Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P56271

- AMYA_ASPNG

UniProt

P56271 - AMYA_ASPNG

Protein

Acid alpha-amylase

Gene
N/A
Organism
Aspergillus niger
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (15 Jul 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    LSAASWRTQS IYFLLTDRFG RTDNSTTATC NTGNEIYCGG SWQGIIDHLD    50
    YIEGMGFTAI WISPITEQLP QDTADGEAYH GYWQQKIYDV NSNFGTADNL 100
    KSLSDALHAR GMYLMVDVVP DHMGYAGNGN DVDYSVFDPF DSSSYFHPYC 150
    LITDWDNLTM VEDCWEGDTI VSLPDLDTTE TAVRTIWYDW VADLVSNYSV 200
    DGLRIDSVLE VQPDFFPGYN KASGVYCVGE IDNGNPASDC PYQKVLDGVL 250
    NYPIYWQLLY AFESSSGSIS NLYNMIKSVA SDCSDPTLLG NFIENHDNPR 300
    FAKYTSDYSQ AKNVLSYIFL SDGIPIVYAG EEQHYAGGKV PYNREATWLS 350
    GYDTSAELYT WIATTNAIRK LAIAADSAYI TYANDAFYTD SNTIAMAKGT 400
    SGSQVITVLS NKGSSGSSYT LTLSGSGYTS GTKLIEAYTC TSVTVDSSGD 450
    IPVPMASGLP RVLLPASVVD SSSLCGGSGR LYVE 484
    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:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 79 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