ID A9UGN2_HORMA Unreviewed; 223 AA.
AC A9UGN2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 45.
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};
DE Flags: Fragment;
OS Hordeum marinum (Seaside barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4519 {ECO:0000313|EMBL:ABX79600.1};
RN [1] {ECO:0000313|EMBL:ABX79600.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18372193; DOI=10.1016/j.ympev.2008.02.008;
RA Mason-Gamer R.J.;
RT "Allohexaploidy, introgression, and the complex phylogenetic history of
RT Elymus repens (Poaceae).";
RL Mol. Phylogenet. Evol. 47:598-611(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU282258; ABX79600.1; -; Genomic_DNA.
DR AlphaFoldDB; A9UGN2; -.
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:SF57; 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.
DR PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR PROSITE; PS00679; BETA_AMYLASE_2; 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}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABX79600.1"
FT NON_TER 223
FT /evidence="ECO:0000313|EMBL:ABX79600.1"
SQ SEQUENCE 223 AA; 25168 MW; 6BC4B52EDBD3A3EE CRC64;
AIMSFHQCGG NVGDVVNIPI PQWVRDIGAG DPDIFYTNRS GTRSIEYLTL GVDDQPLFHG
RTAIQMYADY MASFRENMKK FLDAGTIVDI EVGLGPAGEM RYPSYPQSQG WVFPGIGEFI
CYDKYLEADF KAAAAKAGHP EWELPDDAGE YNDTPEKMQF FKENGTHLTE KGKFFLSWYS
NKLIKHGDKI LDEANKVFLG CRVQLAIKTS GIHWWYRVPN HAA
//