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Protein

Acid alpha-amylase

Gene
N/A
Organism
Aspergillus niger
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.1 Publication

Cofactori

Ca2+1 PublicationNote: Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei83SubstrateBy similarity1
Metal bindingi121Calcium 1Combined sources1 Publication1
Binding sitei122SubstrateBy similarity1
Metal bindingi162Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi175Calcium 1Combined sources1 Publication1
Binding sitei204SubstrateBy similarity1
Active sitei206Nucleophile1 Publication1
Metal bindingi206Calcium 2Combined sources1 Publication1
Metal bindingi210Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Active sitei230Proton donor1 Publication1
Metal bindingi230Calcium 2Combined sources1 Publication1
Binding sitei234Substrate; via amide nitrogenBy similarity1
Binding sitei297SubstrateBy similarity1
Sitei297Transition state stabilizerBy similarity1
Binding sitei344SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Acid alpha-amylase (EC:3.2.1.11 Publication)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000542891 – 484Acid alpha-amylaseAdd BLAST484

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi24N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi30 ↔ 38Combined sources1 Publication
Disulfide bondi150 ↔ 164Combined sources1 Publication
Glycosylationi157N-linked (GlcNAc...)Sequence analysis1
Glycosylationi197N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi240 ↔ 283Combined sources1 Publication
Disulfide bondi440 ↔ 475Combined sources1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP56271.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi5061.CADANGAP00008517.

Structurei

Secondary structure

1484
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 6Combined sources4
Beta strandi11 – 13Combined sources3
Helixi16 – 19Combined sources4
Helixi32 – 34Combined sources3
Helixi42 – 47Combined sources6
Helixi49 – 53Combined sources5
Turni54 – 56Combined sources3
Beta strandi59 – 62Combined sources4
Beta strandi66 – 68Combined sources3
Beta strandi83 – 90Combined sources8
Turni92 – 94Combined sources3
Helixi97 – 108Combined sources12
Turni109 – 111Combined sources3
Beta strandi113 – 118Combined sources6
Beta strandi125 – 127Combined sources3
Helixi129 – 131Combined sources3
Helixi134 – 136Combined sources3
Beta strandi137 – 139Combined sources3
Helixi143 – 145Combined sources3
Helixi158 – 163Combined sources6
Beta strandi164 – 167Combined sources4
Beta strandi169 – 173Combined sources5
Helixi181 – 198Combined sources18
Beta strandi202 – 206Combined sources5
Helixi213 – 215Combined sources3
Helixi216 – 223Combined sources8
Beta strandi225 – 229Combined sources5
Helixi236 – 239Combined sources4
Helixi240 – 244Combined sources5
Beta strandi246 – 250Combined sources5
Helixi252 – 262Combined sources11
Helixi269 – 282Combined sources14
Helixi286 – 288Combined sources3
Beta strandi289 – 291Combined sources3
Helixi301 – 303Combined sources3
Helixi308 – 320Combined sources13
Beta strandi321 – 328Combined sources8
Turni329 – 334Combined sources6
Turni339 – 343Combined sources5
Helixi347 – 350Combined sources4
Helixi357 – 375Combined sources19
Turni377 – 381Combined sources5
Beta strandi385 – 390Combined sources6
Beta strandi393 – 400Combined sources8
Turni401 – 403Combined sources3
Beta strandi405 – 410Combined sources6
Beta strandi419 – 423Combined sources5
Beta strandi433 – 436Combined sources4
Turni437 – 440Combined sources4
Beta strandi441 – 444Combined sources4
Beta strandi451 – 455Combined sources5
Beta strandi461 – 465Combined sources5
Helixi466 – 469Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AAAX-ray2.10A1-484[»]
ProteinModelPortaliP56271.
SMRiP56271.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56271.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni209 – 210Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Phylogenomic databases

eggNOGiKOG0471. Eukaryota.
COG0366. LUCA.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015340. A_amylase_DUF1966_C.
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.
PF09260. DUF1966. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

P56271-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
LSAASWRTQS IYFLLTDRFG RTDNSTTATC NTGNEIYCGG SWQGIIDHLD
60 70 80 90 100
YIEGMGFTAI WISPITEQLP QDTADGEAYH GYWQQKIYDV NSNFGTADNL
110 120 130 140 150
KSLSDALHAR GMYLMVDVVP DHMGYAGNGN DVDYSVFDPF DSSSYFHPYC
160 170 180 190 200
LITDWDNLTM VEDCWEGDTI VSLPDLDTTE TAVRTIWYDW VADLVSNYSV
210 220 230 240 250
DGLRIDSVLE VQPDFFPGYN KASGVYCVGE IDNGNPASDC PYQKVLDGVL
260 270 280 290 300
NYPIYWQLLY AFESSSGSIS NLYNMIKSVA SDCSDPTLLG NFIENHDNPR
310 320 330 340 350
FAKYTSDYSQ AKNVLSYIFL SDGIPIVYAG EEQHYAGGKV PYNREATWLS
360 370 380 390 400
GYDTSAELYT WIATTNAIRK LAIAADSAYI TYANDAFYTD SNTIAMAKGT
410 420 430 440 450
SGSQVITVLS NKGSSGSSYT LTLSGSGYTS GTKLIEAYTC TSVTVDSSGD
460 470 480
IPVPMASGLP RVLLPASVVD SSSLCGGSGR LYVE
Length:484
Mass (Da):52,935
Last modified:July 15, 1998 - v1
Checksum:i04D596E34680656D
GO

Sequence databases

PIRiA35282.

Cross-referencesi

Sequence databases

PIRiA35282.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AAAX-ray2.10A1-484[»]
ProteinModelPortaliP56271.
SMRiP56271.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00008517.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbiP56271.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0471. Eukaryota.
COG0366. LUCA.

Miscellaneous databases

EvolutionaryTraceiP56271.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015340. A_amylase_DUF1966_C.
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.
PF09260. DUF1966. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAMYA_ASPNG
AccessioniPrimary (citable) accession number: P56271
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: November 2, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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.