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Protein

Alpha-amylase-related protein

Gene

Amyrel

Organism
Drosophila atripex (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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:
  • Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity
  • chlorideBy similarityNote: Binds 1 Cl- ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi118 – 1181CalciumBy similarity
Metal bindingi169 – 1691Calcium; via carbonyl oxygenBy similarity
Metal bindingi178 – 1781CalciumBy similarity
Binding sitei206 – 2061ChlorideBy similarity
Active sitei208 – 2081NucleophileBy similarity
Metal bindingi212 – 2121Calcium; via carbonyl oxygenBy similarity
Active sitei245 – 2451Proton donorBy similarity
Binding sitei308 – 3081ChlorideBy similarity
Sitei310 – 3101Transition state stabilizerBy similarity
Binding sitei343 – 3431ChlorideBy similarity

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-related protein (EC:3.2.1.1By similarity)
Gene namesi
Name:Amyrel
OrganismiDrosophila atripex (Fruit fly)
Taxonomic identifieri60715 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Organism-specific databases

FlyBaseiFBgn0021694. Datr\Amyrel.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020By similarityAdd
BLAST
Chaini21 – 494474Alpha-amylase-related proteinPRO_0000001369Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Pyrrolidone carboxylic acidBy similarity
Disulfide bondi48 ↔ 104By similarity
Disulfide bondi157 ↔ 171By similarity
Disulfide bondi376 ↔ 382By similarity
Disulfide bondi418 ↔ 441Sequence analysis
Disulfide bondi448 ↔ 460By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO77011.
SMRiO77011. Positions 21-494.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

O77011-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKFAAAVIL CLVAASSTLA QHNPHWWGNR NTIVHLFEWK WSDIAAECES
60 70 80 90 100
FLGPRGFAGV QVSPVNENII SAGRPWWERY QPISYKLVTR SGNEQEFADM
110 120 130 140 150
VRRCNDVGVR IYVDVLLNHM SGDFDGIAVG TAGSEAEPSK KSYPGVPYSA
160 170 180 190 200
LDFHPTCEIT DWNDRFQVQQ CELVGLKDLD QSSEWVRSKL IEFLDHLIEL
210 220 230 240 250
GVAGFRVDAA KHMAADDLSY IYSSISDLNI EHGFPHNARP FIFQEVIDHG
260 270 280 290 300
HETVSREEYN QLGAVTEFRF SEEIGNAFRG NNALKWLQSW GTGWGFLPSG
310 320 330 340 350
QALTFVDNHD NQRDMGAVLN YKSPKQYKMA TAFHLAYPYG ISRVMSSFAF
360 370 380 390 400
DDHDTAPPQD EQERIISPEF DEEGACVNGW ICEHRWRQIY AMVGFKNAVR
410 420 430 440 450
DTELSNWWDN GDNQISFCRG NKGFLAVNNN LYDLSRELQT CLPAGVYCDV
460 470 480 490
ISGSLIDGSC TGKSVTVDGN GYGYIHIGSD DFDGVLALHV DARI
Length:494
Mass (Da):55,505
Last modified:June 6, 2002 - v3
Checksum:i3AE5843F51C31C1B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96154 Genomic DNA. Translation: AAC39104.3.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96154 Genomic DNA. Translation: AAC39104.3.

3D structure databases

ProteinModelPortaliO77011.
SMRiO77011. Positions 21-494.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

FlyBaseiFBgn0021694. Datr\Amyrel.

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...

Publicationsi

  1. Da Lage J.-L.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiAMYR_DROAP
AccessioniPrimary (citable) accession number: O77011
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: June 6, 2002
Last modified: May 11, 2016
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  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.