ID A0A059BS05_EUCGR Unreviewed; 364 AA.
AC A0A059BS05;
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=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN ORFNames=EUGRSUZ_F02347 {ECO:0000313|EMBL:KCW68749.1};
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:KCW68749.1};
RN [1] {ECO:0000313|EMBL:KCW68749.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW68749.1};
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=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548,
CC ECO:0000256|RuleBase:RU361134};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; KK198758; KCW68749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059BS05; -.
DR EnsemblPlants; KCW68749; KCW68749; EUGRSUZ_F02347.
DR Gramene; KCW68749; KCW68749; EUGRSUZ_F02347.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11314; AmyAc_arch_bac_plant_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF37; ALPHA-AMYLASE 1; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..364
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001574578"
FT DOMAIN 25..355
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 364 AA; 40675 MW; 373563226B73E41D CRC64;
MMSSPSLFWL FVISVSYLAA SASPALLFQG FNWESWKKEG GWYNSLKNLV PDLANAGITH
VWLPPPSQSA AQQGYLPGRL YDLNASSYGN QDELKHLIDA FHQKGIKCLA DIVINHRTAE
KQDSRGIWCI FEGGTPDDRL DWGPSFICRN DANYSDGMGN PDTGEDYEFA PDIDHLNPRV
QKELSDWMNW LKSDIGFDGW RFDFVKGYSS SITKIYMDRT LPNFAVGENW ESLSYGQDGK
LNPNQDAHRL KLADWVNAAG GAITAFDFTT KGILQAAIER ELWRLRDSNG MPPGLIGLQP
RSAVTFIDNH DTGSTQKMWP FPSYKVMQGY AYILTHPGVP SIVMSSSSRL IDSSHCCPVS
VPCL
//