Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alpha-amylase

Gene

amyS

Organism
Bacillus licheniformis
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Active up to pH 11.

Temperature dependencei

Active up to 100 degrees Celsius.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi133Calcium 1Combined sources2 Publications1
Metal bindingi190Calcium 2Combined sources2 Publications1
Metal bindingi190Sodium2 Publications1
Metal bindingi210Calcium 2; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi212Calcium 2Combined sources2 Publications1
Metal bindingi212Sodium2 Publications1
Metal bindingi223Calcium 1Combined sources2 Publications1
Metal bindingi223Sodium2 Publications1
Metal bindingi229Calcium 1Combined sources2 Publications1
Metal bindingi229Sodium2 Publications1
Metal bindingi231Calcium 2Combined sources2 Publications1
Metal bindingi233Calcium 2Combined sources2 Publications1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei260Nucleophile1
Metal bindingi264Calcium 1; via carbonyl oxygenCombined sources1
Active sitei290Proton donor1
Metal bindingi329Calcium 3; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi331Calcium 3; via carbonyl oxygenCombined sources2 Publications1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei357Transition state stabilizerBy similarity1
Metal bindingi435Calcium 3; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi436Calcium 3Combined sources2 Publications1
Metal bindingi459Calcium 3Combined sources2 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.1 669

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH13 Glycoside Hydrolase Family 13

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Alpha-amylase (EC:3.2.1.13 Publications)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
BLA
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:amyS
Synonyms:amyL
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBacillus licheniformis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1402 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Used in the food industry for high temperature liquefaction of starch-containing mashes and in the detergent industry to remove starch. Sold under the name Termamyl by Novozymes.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi64H → X: No effect on thermostability. 1 Publication1
Mutagenesisi150D → X: Decrease in thermostability. 1 Publication1
Mutagenesisi155N → X: Decrease in thermostability. 1 Publication1
Mutagenesisi162H → I or V: Increase in thermostability. 1 Publication1
Mutagenesisi162H → P: Great decrease in thermostability. 1 Publication1
Mutagenesisi162H → V: Great increase in thermostability; when associated with F-219; V-238; S-293 and Y-294. 1 Publication1
Mutagenesisi175R → X: No effect on thermostability. 1 Publication1
Mutagenesisi193D → A, C, E, H or R: Loss of activity. 1 Publication1
Mutagenesisi201N → H or K: Increase in thermostability. 1 Publication1
Mutagenesisi201N → R: Great increase in thermostability. 1 Publication1
Mutagenesisi207Q → X: No effect on thermostability. 1 Publication1
Mutagenesisi217N → P: Great increase in thermostability. 1 Publication1
Mutagenesisi219N → A, E, Q, P or S: Great decrease in thermostability. 1 Publication1
Mutagenesisi219N → F: Great increase in thermostability. Great increase in thermostability; when associated with V-162; V-238; S-293 and Y-294. 1 Publication1
Mutagenesisi219N → L: Increase in thermostability. 1 Publication1
Mutagenesisi221N → X: Great decrease in thermostability. 1 Publication1
Mutagenesisi229D → X: Great decrease in thermostability. 1 Publication1
Mutagenesisi233D → X: Great decrease in thermostability. 1 Publication1
Mutagenesisi238A → V: Increase in thermostability. Great increase in thermostability; when associated with V-162; F-219; S-293 and Y-294. 1 Publication1
Mutagenesisi276H → X: No effect on thermostability. 1 Publication1
Mutagenesisi292W → L: Decrease in activity; when associated with Y-315. 1 Publication1
Mutagenesisi293Q → S: Increase in thermostability; when associated with Y-294. Great increase in thermostability; when associated with V-162; F-219; V-238 and Y-294. 1 Publication1
Mutagenesisi294N → Y: Increase in thermostability; when associated with S-293. Great increase in thermostability; when associated with V-162; F-219; V-238 and S-293. 1 Publication1
Mutagenesisi298A → H, K, L, Q or R: Loss of activity. 1 Publication1
Mutagenesisi300E → X: No effect on thermostability. 1 Publication1
Mutagenesisi315V → F: Decrease in activity. 1 Publication1
Mutagenesisi315V → Y: Increase in activity. Decrease in activity; when associated with W-292. 1 Publication1
Mutagenesisi322H → X: No effect on thermostability. 1 Publication1
Mutagenesisi359Q → X: No effect on thermostability. 1 Publication1
Mutagenesisi365E → H: Loss of activity. 1 Publication1
Mutagenesisi435H → X: No effect on thermostability. 1 Publication1
Mutagenesisi479H → X: No effect on thermostability. 1 Publication1

Protein family/group databases

Allergome; a platform for allergen knowledge

More...
Allergomei
8255 Bac li aA

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4215

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 291 PublicationAdd BLAST29
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000133230 – 512Alpha-amylaseAdd BLAST483

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P06278

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P06278

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1512
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P06278

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P06278

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P06278

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105E5K Bacteria
COG0366 LUCA

