AMYB_SOYBN
ID AMYB_SOYBN Reviewed; 496 AA.
AC P10538;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Beta-amylase;
DE EC=3.2.1.2;
DE AltName: Full=1,4-alpha-D-glucan maltohydrolase;
GN Name=BMY1;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8319688; DOI=10.1111/j.1432-1033.1993.tb17981.x;
RA Totsuka A., Fukazawa C.;
RT "Expression and mutation of soybean beta-amylase in Escherichia coli.";
RL Eur. J. Biochem. 214:787-794(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2457058;
RA Mikami B., Morita Y., Fukazawa C.;
RT "Primary structure and function of beta-amylase.";
RL Seikagaku 60:211-216(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ehrlich K.C., Montalbano B.G.;
RT "Nucleotide and deduced protein sequence of beta-amylase.";
RL Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
RX PubMed=2430952; DOI=10.1093/oxfordjournals.jbchem.a121741;
RA Mikami B., Nomura K., Morita Y.;
RT "N-terminal sequence of soybean beta-amylase.";
RL J. Biochem. 100:513-516(1986).
RN [5]
RP ACTIVE SITE GLU-187.
RX PubMed=2474529; DOI=10.1093/oxfordjournals.jbchem.a122706;
RA Nitta Y., Isoda Y., Toda H., Sakiyama F.;
RT "Identification of glutamic acid 186 affinity-labeled by 2,3-epoxypropyl
RT alpha-D-glucopyranoside in soybean beta-amylase.";
RL J. Biochem. 105:573-576(1989).
RN [6]
RP ACTIVE SITE, AND MUTAGENESIS OF ASP-102 AND GLU-187.
RX PubMed=8174545; DOI=10.1111/j.1432-1033.1994.tb18777.x;
RA Totsuka A., Nong V.H., Kadokawa H., Kim C.-S., Itoh Y., Fukazawa C.;
RT "Residues essential for catalytic activity of soybean beta-amylase.";
RL Eur. J. Biochem. 221:649-654(1994).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=1491009; DOI=10.1093/oxfordjournals.jbchem.a123935;
RA Mikami B., Sato M., Shibata T., Hirose M., Aibara S., Katsube Y.,
RA Morita Y.;
RT "Three-dimensional structure of soybean beta-amylase determined at 3.0-A
RT resolution: preliminary chain tracing of the complex with alpha-
RT cyclodextrin.";
RL J. Biochem. 112:541-546(1992).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8334116; DOI=10.1021/bi00078a006;
RA Mikami B., Hehre E.J., Sato M., Katsube Y., Hirose M., Morita Y.,
RA Sacchettini J.C.;
RT "The 2.0-A resolution structure of soybean beta-amylase complexed with
RT alpha-cyclodextrin.";
RL Biochemistry 32:6836-6845(1993).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND ACTIVE SITE.
RX PubMed=8011643; DOI=10.1021/bi00191a005;
RA Mikami B., Degano M., Hehre E.J., Sacchettini J.C.;
RT "Crystal structures of soybean beta-amylase reacted with beta-maltose and
RT maltal: active site components and their apparent roles in catalysis.";
RL Biochemistry 33:7779-7787(1994).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS).
RX PubMed=9677422; DOI=10.1074/jbc.273.31.19859;
RA Adachi M., Mikami B., Katsube T., Utsumi S.;
RT "Crystal structure of recombinant soybean beta-amylase complexed with beta-
RT cyclodextrin.";
RL J. Biol. Chem. 273:19859-19865(1998).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MUTANTS GLN-187 AND GLN-381 IN
RP COMPLEXES WITH SUBSTRATE ANALOGS, ACTIVE SITE, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF GLU-187 AND GLU-381, AND SUBSTRATE-BINDING.
