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Protein

Alpha-amylase

Gene
N/A
Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Unreviewed-Annotation score: Annotation score: 2 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.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Keywords - Biological processi

Carbohydrate metabolismUniRule annotation

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylaseUniRule annotation (EC:3.2.1.1UniRule annotation)
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)Imported
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4412.

Interactioni

Chemistry

BindingDBiP94451.

Structurei

3D structure databases

ProteinModelPortaliP94451.
SMRiP94451. Positions 2-555.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 415403AamyInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.UniRule annotation

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR006046. 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.
IPR032091. Malt_amylase_C.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF16657. Malt_amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

P94451-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKTWWKEGV AYQIYPRSFM DANGDGIGDL RGIIEKLDYL VELGVDIVWI
60 70 80 90 100
CPIYRSPNAD NGYDISDYYA IMDEFGTMDD FDELLAQAHR RGLKIILDLV
110 120 130 140 150
INHTSDEHPW FIESRSSRDN PKRDWYIWRD GKDGREPNNW ESIFGGSAWQ
160 170 180 190 200
YDERTGQYYL HLFDVKQPDL NWENSEVRQA LYDMINWWLD KGIDGFRIDA
210 220 230 240 250
ISHIKKKPGL PDLPNPKGLK YVPSFAAHMN QPGIMEYLRE LKEQTFARYD
260 270 280 290 300
IMTVGEANGV TVDEAEQWVG EENGVFHMIF QFEHLGLWKR KADGSIDVRR
310 320 330 340 350
LKRTLTKWQK GLENRGWNAL FLENHDLPRS VSTWGNDREY WAESAKALGA
360 370 380 390 400
LYFFMQGTPF IYQGQEIGMT NVQFSDIRDY RDVAALRLYE LERANGRTHE
410 420 430 440 450
EVMKIIWKTG RDNSRTPMQW SDAPNAGFTT GTPWIKVNEN YRTINVEAER
460 470 480 490 500
RDPNSVWSFY RQMIQLRKAN ELFVYGAYDL LLENHPSIYA YTRTLGRDRA
510 520 530 540 550
LIIVNVSDRP SLYRYDGFRL QSSDLALSNY PVRPHKNATR FKLKPYEARV

YIWKE
Length:555
Mass (Da):65,235
Last modified:May 1, 1997 - v1
Checksum:iE7275ED753918DE6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84648 Genomic DNA. Translation: BAA12704.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84648 Genomic DNA. Translation: BAA12704.1.

3D structure databases

ProteinModelPortaliP94451.
SMRiP94451. Positions 2-555.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP94451.
ChEMBLiCHEMBL4412.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR006046. 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.
IPR032091. Malt_amylase_C.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 2 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF16657. Malt_amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Bacillus stearothermophilus ATCC12016 alpha-glucosidase specific for alpha-1,4 bonds of maltosaccharides and alpha-glucans shows high amino acid sequence similarities to seven alpha-D-glucohydrolases with different substrate specificity."
    Takii Y., Takahashi K., Yamamoto K., Sogabe Y., Suzuki Y.
    Appl. Microbiol. Biotechnol. 44:629-634(1996)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC 12016Imported.

Entry informationi

Entry nameiP94451_GEOSE
AccessioniPrimary (citable) accession number: P94451
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1997
Last sequence update: May 1, 1997
Last modified: May 11, 2016
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.