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P56634

- AMY_TENMO

UniProt

P56634 - AMY_TENMO

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Protein

Alpha-amylase

Gene
N/A
Organism
Tenebrio molitor (Yellow mealworm beetle)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Binds 1 calcium ion per subunit.
Binds 1 chloride ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi98 – 981Calcium
Metal bindingi146 – 1461Calcium; via carbonyl oxygen
Metal bindingi155 – 1551Calcium
Binding sitei183 – 1831Chloride
Active sitei185 – 1851Nucleophile
Metal bindingi189 – 1891Calcium; via carbonyl oxygen
Active sitei222 – 2221Proton donor
Binding sitei285 – 2851Chloride
Sitei287 – 2871Transition state stabilizer By similarity
Binding sitei321 – 3211Chloride

GO - Molecular functioni

  1. alpha-amylase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Chloride, Metal-binding

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase (EC:3.2.1.1)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
OrganismiTenebrio molitor (Yellow mealworm beetle)
Taxonomic identifieri7067 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaColeopteraPolyphagaCucujiformiaTenebrionidaeTenebrio

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471Alpha-amylasePRO_0000054290Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acid1 Publication
Disulfide bondi28 ↔ 84
Disulfide bondi134 ↔ 148
Disulfide bondi354 ↔ 360
Disulfide bondi425 ↔ 437

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

MINTiMINT-88080.

Structurei

Secondary structure

1
471
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 166
Helixi21 – 3010
Turni31 – 366
Beta strandi37 – 415
Helixi56 – 605
Beta strandi61 – 633
Beta strandi67 – 693
Helixi74 – 8613
Beta strandi90 – 956
Beta strandi105 – 1073
Beta strandi112 – 1143
Turni115 – 1184
Turni121 – 1244
Helixi127 – 1293
Helixi142 – 1476
Beta strandi148 – 1503
Helixi161 – 17616
Beta strandi181 – 1844
Helixi187 – 1893
Helixi192 – 2009
Helixi207 – 2093
Beta strandi218 – 2225
Beta strandi227 – 2304
Helixi233 – 2353
Turni236 – 2383
Beta strandi239 – 2435
Helixi245 – 25511
Turni256 – 2583
Helixi261 – 2666
Helixi269 – 2713
Helixi276 – 2783
Beta strandi279 – 2813
Helixi288 – 2914
Beta strandi292 – 2965
Helixi302 – 31413
Beta strandi317 – 3248
Beta strandi329 – 3324
Beta strandi335 – 3373
Beta strandi338 – 3403
Beta strandi347 – 3493
Turni350 – 3523
Beta strandi353 – 3553
Helixi361 – 3633
Helixi365 – 37612
Turni377 – 3793
Beta strandi382 – 3876
Beta strandi389 – 3979
Turni398 – 4003
Beta strandi401 – 4099
Beta strandi411 – 4166
Beta strandi421 – 4255
Turni427 – 4293
Beta strandi436 – 4394
Beta strandi441 – 4444
Beta strandi448 – 4547
Beta strandi461 – 4666
Helixi467 – 4693

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CLVX-ray2.00A1-471[»]
1JAEX-ray1.65A2-471[»]
1TMQX-ray2.50A1-471[»]
1VIWX-ray3.00A2-471[»]
ProteinModelPortaliP56634.
SMRiP56634. Positions 1-471.

Miscellaneous databases

EvolutionaryTraceiP56634.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

P56634-1 [UniParc]FASTAAdd to Basket

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QKDANFASGR NSIVHLFEWK WNDIADECER FLQPQGFGGV QISPPNEYLV    50
ADGRPWWERY QPVSYIINTR SGDESAFTDM TRRCNDAGVR IYVDAVINHM 100
TGMNGVGTSG SSADHDGMNY PAVPYGSGDF HSPCEVNNYQ DADNVRNCEL 150
VGLRDLNQGS DYVRGVLIDY MNHMIDLGVA GFRVDAAKHM SPGDLSVIFS 200
GLKNLNTDYG FADGARPFIY QEVIDLGGEA ISKNEYTGFG CVLEFQFGVS 250
LGNAFQGGNQ LKNLANWGPE WGLLEGLDAV VFVDNHDNQR TGGSQILTYK 300
NPKPYKMAIA FMLAHPYGTT RIMSSFDFTD NDQGPPQDGS GNLISPGIND 350
DNTCSNGYVC EHRWRQVYGM VGFRNAVEGT QVENWWSNDD NQIAFSRGSQ 400
GFVAFTNGGD LNQNLNTGLP AGTYCDVISG ELSGGSCTGK SVTVGDNGSA 450
DISLGSAEDD GVLAIHVNAK L 471
Length:471
Mass (Da):51,240
Last modified:December 15, 1998 - v1
Checksum:i9C3D48933D6C24C8
GO

Sequence databases

PIRiS75702.

Cross-referencesi

Sequence databases

PIRi S75702.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CLV X-ray 2.00 A 1-471 [» ]
1JAE X-ray 1.65 A 2-471 [» ]
1TMQ X-ray 2.50 A 1-471 [» ]
1VIW X-ray 3.00 A 2-471 [» ]
ProteinModelPortali P56634.
SMRi P56634. Positions 1-471.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-88080.

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P56634.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR006048. 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 ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view ]
PRINTSi PR00110. ALPHAAMYLASE.
SMARTi SM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiAMY_TENMO
AccessioniPrimary (citable) accession number: P56634
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: July 9, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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