ID A0A059B466_EUCGR Unreviewed; 531 AA.
AC A0A059B466;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Beta-amylase {ECO:0000256|RuleBase:RU000509};
DE EC=3.2.1.2 {ECO:0000256|RuleBase:RU000509};
GN ORFNames=EUGRSUZ_H03767 {ECO:0000313|EMBL:KCW61012.1};
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:KCW61012.1};
RN [1] {ECO:0000313|EMBL:KCW61012.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW61012.1};
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|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; KCW61012.1; -; Genomic_DNA.
DR RefSeq; XP_010024563.1; XM_010026261.2.
DR AlphaFoldDB; A0A059B466; -.
DR EnsemblPlants; KCW61012; KCW61012; EUGRSUZ_H03767.
DR GeneID; 104415036; -.
DR Gramene; KCW61012; KCW61012; EUGRSUZ_H03767.
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; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR31352:SF3; INACTIVE BETA-AMYLASE 9; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000509};
KW Glycosidase {ECO:0000256|RuleBase:RU000509};
KW Hydrolase {ECO:0000256|RuleBase:RU000509};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU000509}.
FT REGION 501..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 445
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
SQ SEQUENCE 531 AA; 58319 MW; A64F9604BF9A6074 CRC64;
MEVSVIGSSQ ANILKTDLAC RELGLLSFKN GSRVSWGKSQ ISFGRSCGLR NSGVRLTLKA
VQTEAIRPQK ISRPQSHGVR LYVGLPLDAV SYCNAVNHAK AIAAGLKALK LLGVEGVELP
IWWGVVEKEA MGKYDWSGYL ALVEMVHKVG LKLHVSLCFH GSKHAKIPLP EWVIKIGEQN
PSIFFTDRTG QQYKECLSLA VDEVPVLEGK TPVEVYNDFC ESFKSSFSSF IGSTIDGISM
GLGPDGELRY PSHQGLSRSS KVPGVGEFQC YDKSMLALLK EHGETTGNPL WGLGGPHDAP
AYDASPSSNS FFKDDGGSWE SPYGDFFLSW YSSLLVRHAD RLLSLASSAF GDSEVAIYSK
VPLVHQWYKT RSHPAELTAG FYNTQNRDGY EVIAEMFAQH SCKMILPGMD LSDEGQLQEG
LSSPEQLLGQ IWSACKKHGV EVSGENSSDA VAHGGFEQIR KHLSGEDAAH SFFYQRMGAY
FFSPEHFPSF TQLVRNMKQP QMHTDDLLSE EEKAKEPVAA TSESGIQMQT A
//
