACT_SITE 283
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 479
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 396
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 438
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 480..481
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 515
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ SEQUENCE 546 AA; 61771 MW; 25DDBB23614C31F1 CRC64;
MAPAPAPSVL LATSGASCPD ARAWRWSWSS LPRVGAADWR SRGSARCSPR RAGDGRLVAG
ARRLRTRAMV RKPEDGRIAG GSVDASEDEQ VADLPIKIPE RDFAGTPYVP VYVMLPLGVV
NLQCELVDPE GLLEQLKILK SVNVDGVMID CWWGIVEADA PQAYNWSGYK RLFQMVRDLK
LKLQVVMSFH DCGGNVGDDV HIPLPSWVME IGQKNPDIYF TDREGRRNME CLTWGIDKER
VLRGRTAVEV YFDYMRSFRV EFNEFFEDGI ISEIEIGLGP CGELRYPSYP AKHGWEYPGI
GEFQCYDRYL MKSLEKAAEV RGHSFWGRAP DNAGCYNSRP HDTSFFRDGG EYDGYYGRFF
LNWYSRVLID HGDRVLSLAN LAFEGCCIAV KLSGIHWWYK TASHAAELTA GFYNSCNRDG
YATIVSMLKK HEIAMNFTCV ELRTLDQYED FPEAMADPEG LVWQVLNAAW DAQIPVASEN
ALPCYDGEGY NKILENAKPR DDPDGRHLSA FTYLRLSPTL TEGNNLMEFE RFVKRMHGET
VLDKLM
//
