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Protein

Alpha-amylase

Gene

amy

Organism
Streptomyces griseus
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.

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

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, 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:amy
OrganismiStreptomyces griseus
Taxonomic identifieri1911 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28By similarityAdd BLAST28
ChainiPRO_000000134029 – 566Alpha-amylaseAdd BLAST538

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP30270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini465 – 566CBM20PROSITE-ProRule annotationAdd BLAST102

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated
Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation

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.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF00686. CBM_20. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P30270-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARRLATASL AVLAAAATAL TAPTPAAAAP PGAKDVTAVL FEWKFASVAR
60 70 80 90 100
ACTDSLGPAG YGYVQVSPPQ EHIQGSQWWT SYQPVSYKIA GRLGDRAAFK
110 120 130 140 150
SMVDTCHAAG VKVVADSVIN HMAAGSGTGT GGSAYQKYDY PGIWSGADMD
160 170 180 190 200
DCRSEINDYG NRANVQNCEL VGLADLDTGE PYVRDRIAAY LNDLLLLGVD
210 220 230 240 250
GFRIDAAKHM PAADLTAIKA KVGNGSTYWK QEAIHGAGEA VQPSEYLGTG
260 270 280 290 300
DVQEFRYARD LKRVFQNENL AHLKNFGEDW GYMASGKSAV FVDNHDTERG
310 320 330 340 350
GDTLNYKNGS AYTLAGVFML AWPYGSPDVH SGYEFTDHDA GPPNGGTVNA
360 370 380 390 400
CYSDGWKCQH AWPELSSMVG LRNTASGQPV TNWWDNGGDQ IAFGRGDKAY
410 420 430 440 450
VAINHEGSAL NRTFQSGLPG GAYCDVQSGR SVTVGSDGTF TATVAAGTAL
460 470 480 490 500
ALHTGARTCS GGGTGPGTGQ TSASFHVNAT TAWGENIYVT GDQAALGNWD
510 520 530 540 550
PARALKLDPA AYPVWKLDVP LAAGTPFQYK YLRKDAAGKA VWESGANRTA
560
TVGTTGALTL NDTWRG
Length:566
Mass (Da):59,706
Last modified:April 1, 1993 - v1
Checksum:iFCBAA7B172A617C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57568 Genomic DNA. Translation: CAA40798.1.
PIRiS14063.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57568 Genomic DNA. Translation: CAA40798.1.
PIRiS14063.

3D structure databases

ProteinModelPortaliP30270.
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.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
PF00686. CBM_20. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMY_STRGR
AccessioniPrimary (citable) accession number: P30270
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: May 11, 2016
This is version 90 of the entry and version 1 of the sequence. [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.