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Protein

Alpha-amylase

Gene

aml

Organism
Streptomyces violaceus (Streptomyces venezuelae)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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.

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi120CalciumBy similarity1
Metal bindingi166Calcium; via carbonyl oxygenBy similarity1
Metal bindingi175CalciumBy similarity1
Active sitei205NucleophileBy similarity1
Metal bindingi209Calcium; via carbonyl oxygenBy similarity1
Active sitei232Proton donorBy similarity1
Sitei296Transition state stabilizerBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism
LigandCalcium, Metal-binding

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase (EC:3.2.1.1)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene namesi
Name:aml
OrganismiStreptomyces violaceus (Streptomyces venezuelae)
Taxonomic identifieri1936 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000000134429 – 569Alpha-amylaseAdd BLAST541

Expressioni

Inductioni

By maltose, and repression by glucose.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP22998.
SMRiP22998.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini468 – 569CBM20PROSITE-ProRule annotationAdd BLAST102

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiView protein in InterPro
IPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
PfamiView protein in Pfam
PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF00686. CBM_20. 1 hit.
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiView protein in SMART
SM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiView protein in PROSITE
PS51166. CBM20. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P22998-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARKTVAAAL ALVAGAAVAV TGNAPAQAVP PGEKDVTAVM FEWNFASVAR
60 70 80 90 100
ECTDRLGPAG YGYVQVSPPQ EHLQGGQWWT SYQPVSYKIA GRLGDRTAFK
110 120 130 140 150
NMIDTCHAAG VKVVADSVIN HMANGSGTGT GGTSFSKYDY PGLYSGSDMD
160 170 180 190 200
DCRATISNYQ DRANVQNCEL VQLPDLDTGE DHVRGKIAGY LNDLASLGVD
210 220 230 240 250
GFRIDAAKHM PAADLANIKS RLTNPNVFWK LEAIHGAGEA VSPSEYLGSG
260 270 280 290 300
DVQEFRYARD LKRVLQGEKL SYLKNFGEAW GHMPSGQSGV FVDNHDTERG
310 320 330 340 350
GDTLSYKDGA NYTLASVFML AWPYGSPDVH SGYEWTDKDA GPPNNGQVNA
360 370 380 390 400
CYTDGWKCQH AWREISSMVA FRNTARGQAV TNWWDNGNNA IAFGRGSKAY
410 420 430 440 450
VAINHETSAL TRTFQTSLPA GSYCDVQSNT PVTVNSSGQF TATLAANTAV
460 470 480 490 500
ALHVNATGCG STPTTPPTTP PATSGASFNV TATTVVGQNI YVTGNRAELG
510 520 530 540 550
NWAPASALKL DPATYPVWKL TVGLPAGTSF EYKYIRKDAA GNVTWESGAN
560
RTATVPASGQ LVLNDTFRS
Length:569
Mass (Da):60,637
Last modified:August 1, 1991 - v1
Checksum:i14CA5B1D56720043
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25263 Genomic DNA. Translation: AAB36561.1.
PIRiJS0101.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25263 Genomic DNA. Translation: AAB36561.1.
PIRiJS0101.

3D structure databases

ProteinModelPortaliP22998.
SMRiP22998.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiView protein in InterPro
IPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
PfamiView protein in Pfam
PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF00686. CBM_20. 1 hit.
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiView protein in SMART
SM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiView protein in PROSITE
PS51166. CBM20. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAMY_STRVL
AccessioniPrimary (citable) accession number: P22998
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: March 15, 2017
This is version 95 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.