ID U5NIV6_HORVS Unreviewed; 535 AA.
AC U5NIV6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 Name=Bmy1 {ECO:0000313|EMBL:AGY14538.1};
OS Hordeum vulgare subsp. spontaneum (Wild barley) (Hordeum spontaneum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=77009 {ECO:0000313|EMBL:AGY14538.1};
RN [1] {ECO:0000313|EMBL:AGY14538.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HUA0640 {ECO:0000313|EMBL:AGY14538.1};
RX PubMed=24019884;
RA Gong X., Westcott S., Zhang X.Q., Yan G., Lance R., Zhang G., Sun D.,
RA Li C.;
RT "Discovery of Novel Bmy1 Alleles Increasing beta-Amylase Activity in
RT Chinese Landraces and Tibetan Wild Barley for Improvement of Malting
RT Quality via MAS.";
RL PLoS ONE 8:E72875-E72875(2013).
RN [2] {ECO:0000313|EMBL:AGY14538.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HUA0640 {ECO:0000313|EMBL:AGY14538.1};
RA Xue G., Sharon W., Qi Z.X., Jun Y.G., Reg L., Ping Z.G., Fa S.D., Dao L.C.;
RL Submitted (JUN-2013) 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}.
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; KF302675; AGY14538.1; -; Genomic_DNA.
DR AlphaFoldDB; U5NIV6; -.
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 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 REGION 513..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-1"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 379..380
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601554-2"
SQ SEQUENCE 535 AA; 59532 MW; E4D6F78554EE6119 CRC64;
MEVNVKGNYV QVYVMLPLDA VSVNNRFEKG DELRAQLRKL VEAGVDGVMV DVWWGLVEGK
GPKAYDWSAY KQLFELVQKA GLKLQAIMSF HQCGGNVGDA VNIPIPQWVR DVGTRDPDIF
YTDGHGTRNI EYLTLGVDNQ PLFHGRSAVQ MYADYMTSFR ENMKDFLDAG VIVDIEVGLG
PAGEMRYPSY PQSHGWSFPG IGEFICYDKY LQADFKAAAA AVGHPEWEFP NDAGQYNDTP
QRTQFLRDNG TFLSEKGKFF LAWYSNNLIK HGDRILDEAN KVFLGYKVQL AIKISGIHWW
YKVPSHAAEL TAGYYNLHDR DGYRTIARML KRHRASINFT CAEMRDSEQS SQAMSAPEEL
VQQVLSAGWR EGLNVACENA LPRYDPTAYN TILRNARPHG INQSGPPEHK LFGFTYLRLS
NQLVEGQNYV NFKTFVDRMH ANLPRDPYVD PMAPLPRSGP EISIEMILQA AQPKLQPFPF
QEHTDLPVGP TGGMGGQAEG PTCGMGGQVK GPTGGMGGQA EDPTSGMGGE LPATM
//
