UniProtKB - P00690 (AMYP_PIG)
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>sp|P00690|AMYP_PIG Pancreatic alpha-amylase OS=Sus scrofa OX=9823 GN=AMY2 PE=1 SV=3 MKLFLLLSAFGFCWAQYAPQTQSGRTSIVHLFEWRWVDIALECERYLGPKGFGGVQVSPP NENIVVTNPSRPWWERYQPVSYKLCTRSGNENEFRDMVTRCNNVGVRIYVDAVINHMCGS GAAAGTGTTCGSYCNPGNREFPAVPYSAWDFNDGKCKTASGGIESYNDPYQVRDCQLVGL LDLALEKDYVRSMIADYLNKLIDIGVAGFRIDASKHMWPGDIKAVLDKLHNLNTNWFPAG SRPFIFQEVIDLGGEAIQSSEYFGNGRVTEFKYGAKLGTVVRKWSGEKMSYLKNWGEGWG FMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKVAVGFMLAHPYGFTRVMSSYRWA RNFVNGQDVNDWIGPPNNNGVIKEVTINADTTCGNDWVCEHRWRQIRNMVWFRNVVDGQP FANWWANGSNQVAFGRGNRGFIVFNNDDWQLSSTLQTGLPGGTYCDVISGDKVGNSCTGI KVYVSSDGTAQFSISNSAEDPFIAIHAESKLCommunity curation ()Add a publicationFeedback
Pancreatic alpha-amylase
AMY2
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>Select a section on the left to see content.
<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
Miscellaneous
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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
- Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
EC:3.2.1.1
<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:- Ca2+
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Three dimensional structure of porcine pancreatic alpha-amylase at 2.9-A resolution. Role of calcium in structure and activity."
Buisson G., Duee E., Haser R., Payan F.
EMBO J. 6:3909-3916(1987) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), COFACTOR, DISULFIDE BONDS. - Ref.8"The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution."
Qian M., Haser R., Buisson G., Duee E., Payan F.
Biochemistry 33:6284-6294(1994) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM, DISULFIDE BONDS, COFACTOR. - Ref.9"The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat."
Wiegand G., Epp O., Huber R.
J. Mol. Biol. 247:99-110(1995) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 16-511 IN COMPLEX WITH INHIBITOR; CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.10"Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics."
Machius M., Vertesy L., Huber R., Wiegand G.
J. Mol. Biol. 260:409-421(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM; GLUCOSE AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.11"Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose."
Gilles C., Astier J.-P., Marchis-Mouren G., Cambillau C., Payan F.
Eur. J. Biochem. 238:561-569(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM, SEQUENCE REVISION, COFACTOR, DISULFIDE BONDS. - Ref.12"Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex."
Bompard-Gilles C., Rousseau P., Rouge P., Payan F.
Structure 4:1441-1452(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 17-511 IN COMPLEX WITH INHIBITOR AND CALCIUM, COFACTOR, DISULFIDE BONDS. - Ref.13"Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03-A resolution."
Qian M., Spinelli S., Driguez H., Payan F.
Protein Sci. 6:2285-2296(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.14"Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex."
Qian M., Nahoum V., Bonicel J., Bischoff H., Henrissat B., Payan F.
Biochemistry 40:7700-7709(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) IN COMPLEX WITH CALCIUM; CHLORIDE AND OLIGOSACCHARIDE INHIBITOR, COFACTOR, DISULFIDE BOND. - Ref.15"Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology."
Desmyter A., Spinelli S., Payan F., Lauwereys M., Wyns L., Muyldermans S., Cambillau C.
J. Biol. Chem. 277:23645-23650(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR.
Manual assertion based on experiment ini
- Ref.6"Three dimensional structure of porcine pancreatic alpha-amylase at 2.9-A resolution. Role of calcium in structure and activity."
Buisson G., Duee E., Haser R., Payan F.
EMBO J. 6:3909-3916(1987) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), COFACTOR, DISULFIDE BONDS. - Ref.8"The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution."