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.1180, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013776 A-amylase_thermo
IPR015237 Alpha-amylase_C_pro
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF09154 DUF1939, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001021 Alph-amls_thrmst, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00642 Aamy, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445 SSF51445, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P06278-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKQQKRLYAR LLTLLFALIF LLPHSAAAAA NLNGTLMQYF EWYMPNDGQH
60 70 80 90 100
WKRLQNDSAY LAEHGITAVW IPPAYKGTSQ ADVGYGAYDL YDLGEFHQKG
110 120 130 140 150
TVRTKYGTKG ELQSAIKSLH SRDINVYGDV VINHKGGADA TEDVTAVEVD
160 170 180 190 200
PADRNRVISG EHRIKAWTHF HFPGRGSTYS DFKWHWYHFD GTDWDESRKL
210 220 230 240 250
NRIYKFQGKA WDWEVSNENG NYDYLMYADI DYDHPDVAAE IKRWGTWYAN
260 270 280 290 300
ELQLDGFRLD AVKHIKFSFL RDWVNHVREK TGKEMFTVAE YWQNDLGALE
310 320 330 340 350
NYLNKTNFNH SVFDVPLHYQ FHAASTQGGG YDMRKLLNST VVSKHPLKAV
360 370 380 390 400
TFVDNHDTQP GQSLESTVQT WFKPLAYAFI LTRESGYPQV FYGDMYGTKG
410 420 430 440 450
DSQREIPALK HKIEPILKAR KQYAYGAQHD YFDHHDIVGW TREGDSSVAN
460 470 480 490 500
SGLAALITDG PGGAKRMYVG RQNAGETWHD ITGNRSEPVV INSEGWGEFH
510
VNGGSVSIYV QR
Length:512
Mass (Da):58,549
Last modified:January 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD8BB77759CD4C482
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti4Q → H no nucleotide entry (PubMed:6334606).Curated1
Sequence conflicti13T → P in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti13T → P no nucleotide entry (PubMed:6334606).Curated1
Sequence conflicti33N → I in AAA22232 (PubMed:2265757).Curated1
Sequence conflicti38Q → Y AA sequence (PubMed:6172418).Curated1
Sequence conflicti48G → R no nucleotide entry (PubMed:6334606).Curated1
Sequence conflicti62 – 64AEH → VED no nucleotide entry (PubMed:6334606).Curated3
Sequence conflicti68 – 69AV → VA no nucleotide entry (PubMed:6334606).Curated2
Sequence conflicti72P → S no nucleotide entry (PubMed:6334606).Curated1
Sequence conflicti81A → D in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti81A → D no nucleotide entry (PubMed:6334606).Curated1
Sequence conflicti105 – 117Missing no nucleotide entry (PubMed:6334606).CuratedAdd BLAST13
Sequence conflicti117K → N in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti158I → T in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti162H → Q in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti163R → L in AAA22240 (PubMed:3009417).Curated1
Sequence conflicti171H → Q in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti218E → V in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti237 – 238VA → AT in AAO26743 (PubMed:14632998).Curated2
Sequence conflicti339S → G in AAA22240 (PubMed:3009417).Curated1
Sequence conflicti339S → G in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti347L → V in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti349A → S in AAA22240 (PubMed:3009417).Curated1
Sequence conflicti385S → A in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti390V → I in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti401D → A in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti421K → I in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti464A → T in AAO26743 (PubMed:14632998).Curated1
Sequence conflicti487 – 488EP → DS in AAO26743 (PubMed:14632998).Curated2
Sequence conflicti493S → A in AAO26743 (PubMed:14632998).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X03236 Genomic DNA Translation: CAA26981.1
M38570 Genomic DNA Translation: AAA22226.1
M13256 Genomic DNA Translation: AAA22240.1
AF438149 Genomic DNA Translation: AAO26743.1
K01984 Genomic DNA Translation: AAA22193.1
M62637 Genomic DNA Translation: AAA22232.1
M26412 Genomic DNA Translation: AAA22237.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A91997 ALBSL

NCBI Reference Sequences

More...
RefSeqi
WP_017474613.1, NZ_PIJD01000016.1
WP_025807921.1, NZ_NPCV01000044.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03236 Genomic DNA Translation: CAA26981.1
M38570 Genomic DNA Translation: AAA22226.1
M13256 Genomic DNA Translation: AAA22240.1
AF438149 Genomic DNA Translation: AAO26743.1
K01984 Genomic DNA Translation: AAA22193.1
M62637 Genomic DNA Translation: AAA22232.1
M26412 Genomic DNA Translation: AAA22237.1
PIRiA91997 ALBSL
RefSeqiWP_017474613.1, NZ_PIJD01000016.1
WP_025807921.1, NZ_NPCV01000044.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BLIX-ray1.90A30-512[»]
1BPLX-ray2.20A30-218[»]
B219-512[»]
1E3XX-ray1.90A330-512[»]
1E3ZX-ray1.93A330-512[»]
1E40X-ray2.20A330-512[»]
1E43X-ray1.70A330-512[»]
1OB0X-ray1.83A30-512[»]
1VJSX-ray1.70A30-512[»]
ProteinModelPortaliP06278
SMRiP06278
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP06278
ChEMBLiCHEMBL4215

Protein family/group databases

Allergomei8255 Bac li aA
CAZyiGH13 Glycoside Hydrolase Family 13

Proteomic databases

PRIDEiP06278

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105E5K Bacteria
COG0366 LUCA

Enzyme and pathway databases

BRENDAi3.2.1.1 669

Miscellaneous databases

EvolutionaryTraceiP06278

Family and domain databases

Gene3Di2.60.40.1180, 1 hit
InterProiView protein in InterPro
IPR013776 A-amylase_thermo
IPR015237 Alpha-amylase_C_pro
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF09154 DUF1939, 1 hit
PIRSFiPIRSF001021 Alph-amls_thrmst, 1 hit
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAMY_BACLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P06278
Secondary accession number(s): Q45283, Q84I71
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: December 5, 2018
This is version 148 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again