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P10538 (AMYB_SOYBN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-amylase
EC=3.2.1.2
Alternative name(s):
1,4-alpha-D-glucan maltohydrolase
Gene names
Name:BMY1
OrganismGlycine max (Soybean) (Glycine hispida) [Reference proteome]
Taxonomic identifier3847 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Glycine

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.11

Subunit structure

Monomer.

Sequence similarities

Belongs to the glycosyl hydrolase 14 family.

Sequence caution

The sequence AAA33941.1 differs from that shown. Reason: Frameshift at several positions.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 496495Beta-amylase
PRO_0000153938

Regions

Region382 – 3832Substrate binding

Sites

Active site1871Proton donor Ref.5 Ref.6 Ref.11
Active site3811Proton acceptor Ref.6 Ref.11
Binding site541Substrate
Binding site941Substrate
Binding site1021Substrate
Binding site2961Substrate
Binding site3011Substrate
Binding site3431Substrate
Binding site4211Substrate

Amino acid modifications

Modified residue21N-acetylalanine Ref.4

Experimental info

Mutagenesis1021D → N or E: Loss of activity. Ref.6
Mutagenesis1871E → Q or D: Loss of activity. Ref.6 Ref.11
Mutagenesis3431T → A: Reduces activity 1700-fold.
Mutagenesis3431T → S: Reduces activity 360-fold.
Mutagenesis3431T → V: Reduces activity 16-fold.
Mutagenesis3811E → Q: Loss of activity. Ref.11
Sequence conflict91L → G AA sequence Ref.4
Sequence conflict184 – 1907PAGELRY → QQESSDT in AAA33941. Ref.3
Sequence conflict2031R → G in AAA33941. Ref.3
Sequence conflict4001K → R in AAA33941. Ref.3
Sequence conflict473 – 4742VL → FF in AAA33941. Ref.3

Secondary structure

1 ........................................................................................ 496
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10538 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: FB87917244FEF798

FASTA49656,143
        10         20         30         40         50         60 
MATSDSNMLL NYVPVYVMLP LGVVNVDNVF EDPDGLKEQL LQLRAAGVDG VMVDVWWGII 

        70         80         90        100        110        120 
ELKGPKQYDW RAYRSLFQLV QECGLTLQAI MSFHQCGGNV GDIVNIPIPQ WVLDIGESNH 

       130        140        150        160        170        180 
DIFYTNRSGT RNKEYLTVGV DNEPIFHGRT AIEIYSDYMK SFRENMSDFL ESGLIIDIEV 

       190        200        210        220        230        240 
GLGPAGELRY PSYPQSQGWE FPRIGEFQCY DKYLKADFKA AVARAGHPEW ELPDDAGKYN 

       250        260        270        280        290        300 
DVPESTGFFK SNGTYVTEKG KFFLTWYSNK LLNHGDQILD EANKAFLGCK VKLAIKVSGI 

       310        320        330        340        350        360 
HWWYKVENHA AELTAGYYNL NDRDGYRPIA RMLSRHHAIL NFTCLEMRDS EQPSDAKSGP 

       370        380        390        400        410        420 
QELVQQVLSG GWREDIRVAG ENALPRYDAT AYNQIILNAK PQGVNNNGPP KLSMFGVTYL 

       430        440        450        460        470        480 
RLSDDLLQKS NFNIFKKFVL KMHADQDYCA NPQKYNHAIT PLKPSAPKIP IEVLLEATKP 

