Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q42795 (Q42795_SOYBN) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 82. Feed History...

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

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
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. RuleBase RU000509

Sequence similarities

Belongs to the glycosyl hydrolase 14 family. RuleBase RU004157

Sequences

Sequence LengthMass (Da)Tools
Q42795 [UniParc].

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

FASTA49656,072
        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

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"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: NUCLEOTIDE SEQUENCE.
Tissue: Cotyledon EMBL BAA09462.1.
[3]Jiang J., Zhang G., Zhou W.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[4]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-496.
[5]"Genome sequence of the palaeopolyploid soybean."
Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D., Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D. expand/collapse author list , Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K., Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.C., Jackson S.A.
Nature 463:178-183(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Williams 82 EnsemblPlants GLYMA06G45700.1.
[6]EnsemblPlants
Submitted (NOV-2012) to UniProtKB
Cited for: IDENTIFICATION.
Strain: Williams 82 EnsemblPlants GLYMA06G45700.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB189842 Genomic DNA. No translation available.
AB189843 Genomic DNA. No translation available.
AB189915 Genomic DNA. No translation available.
AB189916 Genomic DNA. No translation available.
DQ114422 Genomic DNA. No translation available.
M92090 Genomic DNA. No translation available.
X71419 Genomic DNA. No translation available.
DQ114423 mRNA. Translation: AAZ38832.1.
D50866 mRNA. Translation: BAA09462.1.
AB004271 mRNA. Translation: BAA20453.1.
UniGeneGma.595.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DQXX-ray2.20A2-496[»]
SMRQ42795. Positions 4-496.
ModBaseSearch...

Protein family/group databases

CAZyGH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsGLYMA06G45700.1; GLYMA06G45700.1; GLYMA06G45700.

Gene expression databases

GenevestigatorQ42795.

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

EvolutionaryTraceQ42795.

Entry information

Entry nameQ42795_SOYBN
AccessionPrimary (citable) accession number: Q42795
Entry history
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info