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 02-SEP-2026, entry version 158. 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}; 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; X71419; CAA50551.1; -; mRNA. DR EMBL; M92090; AAA33941.1; ALT_FRAME; mRNA. DR PIR; A29291; A60473. DR RefSeq; NP_001236247.2; NM_001249318.2. 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 AlphaFoldDB; P10538; -. DR MDposit; P10538; -. DR MDRepo; P10538; -. DR SMR; P10538; -. DR FunCoup; P10538; 250. DR STRING; 3847.P10538; -. DR CAZy; GH14; Glycoside Hydrolase Family 14. DR iPTMnet; P10538; -. DR PaxDb; 3847-P10538; -. DR GeneID; 547931; -. DR KEGG; gmx:547931; -. DR eggNOG; ENOG502QUU5; Eukaryota. DR InParanoid; P10538; -. DR OrthoDB; 1660156at2759; -. DR BRENDA; 3.2.1.2; 2483. DR EvolutionaryTrace; P10538; -. DR Proteomes; UP000008827; Unplaced. DR GO; GO:0016161; F:beta-amylase activity; EXP:UniProtKB. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro. DR FunFam; 3.20.20.80:FF:000066; Beta-amylase; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR001554; Glyco_hydro_14. DR InterPro; IPR018238; Glyco_hydro_14_CS. DR InterPro; IPR001371; Glyco_hydro_14B_pln. DR PANTHER; PTHR31352; BETA-AMYLASE 1, CHLOROPLASTIC; 1. DR PANTHER; PTHR31352:SF40; BETA-AMYLASE 6; 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. 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; -. 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 446..448 FT /evidence="ECO:0007829|PDB:1WDP" FT HELIX 452..455 FT /evidence="ECO:0007829|PDB:1WDP" FT HELIX 461..468 FT /evidence="ECO:0007829|PDB:1WDP" FT HELIX 471..476 FT /evidence="ECO:0007829|PDB:1WDP" FT HELIX 482..485 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 //