       490 
TLPFPWLPET DMKVDG

« Hide

References

[1]"Expression and mutation of soybean beta-amylase in Escherichia coli."
Totsuka A., Fukazawa C.
Eur. J. Biochem. 214:787-794(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Primary structure and function of beta-amylase."
Mikami B., Morita Y., Fukazawa C.
Seikagaku 60:211-216(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Nucleotide and deduced protein sequence of beta-amylase."
Ehrlich K.C., Montalbano B.G.
Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"N-terminal sequence of soybean beta-amylase."
Mikami B., Nomura K., Morita Y.
J. Biochem. 100:513-516(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-10.
[5]"Identification of glutamic acid 186 affinity-labeled by 2,3-epoxypropyl alpha-D-glucopyranoside in soybean beta-amylase."
Nitta Y., Isoda Y., Toda H., Sakiyama F.
J. Biochem. 105:573-576(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE GLU-187.
[6]"Residues essential for catalytic activity of soybean beta-amylase."
Totsuka A., Nong V.H., Kadokawa H., Kim C.-S., Itoh Y., Fukazawa C.
Eur. J. Biochem. 221:649-654(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITES, MUTAGENESIS OF ASP-102 AND GLU-187.
[7]"Three-dimensional structure of soybean beta-amylase determined at 3.0-A resolution: preliminary chain tracing of the complex with alpha-cyclodextrin."
Mikami B., Sato M., Shibata T., Hirose M., Aibara S., Katsube Y., Morita Y.
J. Biochem. 112:541-546(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[8]"The 2.0-A resolution structure of soybean beta-amylase complexed with alpha-cyclodextrin."
Mikami B., Hehre E.J., Sato M., Katsube Y., Hirose M., Morita Y., Sacchettini J.C.
Biochemistry 32:6836-6845(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[9]"Crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: active site components and their apparent roles in catalysis."
Mikami B., Degano M., Hehre E.J., Sacchettini J.C.
Biochemistry 33:7779-7787(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[10]"Crystal structure of recombinant soybean beta-amylase complexed with beta-cyclodextrin."
Adachi M., Mikami B., Katsube T., Utsumi S.
J. Biol. Chem. 273:19859-19865(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS).
[11]"The roles of Glu186 and Glu380 in the catalytic reaction of soybean beta-amylase."
Kang Y.N., Adachi M., Utsumi S., Mikami B.
J. Mol. Biol. 339:1129-1140(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: 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.
[12]"Structural analysis of threonine 342 mutants of soybean beta-amylase: role of a conformational change of the inner loop in the catalytic mechanism."
Kang Y.N., Tanabe A., Adachi M., Utsumi S., Mikami B.
Biochemistry 44:5106-5116(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) OF MUTANTS ALA/SER/VAL-343 IN COMPLEXES WITH MALTOSE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X71419 mRNA. Translation: CAA50551.1.
M92090 mRNA. Translation: AAA33941.1. Frameshift.
PIRA60473. A29291.
RefSeqNP_001236247.1. NM_001249318.1.
UniGeneGma.595.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BFNX-ray2.07A2-496[»]
1BTCX-ray2.00A6-496[»]
1BYAX-ray2.20A2-496[»]
1BYBX-ray1.90A2-496[»]
1BYCX-ray2.20A2-496[»]
1BYDX-ray2.20A2-496[»]
1Q6CX-ray1.86A2-496[»]
1Q6DX-ray2.00A2-496[»]
1Q6EX-ray1.95A2-496[»]
1Q6FX-ray2.10A2-496[»]
1Q6GX-ray2.00A2-496[»]
1UKOX-ray2.10A/B/C/D2-495[»]
1UKPX-ray2.10A/B/C/D2-495[»]
1V3HX-ray1.60A2-495[»]
1V3IX-ray1.90A2-495[»]
1WDPX-ray1.27A2-495[»]
1WDQX-ray1.28A2-495[»]
1WDRX-ray1.35A2-495[»]
1WDSX-ray1.64A2-496[»]
ProteinModelPortalP10538.
SMRP10538. Positions 6-496.
ModBaseSearch...

Protein family/group databases

CAZyGH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID547931.
KEGGgmx:547931.

Gene expression databases

GenevestigatorP10538.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR001371. Glyco_hydro_14B_pln.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSPR00750. BETAAMYLASE.
PR00842. GLHYDLASE14B.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10538.

Entry information

Entry nameAMYB_SOYBN
AccessionPrimary (citable) accession number: P10538
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents