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

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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56634.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

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

« Hide

        10         20         30         40         50
QKDANFASGR NSIVHLFEWK WNDIADECER FLQPQGFGGV QISPPNEYLV
60 70 80 90 100
ADGRPWWERY QPVSYIINTR SGDESAFTDM TRRCNDAGVR IYVDAVINHM
110 120 130 140 150
TGMNGVGTSG SSADHDGMNY PAVPYGSGDF HSPCEVNNYQ DADNVRNCEL
160 170 180 190 200
VGLRDLNQGS DYVRGVLIDY MNHMIDLGVA GFRVDAAKHM SPGDLSVIFS
210 220 230 240 250
GLKNLNTDYG FADGARPFIY QEVIDLGGEA ISKNEYTGFG CVLEFQFGVS
260 270 280 290 300
LGNAFQGGNQ LKNLANWGPE WGLLEGLDAV VFVDNHDNQR TGGSQILTYK
310 320 330 340 350
NPKPYKMAIA FMLAHPYGTT RIMSSFDFTD NDQGPPQDGS GNLISPGIND
360 370 380 390 400
DNTCSNGYVC EHRWRQVYGM VGFRNAVEGT QVENWWSNDD NQIAFSRGSQ
410 420 430 440 450
GFVAFTNGGD LNQNLNTGLP AGTYCDVISG ELSGGSCTGK SVTVGDNGSA
460 470
DISLGSAEDD GVLAIHVNAK L
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: October 29, 2014
This is version 88 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