ID A0A0A1TW34_ENTIV Unreviewed; 431 AA.
AC A0A0A1TW34;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=EIN_173970 {ECO:0000313|EMBL:ELP84722.1};
OS Entamoeba invadens IP1.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP84722.1, ECO:0000313|Proteomes:UP000014680};
RN [1] {ECO:0000313|EMBL:ELP84722.1, ECO:0000313|Proteomes:UP000014680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP1 {ECO:0000313|EMBL:ELP84722.1,
RC ECO:0000313|Proteomes:UP000014680};
RA Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL Submitted (OCT-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; KB207112; ELP84722.1; -; Genomic_DNA.
DR RefSeq; XP_004184068.1; XM_004184020.1.
DR AlphaFoldDB; A0A0A1TW34; -.
DR EnsemblProtists; ELP84722; ELP84722; EIN_173970.
DR GeneID; 14883737; -.
DR KEGG; eiv:EIN_173970; -.
DR VEuPathDB; AmoebaDB:EIN_173970; -.
DR OrthoDB; 46229at2759; -.
DR Proteomes; UP000014680; Unassembled WGS sequence.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000014680}.
SQ SEQUENCE 431 AA; 46252 MW; 1C958C5A1C94F6F6 CRC64;
MLLLLLTVAL SVEVNVMLPL DVVGSSGLTN SAQLKNDFTK LKSGGVAGVM TDVWWGLVET
SAKSYNWAGY TDMAKLAKDA GLKLQVVMSF HKCGGNVGDT CNIPIPSWAR SSSSAAFKDP
QGNTNDEYIS FGADSLAVFG GRTPLQIYKD FMSAFKTKFA SYISDGTINE VQVGMGPCGE
TRYPAYPLSR WTYCGVGEFQ CSDSNSLSQL QSAATAAGHS EWGKASPSNA GTYNSKPPSS
TGFFGSGSDN YKSEYGKFFL NWYHQQLIKH AENILSSAKS VFGSLAIAGK VAGIHWWYND
NSHAAELTAG YYNTNSQDAY SNIAKAFKKY GARFDFTCLE MTGTDSNCGS TPANLVNQAY
TAAGSAGAVK CGENALELCG YGGCNTSGFN QIVSQAKKYG LTAFTYLRLT RALLDDGTAW
SQFKSFVNNM K
//
