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Beta-amylase (EC 3.2.1.2) (1,4-alpha-D-glucan maltohydrolase)

 AMYB_SOYBN              Reviewed;         496 AA.
P10538;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 128.
RecName: Full=Beta-amylase;
EC=3.2.1.2;
AltName: Full=1,4-alpha-D-glucan maltohydrolase;
Name=BMY1;
Glycine max (Soybean) (Glycine hispida).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Phaseoleae; Glycine; Soja.
NCBI_TaxID=3847;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8319688; DOI=10.1111/j.1432-1033.1993.tb17981.x;
Totsuka A., Fukazawa C.;
"Expression and mutation of soybean beta-amylase in Escherichia
coli.";
Eur. J. Biochem. 214:787-794(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2457058;
Mikami B., Morita Y., Fukazawa C.;
"Primary structure and function of beta-amylase.";
Seikagaku 60:211-216(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Ehrlich K.C., Montalbano B.G.;
"Nucleotide and deduced protein sequence of beta-amylase.";
Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
PubMed=2430952;
Mikami B., Nomura K., Morita Y.;
"N-terminal sequence of soybean beta-amylase.";
J. Biochem. 100:513-516(1986).
[5]
ACTIVE SITE GLU-187.
PubMed=2474529;
Nitta Y., Isoda Y., Toda H., Sakiyama F.;
"Identification of glutamic acid 186 affinity-labeled by 2,3-
epoxypropyl alpha-D-glucopyranoside in soybean beta-amylase.";
J. Biochem. 105:573-576(1989).
[6]
ACTIVE SITE, AND MUTAGENESIS OF ASP-102 AND GLU-187.
PubMed=8174545; DOI=10.1111/j.1432-1033.1994.tb18777.x;
Totsuka A., Nong V.H., Kadokawa H., Kim C.-S., Itoh Y., Fukazawa C.;
"Residues essential for catalytic activity of soybean beta-amylase.";
Eur. J. Biochem. 221:649-654(1994).
[7]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=1491009;
Mikami B., Sato M., Shibata T., Hirose M., Aibara S., Katsube Y.,
Morita Y.;
"Three-dimensional structure of soybean beta-amylase determined at
3.0-A resolution: preliminary chain tracing of the complex with alpha-
cyclodextrin.";
J. Biochem. 112:541-546(1992).
[8]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=8334116; DOI=10.1021/bi00078a006;
Mikami B., Hehre E.J., Sato M., Katsube Y., Hirose M., Morita Y.,
Sacchettini J.C.;
"The 2.0-A resolution structure of soybean beta-amylase complexed with
alpha-cyclodextrin.";
Biochemistry 32:6836-6845(1993).
[9]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND ACTIVE SITE.
PubMed=8011643; DOI=10.1021/bi00191a005;
Mikami B., Degano M., Hehre E.J., Sacchettini J.C.;
"Crystal structures of soybean beta-amylase reacted with beta-maltose
and maltal: active site components and their apparent roles in
catalysis.";
Biochemistry 33:7779-7787(1994).
[10]
X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS).
PubMed=9677422; DOI=10.1074/jbc.273.31.19859;
Adachi M., Mikami B., Katsube T., Utsumi S.;
"Crystal structure of recombinant soybean beta-amylase complexed with
beta-cyclodextrin.";
J. Biol. Chem. 273:19859-19865(1998).
[11]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MUTANTS GLN-187 AND GLN-381
IN COMPLEXES WITH SUBSTRATE ANALOGS, ACTIVE SITE, CATALYTIC ACTIVITY,
MUTAGENESIS OF GLU-187 AND GLU-381, AND SUBSTRATE-BINDING.
PubMed=15178253; DOI=10.1016/j.jmb.2004.04.029;
Kang Y.N., Adachi M., Utsumi S., Mikami B.;
"The roles of Glu186 and Glu380 in the catalytic reaction of soybean
beta-amylase.";
J. Mol. Biol. 339:1129-1140(2004).
[12]
X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) OF MUTANTS ALA/SER/VAL-343 IN
COMPLEXES WITH MALTOSE.
PubMed=15794648; DOI=10.1021/bi0476580;
Kang Y.N., Tanabe A., Adachi M., Utsumi S., Mikami B.;
"Structural analysis of threonine 342 mutants of soybean beta-amylase:
role of a conformational change of the inner loop in the catalytic
mechanism.";
Biochemistry 44:5106-5116(2005).
-!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-alpha-D-glucosidic
linkages in polysaccharides so as to remove successive maltose
units from the non-reducing ends of the chains.
{ECO:0000269|PubMed:15178253}.
-!- SUBUNIT: Monomer.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 14 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA33941.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X71419; CAA50551.1; -; mRNA.
