ID S0AXZ0_ENTHI Unreviewed; 436 AA.
AC S0AXZ0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759 {ECO:0000313|EMBL:BAN38487.1};
RN [1] {ECO:0000313|EMBL:BAN38487.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HM-1:IMSS {ECO:0000313|EMBL:BAN38487.1};
RA Hiranuka K., Kumagai M., Wakaguri H., Suzuki Y., Sugano S., Watanabe J.,
RA Makioka A.;
RT "Short 5' UTR of Entamoeba genes.";
RL Submitted (JUN-2012) 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; AK419843; BAN38487.1; -; mRNA.
DR AlphaFoldDB; S0AXZ0; -.
DR VEuPathDB; AmoebaDB:EHI5A_142640; -.
DR VEuPathDB; AmoebaDB:EHI7A_099610; -.
DR VEuPathDB; AmoebaDB:EHI8A_201720; -.
DR VEuPathDB; AmoebaDB:EHI_192590; -.
DR VEuPathDB; AmoebaDB:KM1_053920; -.
DR VEuPathDB; AmoebaDB:KM1_149110; -.
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; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR31352:SF40; BETA-AMYLASE 5; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00506; BETA_AMYLASE_1; 1.
PE 2: Evidence at transcript level;
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}.
SQ SEQUENCE 436 AA; 47281 MW; B2A3227972E9FF8B CRC64;
MLLTLCFISI AFAVEVNVML PLDVVTSNGL NNKNQLKKDF SKLKSGGVAG VMGDVWWGLV
ETSPKSYNWN GYKELIALCK ETGLKFQAVM SFHKCGGNVG DSVNIPIPQW VRNAGSSQDA
FFKDPQGSKN DEYIAFSADS MSIFQGRTPL QMYKDFMSSF KSTFSSYIND GTINEIQVGM
GPCGETRYPS YPLSRWSYCG VGEFQCSDKN SLSKLASAAS NVGHSEWGHA SPSNAGNYNS
KPPSSTGFFG NGNDNYKSEY GKFFLGWYQQ LLLDHANNVL SAAKSVFGNL AIAGKVAGIH
WWYNDQSHAA ELTAGYYNTN NQNAYANIAN VFKKSGARFD FTCLEMSGTD GNCGSTPANL
VSQAYKAAGS AGIGKCGENA LELCGYGGCN TNGFSQIVKQ AKSNGLISFT YLRMTRALLD
DGTAWGQFCS FVNSMR
//