ID Q9FUK6_HORVU Unreviewed; 533 AA.
AC Q9FUK6;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 82.
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 vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513 {ECO:0000313|EMBL:AAG25638.1};
RN [1] {ECO:0000313|EMBL:AAG25638.1}
RP NUCLEOTIDE SEQUENCE.
RA Ma Y., Evans E.D., Logue S.J., Langridge P.;
RT "The amino acid substitutions of barley beta-amylase that improve
RT thermostability and substrate-binding affinity.";
RL Submitted (AUG-2000) 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; AF300800; AAG25638.1; -; mRNA.
DR AlphaFoldDB; Q9FUK6; -.
DR SMR; Q9FUK6; -.
DR Allergome; 420; Hor v 17.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR EnsemblPlants; HORVU.MOREX.r2.4HG0347710.1; HORVU.MOREX.r2.4HG0347710.1; HORVU.MOREX.r2.4HG0347710.
DR Gramene; HORVU.MOREX.r2.4HG0347710.1; HORVU.MOREX.r2.4HG0347710.1; HORVU.MOREX.r2.4HG0347710.
DR BRENDA; 3.2.1.2; 2687.
DR ExpressionAtlas; Q9FUK6; baseline.
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; IPR001371; Glyco_hydro_14B_pln.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31352:SF39; BETA-AMYLASE; 1.
DR PANTHER; PTHR31352; 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.
DR PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR PROSITE; PS00679; BETA_AMYLASE_2; 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}.
FT REGION 511..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 377..378
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAG25638.1"
SQ SEQUENCE 533 AA; 59312 MW; C0B9780B0F13F48C CRC64;
VNVKGNYVQV YVMLPLDAVS VNNRFEKGDE LRAQLRKLVE AGVDGVMVDV WWGLVEGKGP
KAYDWSAYKQ LFELVQKAGL KLQAIMSFHQ CGGNVGDAVN IPIPQWVRDV GTCDPDIFYT
DGHGTRNIEY LTLGVDNQPL FHGRSAVQMY ADYMTSFREN MKEFLDAGVI VDIEVGLGPA
GEMRYPSYPQ SHGWSFPGIG EFICYDKYLQ ADFKAAAAAV GHPEWEFPND VGQYNDTPER
TQFFRDNGTY LSEKGRFFLA WYSNNLIKHG DRILDEANKV FLGYKVQLAI KISGIHWWYK
VPSHAAELTA GYYNLHDRDG YRTIARMLKR HRASINFTCA EMRDSEQSSQ AMSAPEELVQ
QVLSAGWREG LNVACENALP RYDPTAYNTI LRNARPHGIN QSGPPEHKLF GFTYLRLSNQ
LVEGQNYANF KTFVDRMHAN LPRDPYVDPM APLPRSGPEI SIEMILQAAQ PKLQPFPFQE
HTDLPVGPTG GMGGQAEGPT CGMGGQVKGP TGGMGGQAED PTSGMGGELP ATM
//