RX PubMed=15178253; DOI=10.1016/j.jmb.2004.04.029;
RA Kang Y.N., Adachi M., Utsumi S., Mikami B.;
RT "The roles of Glu186 and Glu380 in the catalytic reaction of soybean beta-
RT amylase.";
RL J. Mol. Biol. 339:1129-1140(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) OF MUTANTS ALA/SER/VAL-343 IN
RP COMPLEXES WITH MALTOSE.
RX PubMed=15794648; DOI=10.1021/bi0476580;
RA Kang Y.N., Tanabe A., Adachi M., Utsumi S., Mikami B.;
RT "Structural analysis of threonine 342 mutants of soybean beta-amylase: role
RT of a conformational change of the inner loop in the catalytic mechanism.";
RL Biochemistry 44:5106-5116(2005).
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:0000269|PubMed:15178253};
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA33941.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X71419; CAA50551.1; -; mRNA.
DR EMBL; M92090; AAA33941.1; ALT_FRAME; mRNA.
DR PIR; A29291; A60473.
DR RefSeq; NP_001236247.1; NM_001249318.1.
DR PDB; 1BFN; X-ray; 2.07 A; A=2-496.
DR PDB; 1BTC; X-ray; 2.00 A; A=6-496.
DR PDB; 1BYA; X-ray; 2.20 A; A=2-496.
DR PDB; 1BYB; X-ray; 1.90 A; A=2-496.
DR PDB; 1BYC; X-ray; 2.20 A; A=2-496.
DR PDB; 1BYD; X-ray; 2.20 A; A=2-496.
DR PDB; 1Q6C; X-ray; 1.86 A; A=2-496.
DR PDB; 1Q6D; X-ray; 2.00 A; A=2-496.
DR PDB; 1Q6E; X-ray; 1.95 A; A=2-496.
DR PDB; 1Q6F; X-ray; 2.10 A; A=2-496.
DR PDB; 1Q6G; X-ray; 2.00 A; A=2-496.
DR PDB; 1UKO; X-ray; 2.10 A; A/B/C/D=2-496.
DR PDB; 1UKP; X-ray; 2.10 A; A/B/C/D=2-496.
DR PDB; 1V3H; X-ray; 1.60 A; A=2-496.
DR PDB; 1V3I; X-ray; 1.90 A; A=2-496.
DR PDB; 1WDP; X-ray; 1.27 A; A=2-496.
DR PDB; 1WDQ; X-ray; 1.28 A; A=2-496.
DR PDB; 1WDR; X-ray; 1.35 A; A=2-496.
DR PDB; 1WDS; X-ray; 1.64 A; A=2-496.
DR PDBsum; 1BFN; -.
DR PDBsum; 1BTC; -.
DR PDBsum; 1BYA; -.
DR PDBsum; 1BYB; -.
DR PDBsum; 1BYC; -.
DR PDBsum; 1BYD; -.
DR PDBsum; 1Q6C; -.
DR PDBsum; 1Q6D; -.
DR PDBsum; 1Q6E; -.
DR PDBsum; 1Q6F; -.
DR PDBsum; 1Q6G; -.
DR PDBsum; 1UKO; -.
DR PDBsum; 1UKP; -.
DR PDBsum; 1V3H; -.
DR PDBsum; 1V3I; -.
DR PDBsum; 1WDP; -.
DR PDBsum; 1WDQ; -.
DR PDBsum; 1WDR; -.
DR PDBsum; 1WDS; -.
DR AlphaFoldDB; P10538; -.
DR SMR; P10538; -.
DR STRING; 3847.GLYMA06G45700.1; -.
DR CAZy; GH14; Glycoside Hydrolase Family 14.
DR iPTMnet; P10538; -.
DR GeneID; 547931; -.
DR KEGG; gmx:547931; -.
DR eggNOG; ENOG502QUU5; Eukaryota.
DR InParanoid; P10538; -.
DR OrthoDB; 533202at2759; -.
DR BRENDA; 3.2.1.2; 2483.
DR EvolutionaryTrace; P10538; -.
