ID A0A059C2U1_EUCGR Unreviewed; 551 AA.
AC A0A059C2U1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Beta-amylase {ECO:0000256|RuleBase:RU000509};
DE EC=3.2.1.2 {ECO:0000256|RuleBase:RU000509};
GN ORFNames=EUGRSUZ_E01023 {ECO:0000313|EMBL:KCW72554.1};
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:KCW72554.1};
RN [1] {ECO:0000313|EMBL:KCW72554.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW72554.1};
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; KK198757; KCW72554.1; -; Genomic_DNA.
DR RefSeq; XP_010055984.1; XM_010057682.2.
DR RefSeq; XP_018730414.1; XM_018874869.1.
DR AlphaFoldDB; A0A059C2U1; -.
DR STRING; 71139.A0A059C2U1; -.
DR EnsemblPlants; KCW72554; KCW72554; EUGRSUZ_E01023.
DR Gramene; KCW72554; KCW72554; EUGRSUZ_E01023.
DR eggNOG; ENOG502QSJZ; Eukaryota.
DR InParanoid; A0A059C2U1; -.
DR OMA; TEVQIGM; -.
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:SF7; BETA-AMYLASE; 1.
DR PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 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 46..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 261
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 462
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
SQ SEQUENCE 551 AA; 61568 MW; 191DB23674CAF5C1 CRC64;
MAIASPSAPT FSASFCGGRA DPACLTRSPP TAAAFPHPHR RLAASARLNS SSPSGAGSGS
VSPDNGDLSQ YELHHAFSSA ARRWGGSPVF VALPTDAMGP GAGQVRRRRA MAQSFRALAA
AGVEGVVMEV WWGLVEREQP RVYNWDGYWE IVTMARRCGL KVRAVMGFHQ CGTGPGDPHW
IPLPVWVLRE MEKDPDIAYS DRFGRRSMEY ISLGCDSLPV LQGRSPIQAY ADFMRNFRDA
FRPFFGNVIT GVQVGMGPAG ELRYPSCPSH KLMWAWRSRE LGEFQCYDKY MLASLNACAR
EIGMHEWGNG GPIGTGNLMQ DLENTEFFKS DDGSWNTAYG KFFLEWYSGM LLLHGERICR
EAETIFRGIE VNTSAKVAGI HWHYDTKSHP SELTAGYYNT STRDGYLPIT RMFGRYGFTL
CSTCFEMQDV EEKQMNPVSS PEGFLRQLLL AARVCEVALE GENCTSNLDD GSFQQVLKMS
KFYSDGLEKP CFSFNFVRMD KNMFEYNNWV RFTRFVRQMS VAKIFRARLG SHDIHSSAAD
SAKLGFSFAY S
//