EMBL; M92090; AAA33941.1; ALT_FRAME; mRNA.
PIR; A29291; A60473.
RefSeq; NP_001236247.1; NM_001249318.1.
UniGene; Gma.595; -.
PDB; 1BFN; X-ray; 2.07 A; A=2-496.
PDB; 1BTC; X-ray; 2.00 A; A=6-496.
PDB; 1BYA; X-ray; 2.20 A; A=2-496.
PDB; 1BYB; X-ray; 1.90 A; A=2-496.
PDB; 1BYC; X-ray; 2.20 A; A=2-496.
PDB; 1BYD; X-ray; 2.20 A; A=2-496.
PDB; 1Q6C; X-ray; 1.86 A; A=2-496.
PDB; 1Q6D; X-ray; 2.00 A; A=2-496.
PDB; 1Q6E; X-ray; 1.95 A; A=2-496.
PDB; 1Q6F; X-ray; 2.10 A; A=2-496.
PDB; 1Q6G; X-ray; 2.00 A; A=2-496.
PDB; 1UKO; X-ray; 2.10 A; A/B/C/D=2-496.
PDB; 1UKP; X-ray; 2.10 A; A/B/C/D=2-496.
PDB; 1V3H; X-ray; 1.60 A; A=2-496.
PDB; 1V3I; X-ray; 1.90 A; A=2-496.
PDB; 1WDP; X-ray; 1.27 A; A=2-496.
PDB; 1WDQ; X-ray; 1.28 A; A=2-496.
PDB; 1WDR; X-ray; 1.35 A; A=2-496.
PDB; 1WDS; X-ray; 1.64 A; A=2-496.
PDBsum; 1BFN; -.
PDBsum; 1BTC; -.
PDBsum; 1BYA; -.
PDBsum; 1BYB; -.
PDBsum; 1BYC; -.
PDBsum; 1BYD; -.
PDBsum; 1Q6C; -.
PDBsum; 1Q6D; -.
PDBsum; 1Q6E; -.
PDBsum; 1Q6F; -.
PDBsum; 1Q6G; -.
PDBsum; 1UKO; -.
PDBsum; 1UKP; -.
PDBsum; 1V3H; -.
PDBsum; 1V3I; -.
PDBsum; 1WDP; -.
PDBsum; 1WDQ; -.
PDBsum; 1WDR; -.
PDBsum; 1WDS; -.
ProteinModelPortal; P10538; -.
SMR; P10538; -.
CAZy; GH14; Glycoside Hydrolase Family 14.
iPTMnet; P10538; -.
GeneID; 547931; -.
KEGG; gmx:547931; -.
eggNOG; ENOG410IJER; Eukaryota.
eggNOG; ENOG410XNXS; LUCA.
InParanoid; P10538; -.
BRENDA; 3.2.1.2; 2483.
EvolutionaryTrace; P10538; -.
Proteomes; UP000008827; Unplaced.
GO; GO:0102229; F:amylopectin maltohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016161; F:beta-amylase activity; IEA:UniProtKB-EC.
GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
InterPro; IPR001554; Glyco_hydro_14.
InterPro; IPR018238; Glyco_hydro_14_CS.
InterPro; IPR001371; Glyco_hydro_14B_pln.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR31352; PTHR31352; 1.
Pfam; PF01373; Glyco_hydro_14; 1.
PRINTS; PR00750; BETAAMYLASE.
PRINTS; PR00842; GLHYDLASE14B.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00506; BETA_AMYLASE_1; 1.
PROSITE; PS00679; BETA_AMYLASE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Carbohydrate metabolism; Complete proteome;
Direct protein sequencing; Glycosidase; Hydrolase;
Polysaccharide degradation; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2430952}.
CHAIN 2 496 Beta-amylase.
/FTId=PRO_0000153938.
REGION 382 383 Substrate binding.
{ECO:0000269|PubMed:15178253}.
ACT_SITE 187 187 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU10050,
ECO:0000269|PubMed:15178253,
ECO:0000269|PubMed:2474529,
ECO:0000269|PubMed:8011643,
ECO:0000269|PubMed:8174545}.
ACT_SITE 381 381 Proton acceptor.
{ECO:0000269|PubMed:15178253,
ECO:0000269|PubMed:8011643}.
BINDING 54 54 Substrate. {ECO:0000269|PubMed:15178253}.
BINDING 94 94 Substrate. {ECO:0000269|PubMed:15178253}.
BINDING 102 102 Substrate. {ECO:0000269|PubMed:15178253}.
BINDING 296 296 Substrate. {ECO:0000269|PubMed:15178253}.
BINDING 301 301 Substrate. {ECO:0000269|PubMed:15178253}.