DR Proteomes; UP000008827; Unplaced.
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 3D-structure; Acetylation; Carbohydrate metabolism;
KW Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2430952"
FT CHAIN 2..496
FT /note="Beta-amylase"
FT /id="PRO_0000153938"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10050,
FT ECO:0000269|PubMed:15178253, ECO:0000269|PubMed:2474529,
FT ECO:0000269|PubMed:8011643, ECO:0000269|PubMed:8174545"
FT ACT_SITE 381
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:15178253,
FT ECO:0000269|PubMed:8011643"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15178253"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15178253"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15178253"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15178253"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15178253"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15178253"
FT BINDING 382..383
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15178253"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15178253"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2430952"
FT MUTAGEN 102
FT /note="D->N,E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8174545"
FT MUTAGEN 187
FT /note="E->Q,D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15178253,
FT ECO:0000269|PubMed:8174545"
FT MUTAGEN 343
FT /note="T->A: Reduces activity 1700-fold."
FT MUTAGEN 343
FT /note="T->S: Reduces activity 360-fold."
FT MUTAGEN 343
FT /note="T->V: Reduces activity 16-fold."
FT MUTAGEN 381
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15178253"
FT CONFLICT 9
FT /note="L -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 184..190
FT /note="PAGELRY -> QQESSDT (in Ref. 3; AAA33941)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="R -> G (in Ref. 3; AAA33941)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="K -> R (in Ref. 3; AAA33941)"
FT /evidence="ECO:0000305"
FT CONFLICT 473..474
FT /note="VL -> FF (in Ref. 3; AAA33941)"
FT /evidence="ECO:0000305"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:1WDP"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:1WDP"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1BYA"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1BYA"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:1WDP"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:1WDP"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:1WDP"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:1WDQ"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1WDP"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1WDP"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 151..165
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:1WDP"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1WDP"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1WDP"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:1BYB"
FT HELIX 212..224
FT /evidence="ECO:0007829|PDB:1WDP"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1WDP"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 258..285
FT /evidence="ECO:0007829|PDB:1WDP"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:1WDP"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:1WDP"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 310..315
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 327..334
FT /evidence="ECO:0007829|PDB:1WDP"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:1WDP"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:1WDP"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 389..399
FT /evidence="ECO:0007829|PDB:1WDP"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:1V3I"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 424..427
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 429..442
FT /evidence="ECO:0007829|PDB:1WDP"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 452..455
FT /evidence="ECO:0007829|PDB:1WDP"
FT HELIX 471..476
FT /evidence="ECO:0007829|PDB:1WDP"
SQ SEQUENCE 496 AA; 56143 MW; FB87917244FEF798 CRC64;
MATSDSNMLL NYVPVYVMLP LGVVNVDNVF EDPDGLKEQL LQLRAAGVDG VMVDVWWGII
ELKGPKQYDW RAYRSLFQLV QECGLTLQAI MSFHQCGGNV GDIVNIPIPQ WVLDIGESNH
DIFYTNRSGT RNKEYLTVGV DNEPIFHGRT AIEIYSDYMK SFRENMSDFL ESGLIIDIEV
GLGPAGELRY PSYPQSQGWE FPRIGEFQCY DKYLKADFKA AVARAGHPEW ELPDDAGKYN
DVPESTGFFK SNGTYVTEKG KFFLTWYSNK LLNHGDQILD EANKAFLGCK VKLAIKVSGI
HWWYKVENHA AELTAGYYNL NDRDGYRPIA RMLSRHHAIL NFTCLEMRDS EQPSDAKSGP
QELVQQVLSG GWREDIRVAG ENALPRYDAT AYNQIILNAK PQGVNNNGPP KLSMFGVTYL
RLSDDLLQKS NFNIFKKFVL KMHADQDYCA NPQKYNHAIT PLKPSAPKIP IEVLLEATKP
TLPFPWLPET DMKVDG
