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Protein

Alpha-amylase

Gene
N/A
Organism
Tenebrio molitor (Yellow mealworm beetle)
Status
Reviewed-Annotation score: 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.By similarity

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi98CalciumCombined sources3 Publications1
Metal bindingi146Calcium; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi155CalciumCombined sources3 Publications1
Binding sitei183ChlorideCombined sources3 Publications1
Active sitei185Nucleophile1
Metal bindingi189Calcium; via carbonyl oxygenCombined sources3 Publications1
Active sitei222Proton donor1
Binding sitei285ChlorideCombined sources3 Publications1
Sitei287Transition state stabilizerBy similarity1
Binding sitei321ChlorideCombined sources3 Publications1

GO - Molecular functioni

GO - Biological processi

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:3.2.1.1By similarity)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
OrganismiTenebrio molitor (Yellow mealworm beetle)
Taxonomic identifieri7067 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaColeopteraPolyphagaCucujiformiaTenebrionidaeTenebrio

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3580521.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000542901 – 471Alpha-amylaseAdd BLAST471

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1Pyrrolidone carboxylic acid2 Publications1
Disulfide bondi28 ↔ 84Combined sources3 Publications
Disulfide bondi134 ↔ 148Combined sources3 Publications
Disulfide bondi354 ↔ 360Combined sources3 Publications
Disulfide bondi425 ↔ 437Combined sources3 Publications

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

MINTiMINT-88080.

Structurei

Secondary structure

1471
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 16Combined sources6
Helixi21 – 30Combined sources10
Turni31 – 36Combined sources6
Beta strandi37 – 41Combined sources5
Helixi56 – 60Combined sources5
Beta strandi61 – 63Combined sources3
Beta strandi67 – 69Combined sources3
Helixi74 – 86Combined sources13
Beta strandi90 – 95Combined sources6
Beta strandi105 – 107Combined sources3
Beta strandi112 – 114Combined sources3
Turni115 – 118Combined sources4
Turni121 – 124Combined sources4
Helixi127 – 129Combined sources3
Helixi142 – 147Combined sources6
Beta strandi148 – 150Combined sources3
Helixi161 – 176Combined sources16
Beta strandi181 – 184Combined sources4
Helixi187 – 189Combined sources3
Helixi192 – 200Combined sources9
Helixi207 – 209Combined sources3
Beta strandi218 – 222Combined sources5
Beta strandi227 – 230Combined sources4
Helixi233 – 235Combined sources3
Turni236 – 238Combined sources3
Beta strandi239 – 243Combined sources5
Helixi245 – 255Combined sources11
Turni256 – 258Combined sources3
Helixi261 – 266Combined sources6
Helixi269 – 271Combined sources3
Helixi276 – 278Combined sources3
Beta strandi279 – 281Combined sources3
Helixi288 – 291Combined sources4
Beta strandi292 – 296Combined sources5
Helixi302 – 314Combined sources13
Beta strandi317 – 324Combined sources8
Beta strandi329 – 332Combined sources4
Beta strandi335 – 337Combined sources3
Beta strandi338 – 340Combined sources3
Beta strandi347 – 349Combined sources3
Turni350 – 352Combined sources3
Beta strandi353 – 355Combined sources3
Helixi361 – 363Combined sources3
Helixi365 – 376Combined sources12
Turni377 – 379Combined sources3
Beta strandi382 – 387Combined sources6
Beta strandi389 – 397Combined sources9
Turni398 – 400Combined sources3
Beta strandi401 – 409Combined sources9
Beta strandi411 – 416Combined sources6
Beta strandi421 – 425Combined sources5
Turni427 – 429Combined sources3
Beta strandi436 – 439Combined sources4
Beta strandi441 – 444Combined sources4
Beta strandi448 – 454Combined sources7
Beta strandi461 – 466Combined sources6
Helixi467 – 469Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CLVX-ray2.00A1-471[»]
1JAEX-ray1.65A2-471[»]
1TMQX-ray2.50A1-471[»]
1VIWX-ray3.00A2-471[»]
ProteinModelPortaliP56634.
SMRiP56634.
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/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
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

PIRiS75702.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CLVX-ray2.00A1-471[»]
1JAEX-ray1.65A2-471[»]
1TMQX-ray2.50A1-471[»]
1VIWX-ray3.00A2-471[»]
ProteinModelPortaliP56634.
SMRiP56634.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-88080.

Chemistry databases

ChEMBLiCHEMBL3580521.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP56634.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
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.
ProtoNetiSearch...

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: November 30, 2016
This is version 97 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.