AMYB_HORVU
ID AMYB_HORVU Reviewed; 535 AA.
AC P16098;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Beta-amylase;
DE EC=3.2.1.2;
DE AltName: Full=1,4-alpha-D-glucan maltohydrolase;
GN Name=BMY1; Synonyms=AMYB;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Endosperm;
RX PubMed=2446870; DOI=10.1111/j.1432-1033.1987.tb13640.x;
RA Kreis M., Williamson M., Buxton B., Pywell J., Hejgaard J., Svendsen I.;
RT "Primary structure and differential expression of beta-amylase in normal
RT and mutant barleys.";
RL Eur. J. Biochem. 169:517-525(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Haruna Two-rows;
RX PubMed=8534999; DOI=10.1271/bbb.59.1991;
RA Yoshigi N., Okada Y., Sahara H., Tamaki T.;
RT "A structural gene encoding beta-amylase of barley.";
RL Biosci. Biotechnol. Biochem. 59:1991-1993(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Haruna Two-rows;
RX PubMed=8188635; DOI=10.1093/oxfordjournals.jbchem.a124303;
RA Yoshigi N., Okada Y., Sahara H., Koshino S.;
RT "PCR cloning and sequencing of the beta-amylase cDNA from barley.";
RL J. Biochem. 115:47-51(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 5-504.
RX PubMed=9918723; DOI=10.1006/jmbi.1998.2379;
RA Mikami B., Yoon H.-J., Yoshigi N.;
RT "The crystal structure of the sevenfold mutant of barley beta-amylase with
RT increased thermostability at 2.5 A resolution.";
RL J. Mol. Biol. 285:1235-1243(1999).
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.
CC -!- INTERACTION:
CC P16098; P16098: BMY1; NbExp=4; IntAct=EBI-7799617, EBI-7799617;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
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; X52321; CAA36556.1; -; mRNA.
DR EMBL; D49999; BAA08741.1; -; Genomic_DNA.
DR EMBL; D21349; BAA04815.1; -; mRNA.
DR PIR; S00222; S00222.
DR PDB; 1B1Y; X-ray; 2.50 A; A=6-504.
DR PDB; 2XFF; X-ray; 1.31 A; A=1-535.
DR PDB; 2XFR; X-ray; 0.97 A; A=1-535.
DR PDB; 2XFY; X-ray; 1.21 A; A=1-535.
DR PDB; 2XG9; X-ray; 1.80 A; A=1-535.
DR PDB; 2XGB; X-ray; 1.20 A; A=1-535.
DR PDB; 2XGI; X-ray; 1.30 A; A=1-535.
DR PDBsum; 1B1Y; -.
DR PDBsum; 2XFF; -.
DR PDBsum; 2XFR; -.
DR PDBsum; 2XFY; -.
DR PDBsum; 2XG9; -.
DR PDBsum; 2XGB; -.
DR PDBsum; 2XGI; -.
DR AlphaFoldDB; P16098; -.
DR SMR; P16098; -.
DR MINT; P16098; -.
DR BindingDB; P16098; -.
DR ChEMBL; CHEMBL4371; -.
DR Allergome; 420; Hor v 17.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR PRIDE; P16098; -.
DR EnsemblPlants; HORVU.MOREX.r2.4HG0347710.1.mrna1; HORVU.MOREX.r2.4HG0347710.1.mrna1; HORVU.MOREX.r2.4HG0347710.1.
DR Gramene; HORVU.MOREX.r2.4HG0347710.1.mrna1; HORVU.MOREX.r2.4HG0347710.1.mrna1; HORVU.MOREX.r2.4HG0347710.1.
DR BRENDA; 3.2.1.2; 2687.
DR EvolutionaryTrace; P16098; -.
DR ExpressionAtlas; P16098; baseline and differential.
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:0042802; F:identical protein binding; IPI:IntAct.
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 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Repeat.
FT CHAIN 1..535
FT /note="Beta-amylase"
FT /id="PRO_0000153933"
FT REPEAT 489..499
FT /note="1"
FT REPEAT 500..510
FT /note="2"
FT REPEAT 511..521
FT /note="3"
FT REPEAT 522..532
FT /note="4; approximate"
FT REGION 489..532
FT /note="4 X 11 AA tandem repeats"
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 CONFLICT 233
FT /note="V -> A (in Ref. 2; BAA08741 and 3; BAA04815)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="L -> S (in Ref. 2; BAA08741 and 3; BAA04815)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="I -> M (in Ref. 2; BAA08741 and 3; BAA04815)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:2XFR"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:2XFR"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 68..79
FT /evidence="ECO:0007829|PDB:2XFR"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:2XFR"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2XGB"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2XFR"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:2XFR"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:2XFR"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:1B1Y"
FT HELIX 148..168
FT /evidence="ECO:0007829|PDB:2XFR"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:2XFR"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:2XFF"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2XFR"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 255..283
FT /evidence="ECO:0007829|PDB:2XFR"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:2XFR"
FT TURN 299..302
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:2XFR"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:1B1Y"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:2XFR"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:2XFR"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 357..370
FT /evidence="ECO:0007829|PDB:2XFR"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 386..396
FT /evidence="ECO:0007829|PDB:2XFR"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:2XFR"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:2XFR"
FT TURN 421..424
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 426..439
FT /evidence="ECO:0007829|PDB:2XFR"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:2XFR"
FT STRAND 447..450
FT /evidence="ECO:0007829|PDB:1B1Y"
FT HELIX 464..468
FT /evidence="ECO:0007829|PDB:2XFR"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:2XFR"
SQ SEQUENCE 535 AA; 59647 MW; FFDA4CED53E9A89E CRC64;
MEVNVKGNYV QVYVMLPLDA VSVNNRFEKG DELRAQLRKL VEAGVDGVMV DVWWGLVEGK
GPKAYDWSAY KQLFELVQKA GLKLQAIMSF HQCGGNVGDA VNIPIPQWVR DVGTRDPDIF
YTDGHGTRNI EYLTLGVDNQ PLFHGRSAVQ MYADYMTSFR ENMKDFLDAG VIVDIEVGLG
PAGEMRYPSY PQSHGWSFPG IGEFICYDKY LQADFKAAAA AVGHPEWEFP NDVGQYNDTP
ERTQFFRDNG TYLSEKGRFF LAWYSNNLIK HGDRILDEAN KVFLGYKVQL AIKISGIHWW
YKVPSHAAEL TAGYYNLHDR DGYRTIARML KRHRASINFT CAEMRDLEQS SQAMSAPEEL
VQQVLSAGWR EGLNVACENA LPRYDPTAYN TILRNARPHG INQSGPPEHK LFGFTYLRLS
NQLVEGQNYV NFKTFVDRMH ANLPRDPYVD PMAPLPRSGP EISIEMILQA AQPKLQPFPF
QEHTDLPVGP TGGMGGQAEG PTCGMGGQVK GPTGGMGGQA EDPTSGIGGE LPATM
