AMYB_HORVS
ID AMYB_HORVS Reviewed; 535 AA.
AC P82993;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Beta-amylase;
DE EC=3.2.1.2;
DE AltName: Full=1,4-alpha-D-glucan maltohydrolase;
DE AltName: Full=Beta-Amy1;
DE Flags: Precursor;
GN Name=BMY1 {ECO:0000250|UniProtKB:P10538};
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;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=cv. NPGS PI296897 {ECO:0000269|PubMed:9625721};
RC TISSUE=Endosperm {ECO:0000269|PubMed:9625721};
RX PubMed=9625721; DOI=10.1104/pp.117.2.679;
RA Erkkila M.J., Leah R., Ahokas H., Cameron-Mills V.;
RT "Allele-dependent barley grain beta-amylase activity.";
RL Plant Physiol. 117:679-685(1998).
RN [2] {ECO:0000305}
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY, POLYMORPHISM,
RP ACETYLATION AT VAL-3, AND VARIANTS ASP-165; SER-254 AND GLN-472.
RC STRAIN=cv. CPI77146-33 {ECO:0000269|Ref.2};
RC TISSUE=Seed {ECO:0000269|Ref.2};
RA Eglinton J.K., Lahnstein J., Shirley N., Evans D.E.;
RT "The structural basis for functional differences between allelic forms of
RT barley (Hordeum vulgare) beta-amylase.";
RL Submitted (MAY-2001) to UniProtKB.
CC -!- FUNCTION: Catalyzes the liberation of maltose from 1,4-alpha-D glucans.
CC {ECO:0000269|PubMed:9625721, ECO:0000269|Ref.2}.
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 -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P10538}.
CC -!- TISSUE SPECIFICITY: Endosperm. {ECO:0000269|Ref.2}.
CC -!- POLYMORPHISM: There are at least three alleles; SD2H; SD1 and SD2L. The
CC sequence of SD2H is shown here. {ECO:0000269|Ref.2}.
CC -!- MISCELLANEOUS: The three alleles show different thermostabilities and
CC different affinities for soluble starch. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000255}.
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DR EMBL; AF061204; AAC67246.1; -; Genomic_DNA.
DR AlphaFoldDB; P82993; -.
DR SMR; P82993; -.
DR Allergome; 420; Hor v 17.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
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 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; PTHR31352; 1.
DR Pfam; PF01373; Glyco_hydro_14; 1.
DR PRINTS; PR00750; BETAAMYLASE.
DR PRINTS; PR00842; GLHYDLASE14B.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00506; BETA_AMYLASE_1; 1.
DR PROSITE; PS00679; BETA_AMYLASE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Direct protein sequencing;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Repeat.
FT PROPEP 1..2
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000279693"
FT CHAIN 3..489
FT /note="Beta-amylase"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000279694"
FT PROPEP 490..535
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000279695"
FT REPEAT 489..499
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 500..510
FT /note="2"
FT /evidence="ECO:0000255"
FT REPEAT 511..521
FT /note="3"
FT /evidence="ECO:0000255"
FT REPEAT 522..532
FT /note="4; approximate"
FT /evidence="ECO:0000255"
FT REGION 489..532
FT /note="4 X 11 AA tandem repeats"
FT /evidence="ECO:0000255"
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:0000255|PROSITE-ProRule:PRU10050"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 379..380
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10538"
FT MOD_RES 3
FT /note="N-acetylvaline"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 165
FT /note="E -> D"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 254
FT /note="T -> S"
FT /evidence="ECO:0000269|Ref.2"
FT VARIANT 472
FT /note="K -> Q"
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 535 AA; 59639 MW; 0B265EAEEF061C9B CRC64;
MEVNVKGNYV QVYVMLPLDA VSVNNRFEKG DELRAQLRKL VEAGVDGVMV DVWWGLVEGK
GPKAYDWSAY KQLFELVQKA GLKLQAIMSF HQCGGNVGDA VNIPIPQWVR DVGTRDPDIF
YTDGHGTRNI EYLTLGVDNQ PLFHGRSAVQ MYADYMTSFR ENMKEFLDAG VIVDIEVGLG
PAGEMRYPSY PQSHGWSFPG IGEFICYDKY LQADFKAAAA AVGHPEWEFP NDAGQYNDTP
ERTQFFRDNG TYLTEKGRFF LAWYSNNLIK HGDRILDEAN KVFLGYKVQL AIKISGIHWW
YKVPSHAAEL TAGYYNLHDR DGYRTIARML KRHRASINFT CAEMRDSEQS SQAMSAPEEL
VQQVLSAGWR EGLNVACENA LPRYDPTAYN TILRNARPHG INQSGPPEHK LFGFTYLRLS
NQLVEGQNYV NFKTFVDRMH ANLPRDPYVD PMAPLPRSGP EISIEMILQA AKPKLQPFPF
QEHTDLPVGP TGGMGGQAEG PTCGMGGQVK GPTGGMGGQA EDPTSGMGGE LPATM