BINDING 343 343 Substrate. {ECO:0000269|PubMed:15178253}.
BINDING 421 421 Substrate. {ECO:0000269|PubMed:15178253}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:2430952}.
MUTAGEN 102 102 D->N,E: Loss of activity.
{ECO:0000269|PubMed:8174545}.
MUTAGEN 187 187 E->Q,D: Loss of activity.
{ECO:0000269|PubMed:15178253,
ECO:0000269|PubMed:8174545}.
MUTAGEN 343 343 T->A: Reduces activity 1700-fold.
MUTAGEN 343 343 T->S: Reduces activity 360-fold.
MUTAGEN 343 343 T->V: Reduces activity 16-fold.
MUTAGEN 381 381 E->Q: Loss of activity.
{ECO:0000269|PubMed:15178253}.
CONFLICT 9 9 L -> G (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 184 190 PAGELRY -> QQESSDT (in Ref. 3; AAA33941).
{ECO:0000305}.
CONFLICT 203 203 R -> G (in Ref. 3; AAA33941).
{ECO:0000305}.
CONFLICT 400 400 K -> R (in Ref. 3; AAA33941).
{ECO:0000305}.
CONFLICT 473 474 VL -> FF (in Ref. 3; AAA33941).
{ECO:0000305}.
HELIX 5 9 {ECO:0000244|PDB:1WDP}.
STRAND 15 18 {ECO:0000244|PDB:1WDP}.
STRAND 23 25 {ECO:0000244|PDB:1BYA}.
TURN 26 28 {ECO:0000244|PDB:1BYA}.
HELIX 33 45 {ECO:0000244|PDB:1WDP}.
STRAND 50 56 {ECO:0000244|PDB:1WDP}.
HELIX 57 60 {ECO:0000244|PDB:1WDP}.
HELIX 71 82 {ECO:0000244|PDB:1WDP}.
STRAND 86 92 {ECO:0000244|PDB:1WDP}.
STRAND 96 99 {ECO:0000244|PDB:1WDQ}.
HELIX 110 118 {ECO:0000244|PDB:1WDP}.
HELIX 120 122 {ECO:0000244|PDB:1WDP}.
STRAND 123 125 {ECO:0000244|PDB:1WDP}.
STRAND 131 136 {ECO:0000244|PDB:1WDP}.
HELIX 138 140 {ECO:0000244|PDB:1WDP}.
HELIX 151 165 {ECO:0000244|PDB:1WDP}.
HELIX 167 171 {ECO:0000244|PDB:1WDP}.
STRAND 175 180 {ECO:0000244|PDB:1WDP}.
HELIX 184 186 {ECO:0000244|PDB:1WDP}.
STRAND 187 189 {ECO:0000244|PDB:1WDP}.
HELIX 195 197 {ECO:0000244|PDB:1WDP}.
STRAND 201 203 {ECO:0000244|PDB:1BYB}.
HELIX 212 224 {ECO:0000244|PDB:1WDP}.
STRAND 234 236 {ECO:0000244|PDB:1WDP}.
HELIX 243 245 {ECO:0000244|PDB:1WDP}.
TURN 247 249 {ECO:0000244|PDB:1WDP}.
HELIX 254 256 {ECO:0000244|PDB:1WDP}.
HELIX 258 285 {ECO:0000244|PDB:1WDP}.
TURN 286 288 {ECO:0000244|PDB:1WDP}.
STRAND 292 296 {ECO:0000244|PDB:1WDP}.
TURN 302 305 {ECO:0000244|PDB:1WDP}.
HELIX 310 315 {ECO:0000244|PDB:1WDP}.
HELIX 327 334 {ECO:0000244|PDB:1WDP}.
TURN 335 337 {ECO:0000244|PDB:1WDP}.
STRAND 339 342 {ECO:0000244|PDB:1WDP}.
HELIX 349 351 {ECO:0000244|PDB:1WDP}.
HELIX 354 356 {ECO:0000244|PDB:1WDP}.
HELIX 360 373 {ECO:0000244|PDB:1WDP}.
STRAND 378 381 {ECO:0000244|PDB:1WDP}.
HELIX 389 399 {ECO:0000244|PDB:1WDP}.
STRAND 406 409 {ECO:0000244|PDB:1V3I}.
STRAND 415 420 {ECO:0000244|PDB:1WDP}.
HELIX 424 427 {ECO:0000244|PDB:1WDP}.
HELIX 429 442 {ECO:0000244|PDB:1WDP}.
TURN 443 445 {ECO:0000244|PDB:1WDP}.
HELIX 452 455 {ECO:0000244|PDB:1WDP}.
HELIX 471 476 {ECO:0000244|PDB:1WDP}.
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


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