Qian M., Haser R., Buisson G., Duee E., Payan F.
Biochemistry 33:6284-6294(1994) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM, DISULFIDE BONDS, COFACTOR. - Ref.9"The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat."
Wiegand G., Epp O., Huber R.
J. Mol. Biol. 247:99-110(1995) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 16-511 IN COMPLEX WITH INHIBITOR; CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.10"Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics."
Machius M., Vertesy L., Huber R., Wiegand G.
J. Mol. Biol. 260:409-421(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM; GLUCOSE AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.11"Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose."
Gilles C., Astier J.-P., Marchis-Mouren G., Cambillau C., Payan F.
Eur. J. Biochem. 238:561-569(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM, SEQUENCE REVISION, COFACTOR, DISULFIDE BONDS. - Ref.12"Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex."
Bompard-Gilles C., Rousseau P., Rouge P., Payan F.
Structure 4:1441-1452(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 17-511 IN COMPLEX WITH INHIBITOR AND CALCIUM, COFACTOR, DISULFIDE BONDS. - Ref.13"Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03-A resolution."
Qian M., Spinelli S., Driguez H., Payan F.
Protein Sci. 6:2285-2296(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.14"Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex."
Qian M., Nahoum V., Bonicel J., Bischoff H., Henrissat B., Payan F.
Biochemistry 40:7700-7709(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) IN COMPLEX WITH CALCIUM; CHLORIDE AND OLIGOSACCHARIDE INHIBITOR, COFACTOR, DISULFIDE BOND. - Ref.15"Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology."
Desmyter A., Spinelli S., Payan F., Lauwereys M., Wyns L., Muyldermans S., Cambillau C.
J. Biol. Chem. 277:23645-23650(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR.
- chloride
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.6"Three dimensional structure of porcine pancreatic alpha-amylase at 2.9-A resolution. Role of calcium in structure and activity."
Buisson G., Duee E., Haser R., Payan F.
EMBO J. 6:3909-3916(1987) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), COFACTOR, DISULFIDE BONDS. - Ref.9"The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat."
Wiegand G., Epp O., Huber R.
J. Mol. Biol. 247:99-110(1995) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 16-511 IN COMPLEX WITH INHIBITOR; CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.10"Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics."
Machius M., Vertesy L., Huber R., Wiegand G.
J. Mol. Biol. 260:409-421(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM; GLUCOSE AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.13"Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03-A resolution."
Qian M., Spinelli S., Driguez H., Payan F.
Protein Sci. 6:2285-2296(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.14"Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex."
Qian M., Nahoum V., Bonicel J., Bischoff H., Henrissat B., Payan F.
Biochemistry 40:7700-7709(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) IN COMPLEX WITH CALCIUM; CHLORIDE AND OLIGOSACCHARIDE INHIBITOR, COFACTOR, DISULFIDE BOND. - Ref.15"Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology."
Desmyter A., Spinelli S., Payan F., Lauwereys M., Wyns L., Muyldermans S., Cambillau C.
J. Biol. Chem. 277:23645-23650(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR.
Manual assertion based on experiment ini
- Ref.6"Three dimensional structure of porcine pancreatic alpha-amylase at 2.9-A resolution. Role of calcium in structure and activity."
Buisson G., Duee E., Haser R., Payan F.
EMBO J. 6:3909-3916(1987) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), COFACTOR, DISULFIDE BONDS. - Ref.9"The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat."
Wiegand G., Epp O., Huber R.
J. Mol. Biol. 247:99-110(1995) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 16-511 IN COMPLEX WITH INHIBITOR; CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.10"Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics."
Machius M., Vertesy L., Huber R., Wiegand G.
J. Mol. Biol. 260:409-421(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM; GLUCOSE AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.13"Structure of a pancreatic alpha-amylase bound to a substrate analogue at 2.03-A resolution."
Qian M., Spinelli S., Driguez H., Payan F.
Protein Sci. 6:2285-2296(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR. - Ref.14"Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex."
