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Database: UniProt
Entry: A9UGN2_HORMA
LinkDB: A9UGN2_HORMA
Original site: A9UGN2_HORMA 
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}.
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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
//
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