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P56271

- AMYA_ASPNG

UniProt

P56271 - AMYA_ASPNG

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Protein

Acid alpha-amylase

Gene
N/A
Organism
Aspergillus niger
Status
Reviewed - Annotation score: 4 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+Note: Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei83 – 831SubstrateBy similarity
Metal bindingi121 – 1211Calcium 1
Binding sitei122 – 1221SubstrateBy similarity
Metal bindingi162 – 1621Calcium 1; via carbonyl oxygen
Metal bindingi175 – 1751Calcium 1
Binding sitei204 – 2041SubstrateBy similarity
Active sitei206 – 2061Nucleophile1 Publication
Metal bindingi206 – 2061Calcium 2
Metal bindingi210 – 2101Calcium 1; via carbonyl oxygen
Active sitei230 – 2301Proton donor1 Publication
Metal bindingi230 – 2301Calcium 2
Binding sitei234 – 2341Substrate; via amide nitrogenBy similarity
Binding sitei296 – 2961SubstrateBy similarity
Sitei297 – 2971Transition state stabilizer
Binding sitei344 – 3441SubstrateBy similarity

GO - Molecular functioni

  1. alpha-amylase activity Source: UniProtKB-EC
  2. calcium ion binding Source: InterPro

GO - Biological processi

  1. carbohydrate catabolic process Source: InterPro
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:3.2.1.1)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484Acid alpha-amylasePRO_0000054289Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi24 – 241N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi30 ↔ 38
Disulfide bondi150 ↔ 164
Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi240 ↔ 283
Disulfide bondi440 ↔ 475

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
484
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64Combined sources
Beta strandi11 – 133Combined sources
Helixi16 – 194Combined sources
Helixi32 – 343Combined sources
Helixi42 – 476Combined sources
Helixi49 – 535Combined sources
Turni54 – 563Combined sources
Beta strandi59 – 624Combined sources
Beta strandi66 – 683Combined sources
Beta strandi83 – 908Combined sources
Turni92 – 943Combined sources
Helixi97 – 10812Combined sources
Turni109 – 1113Combined sources
Beta strandi113 – 1186Combined sources
Beta strandi125 – 1273Combined sources
Helixi129 – 1313Combined sources
Helixi134 – 1363Combined sources
Beta strandi137 – 1393Combined sources
Helixi143 – 1453Combined sources
Helixi158 – 1636Combined sources
Beta strandi164 – 1674Combined sources
Beta strandi169 – 1735Combined sources
Helixi181 – 19818Combined sources
Beta strandi202 – 2065Combined sources
Helixi213 – 2153Combined sources
Helixi216 – 2238Combined sources
Beta strandi225 – 2295Combined sources
Helixi236 – 2394Combined sources
Helixi240 – 2445Combined sources
Beta strandi246 – 2505Combined sources
Helixi252 – 26211Combined sources
Helixi269 – 28214Combined sources
Helixi286 – 2883Combined sources
Beta strandi289 – 2913Combined sources
Helixi301 – 3033Combined sources
Helixi308 – 32013Combined sources
Beta strandi321 – 3288Combined sources
Turni329 – 3346Combined sources
Turni339 – 3435Combined sources
Helixi347 – 3504Combined sources
Helixi357 – 37519Combined sources
Turni377 – 3815Combined sources
Beta strandi385 – 3906Combined sources
Beta strandi393 – 4008Combined sources
Turni401 – 4033Combined sources
Beta strandi405 – 4106Combined sources
Beta strandi419 – 4235Combined sources
Beta strandi433 – 4364Combined sources
Turni437 – 4404Combined sources
Beta strandi441 – 4444Combined sources
Beta strandi451 – 4555Combined sources
Beta strandi461 – 4655Combined sources
Helixi466 – 4694Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AAAX-ray2.10A1-484[»]
ProteinModelPortaliP56271.
SMRiP56271. Positions 1-476.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56271.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni209 – 2102Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Phylogenomic databases

eggNOGiCOG0366.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013777. A-amylase_fun.
IPR015340. A_amylase_DUF1966_C.
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.
PF09260. DUF1966. 1 hit.
[Graphical view]
PIRSFiPIRSF001024. Alph-amyl_fung. 1 hit.
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

PIRi A35282.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2AAA X-ray 2.10 A 1-484 [» ]
ProteinModelPortali P56271.
SMRi P56271. Positions 1-476.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0366.

Miscellaneous databases

EvolutionaryTracei P56271.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR013777. A-amylase_fun.
IPR015340. A_amylase_DUF1966_C.
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.
PF09260. DUF1966. 1 hit.
[Graphical view ]
PIRSFi PIRSF001024. Alph-amyl_fung. 1 hit.
SMARTi SM00642. Aamy. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus."
    Boel E., Brady L., Brzozowski A.M., Derewenda Z., Dodson G.G., Jensen V.J., Petersen S.B., Swift H., Thim L., Woldike H.F.
    Biochemistry 29:6244-6249(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, CATALYTIC ACTIVITY, ACTIVE SITE.

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 26, 2014
This is version 81 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

External Data

Dasty 3