Beta-amylase - Glycine max (Soybean)

Preferred order of sections

Names and origin

Protein names	Recommended name: Beta-amylase RuleBase RU000509 EC=3.2.1.2 RuleBase RU000509
Organism	Glycine max (Soybean) (Glycine hispida) EMBL BAA09462.1
Taxonomic identifier	3847 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Phaseoleae › Glycine

Protein attributes

Sequence length	496 AA.
Sequence status	Complete.
Protein existence	Evidence 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. RuleBase RU000509
Sequence similarities	Belongs to the glycosyl hydrolase 14 family. RuleBase RU004157

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation RuleBase RU000509
Molecular function	Glycosidase RuleBase RU000509 EMBL BAA09462.1 Hydrolase
Technical term	3D-structure PDB 2DQX
Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	beta-amylase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Region

381 – 383

3

Glucose binding PDB 1Q6E PDB 1Q6G

Sites

Binding site

54

1

Glucose PDB 1Q6E PDB 1Q6G

Binding site

94

1

Glucose PDB 1Q6E PDB 1Q6G

Binding site

102

1

Glucose PDB 1Q6E PDB 1Q6G

Binding site

187

1

Glucose PDB 1Q6E PDB 1Q6G

Binding site

296

1

Glucose PDB 1Q6E PDB 1Q6G

Binding site

301

1

Glucose PDB 1Q6E PDB 1Q6G

Binding site

421

1

Glucose PDB 1Q6E PDB 1Q6G

Sequences

Sequence

Length

Mass (Da)

Tools

Q42795 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B9CD07302B6FA573
Show »

FASTA

496

56,072

        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 FPGIGEFQCY 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 AYNQIILNAR PQGVNNNGPP KLSMFGVTYL 

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

       490 
TLPFPWLPET DMKVDG

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References

[1]	"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: 9677422] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Tissue: Cotyledon EMBL BAA09462.1.
[2]	"Kinetic and structural analysis of enzyme sliding on a substrate: multiple attack in beta-amylase." Ishikawa K., Nakatani H., Katsuya Y., Fukazawa C. Biochemistry 46:792-798(2007) [PubMed: 17223700] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-496.
[3]	Jiang J., Zhang G., Zhou W. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[4]	"MESSENGER RNA OF BETA-AMYLASE, NOVEL RECOMBINANT HAVING COMPLEMENTARY DNA CORRESPONDING TO SAID RNA AND NOVEL BACTERIUM MANIFESTING GENE THEREOF." Fukazawa C., Kainuma K. Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

DQ114423 mRNA. Translation: AAZ38832.1.
D50866 mRNA. Translation: BAA09462.1.
AB004271 mRNA. Translation: BAA20453.1.

RefSeq

XP_003527476.1. XM_003527428.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DQX	X-ray	2.20	A	2-496	[»]

ProteinModelPortal

Q42795.

SMR

Q42795. Positions 4-496.

ModBase

Search...

Protein family/group databases

CAZy

GH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

GLYMA06G45700.1; GLYMA06G45700.1; GLYMA06G45700.
Gmax_FGT39543; Gmax_FGP39543; Gmax_FG39543.

GeneID

547931.

Phylogenomic databases

PhylomeDB

Q42795.

Gene expression databases

Genevestigator

Q42795.

Family and domain databases

InterPro

IPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR001371. Glyco_hydro_14B_pln.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF01373. Glyco_hydro_14. 1 hit.
[Graphical view]

PRINTS

PR00750. BETAAMYLASE.
PR00842. GLHYDLASE14B.

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q42795_SOYBN

Accession

Primary (citable) accession number: Q42795

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)