ID A0A059B1Z6_EUCGR Unreviewed; 584 AA.
AC A0A059B1Z6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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_H02879 {ECO:0000313|EMBL:KCW60153.1};
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:KCW60153.1};
RN [1] {ECO:0000313|EMBL:KCW60153.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW60153.1};
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; KK198760; KCW60153.1; -; Genomic_DNA.
DR RefSeq; XP_010023784.1; XM_010025482.2.
DR AlphaFoldDB; A0A059B1Z6; -.
DR STRING; 71139.A0A059B1Z6; -.
DR EnsemblPlants; KCW60153; KCW60153; EUGRSUZ_H02879.
DR GeneID; 104414396; -.
DR Gramene; KCW60153; KCW60153; EUGRSUZ_H02879.
DR KEGG; egr:104414396; -.
DR eggNOG; ENOG502QTBX; Eukaryota.
DR InParanoid; A0A059B1Z6; -.
DR OMA; WGRRNCE; -.
DR OrthoDB; 46229at2759; -.
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:SF31; BETA-AMYLASE 1, 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.
DR PROSITE; PS00679; BETA_AMYLASE_2; 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 289
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 487
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 402
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 488..489
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 526
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ SEQUENCE 584 AA; 64682 MW; 80E3A6EC53D918F7 CRC64;
MALSMTHQIG TLAGTPIHAE SGSGAGEPST ATVSAAAVWK SPAPSIRCRA QKPDALDALS
PPLSPCRSPV LGGIRPDLSV ACQAFAAEME ALPQAAVREH KEVAPAAGSR EKGSGGVPVF
VMMPLDSVTM NNTVNRRKAM NASLQALKSA GVEGIMMDVW WGLVEREPGS YNWGGYAELL
EMAKKHGLKV QAVMSFHQCG GNVGDSCSIP LPKWAVEEVD KDPDLAYTDQ WGRRNYEYIS
LGCDTLPVLK GRTPVQCYAD FMRAFRDNFQ HLLGETIVEI QVGMGPAGEL RYPSYPEQNG
TWKFPGIGAF QCYDKYMLSS LKAAAEAAGK AEWGHTGPTD AGHYNNWPED APFFKKEGGG
WNSQYGEFFL SWYSQMLLDH GERILSSAKS VFENTGTKIS VKVAGIHWHY GTRSHAPELT
AGYYNTRYRD GYLPIAQMLA RHGAIFNFTC IEMRDHEQPQ DALCAPEKLV KQVALATQKA
EVPLAGENAL QRYDDYAHEQ ILRSALLNID GYPQEDKEMC AFTYLRMNPD LFQADNWRRF
VAFVKKMKEG KNLHRCWEQV EREAEHFVHV TQPLVQEAAV ALRH
//
