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P56634 (AMY_TENMO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 85. 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

Names and origin

Protein namesRecommended name:
Alpha-amylase

EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
OrganismTenebrio molitor (Yellow mealworm beetle)
Taxonomic identifier7067 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaColeopteraPolyphagaCucujiformiaTenebrionidaeTenebrio

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

Cofactor

Binds 1 calcium ion per subunit.

Binds 1 chloride ion per subunit.

Subunit structure

Monomer.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 471471Alpha-amylase
PRO_0000054290

Sites

Active site1851Nucleophile
Active site2221Proton donor
Metal binding981Calcium
Metal binding1461Calcium; via carbonyl oxygen
Metal binding1551Calcium
Metal binding1891Calcium; via carbonyl oxygen
Binding site1831Chloride
Binding site2851Chloride
Binding site3211Chloride
Site2871Transition state stabilizer By similarity

Amino acid modifications

Modified residue11Pyrrolidone carboxylic acid Ref.1
Disulfide bond28 ↔ 84
Disulfide bond134 ↔ 148
Disulfide bond354 ↔ 360
Disulfide bond425 ↔ 437

Secondary structure

.................................................................................................. 471
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56634 [UniParc].

Last modified December 15, 1998. Version 1.
Checksum: 9C3D48933D6C24C8

FASTA47151,240
        10         20         30         40         50         60 
QKDANFASGR NSIVHLFEWK WNDIADECER FLQPQGFGGV QISPPNEYLV ADGRPWWERY 

        70         80         90        100        110        120 
QPVSYIINTR SGDESAFTDM TRRCNDAGVR IYVDAVINHM TGMNGVGTSG SSADHDGMNY 

       130        140        150        160        170        180 
PAVPYGSGDF HSPCEVNNYQ DADNVRNCEL VGLRDLNQGS DYVRGVLIDY MNHMIDLGVA 

       190        200        210        220        230        240 
GFRVDAAKHM SPGDLSVIFS GLKNLNTDYG FADGARPFIY QEVIDLGGEA ISKNEYTGFG 

       250        260        270        280        290        300 
CVLEFQFGVS LGNAFQGGNQ LKNLANWGPE WGLLEGLDAV VFVDNHDNQR TGGSQILTYK 

       310        320        330        340        350        360 
NPKPYKMAIA FMLAHPYGTT RIMSSFDFTD NDQGPPQDGS GNLISPGIND DNTCSNGYVC 

       370        380        390        400        410        420 
EHRWRQVYGM VGFRNAVEGT QVENWWSNDD NQIAFSRGSQ GFVAFTNGGD LNQNLNTGLP 

       430        440        450        460        470 
AGTYCDVISG ELSGGSCTGK SVTVGDNGSA DISLGSAEDD GVLAIHVNAK L 

« Hide

References

[1]"The alpha-amylase from the yellow meal worm: complete primary structure, crystallization and preliminary X-ray analysis."
Strobl S., Gomis-Rueth F.-X., Maskos K., Frank G., Huber R., Glockshuber R.
FEBS Lett. 409:109-114(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Crystal structure of yellow meal worm alpha-amylase at 1.64-A resolution."
Strobl S., Maskos K., Betz M., Wiegand G., Huber R., Gomis-Rueth F.-X., Glockshuber R.
J. Mol. Biol. 278:617-628(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
[3]"A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5-A resolution."
Strobl S., Maskos K., Wiegand G., Huber R., Gomis-Rueth F.-X., Glockshuber R.
Structure 6:911-921(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[4]"Specific inhibition of insect alpha-amylases: yellow meal worm alpha-amylase in complex with the amaranth alpha-amylase inhibitor at 2.0 A resolution."
Pereira P.J., Lozanov V., Patthy A., Huber R., Bode W., Pongor S., Strobl S.
Structure 7:1079-1088(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRS75702.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CLVX-ray2.00A2-471[»]
1JAEX-ray1.65A2-471[»]
1TMQX-ray2.50A2-471[»]
1VIWX-ray3.00A2-471[»]
ProteinModelPortalP56634.
SMRP56634. Positions 1-471.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-88080.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006048. A-amylase_b_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP56634.

Entry information

Entry nameAMY_TENMO
AccessionPrimary (citable) accession number: P56634
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: October 16, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries