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Database: UniProt
Entry: H9WNE6_PINTA
LinkDB: H9WNE6_PINTA
Original site: H9WNE6_PINTA 
ID   H9WNE6_PINTA            Unreviewed;       137 AA.
AC   H9WNE6;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Beta-amylase {ECO:0000256|RuleBase:RU000509};
DE            EC=3.2.1.2 {ECO:0000256|RuleBase:RU000509};
DE   Flags: Fragment;
GN   ORFNames=0_8796_01 {ECO:0000313|EMBL:AFG63539.1};
OS   Pinus taeda (Loblolly pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3352 {ECO:0000313|EMBL:AFG63539.1};
RN   [1] {ECO:0000313|EMBL:AFG63539.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4559 {ECO:0000313|EMBL:AFG63539.1};
RC   TISSUE=Megagametophyte {ECO:0000313|EMBL:AFG63539.1};
RA   Neale D.B., Wegrzyn J.L., Lee J.M., Eckert A.J., Liechty J.D.,
RA   Stevens K.A., Langley C.H.;
RT   "Nucleotide Diversity and Divergence in the Loblolly Pine Gene Space.";
RL   Submitted (AUG-2008) 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|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; FJ083496; AFG63539.1; -; Genomic_DNA.
DR   AlphaFoldDB; H9WNE6; -.
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; IPR001371; Glyco_hydro_14B_pln.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31352:SF31; BETA-AMYLASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF01373; Glyco_hydro_14; 1.
DR   PRINTS; PR00750; BETAAMYLASE.
DR   PRINTS; PR00842; GLHYDLASE14B.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000509};
KW   Glycosidase {ECO:0000256|RuleBase:RU000509};
KW   Hydrolase {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:AFG63539.1"
FT   NON_TER         137
FT                   /evidence="ECO:0000313|EMBL:AFG63539.1"
SQ   SEQUENCE   137 AA;  15849 MW;  C2671CFC3D61FE9F CRC64;
     GSKSHAAELT AGYYNTRESD GYLPIARLFK KHRTVLNFTC FEMKDEEQPQ HARCSPEGLL
     RQVTEATRKT GVGLAGENAL QRFDGSAYAQ IMHNSNIKPR DGNDSESQMC AFTYLRMNQQ
     MFQSENWRRF VWFVRNM
//
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