Qian M., Nahoum V., Bonicel J., Bischoff H., Henrissat B., Payan F.
Biochemistry 40:7700-7709(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) IN COMPLEX WITH CALCIUM; CHLORIDE AND OLIGOSACCHARIDE INHIBITOR, COFACTOR, DISULFIDE BOND. - Ref.15"Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology."
Desmyter A., Spinelli S., Payan F., Lauwereys M., Wyns L., Muyldermans S., Cambillau C.
J. Biol. Chem. 277:23645-23650(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 16-511 IN COMPLEX WITH CALCIUM AND CHLORIDE, DISULFIDE BONDS, COFACTOR.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi | 115 | Calcium8 Publications Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 173 | Calcium; via carbonyl oxygen8 Publications Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 182 | Calcium8 Publications Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 210 | Chloride5 Publications Manual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei | 212 | Nucleophile | 1 | |
Metal bindingi | 216 | Calcium; via carbonyl oxygen8 Publications Manual assertion based on experiment ini
| 1 | |
Active sitei | 248 | Proton donor | 1 | |
Binding sitei | 313 | ChlorideCurated | 1 | |
<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>Sitei | 315 | Transition state stabilizerBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
Binding sitei | 352 | Chloride5 Publications Manual assertion based on experiment ini
| 1 |
<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
- alpha-amylase activity Source: UniProtKB
- alpha-amylase activity (releasing maltohexaose) Source: UniProtKB-EC
- calcium ion binding Source: UniProtKB
- chloride ion binding Source: UniProtKB
GO - Biological processi
- carbohydrate catabolic process Source: UniProtKB
<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 function | Glycosidase, Hydrolase |
Biological process | Carbohydrate metabolism |
Ligand | Calcium, Chloride, Metal-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.2.1.1, 6170 |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P00690 |
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%5Fand%5Ftaxonomy%5Fsection">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: Pancreatic alpha-amylase (EC:3.2.1.1
Manual assertion inferred from sequence similarity toi )Short name: PA Alternative name(s): 1,4-alpha-D-glucan glucanohydrolase |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:AMY2 |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>Organismi | Sus scrofa (Pig) |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri | 9823 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Laurasiatheria › Artiodactyla › Suina › Suidae › Sus |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
<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
Extracellular region or secreted
Extracellular region or secreted
- extracellular space Source: UniProtKB
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
Protein family/group databases
Allergome; a platform for allergen knowledge More...Allergomei | 970, Sus s Amylase |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL5730 |
DrugCentral More...DrugCentrali | P00690 |
<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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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 peptidei | 1 – 15 | 1 Publication Manual assertion based on experiment ini
| 15 | |
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000001399 | 16 – 511 | Pancreatic alpha-amylaseAdd BLAST | 496 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 16 | Pyrrolidone carboxylic acidBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 43 ↔ 101 | 1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| ||
Disulfide bondi | 85 ↔ 130 | 1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| ||
Disulfide bondi | 156 ↔ 175 | 1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| ||
Disulfide bondi | 393 ↔ 399 | 1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| ||
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 427 | N-linked (GlcNAc...) asparagine | 1 | |
Disulfide bondi | 465 ↔ 477 | 1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
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Keywords - PTMi
Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acidProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P00690 |
PeptideAtlas More...PeptideAtlasi | P00690 |
<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Binds to the sea anemone inhibitor helianthamide and magnificamide.
1 PublicationManual assertion inferred by curator fromi
- Ref.4"Magnificamide, a beta-defensin-like peptide from the mucus of the sea anemone Heteractis magnifica, is a strong inhibitor of mammalian alpha-amylases."
Sintsova O., Gladkikh I., Kalinovskii A., Zelepuga E., Monastyrnaya M., Kim N., Shevchenko L., Peigneur S., Tytgat J., Kozlovskaya E., Leychenko E.
Mar. Drugs 17:0-0(2019) [PubMed] [Europe PMC] [Abstract]Cited for: SUBUNIT, INTERACTION WITH THE SEA ANEMONE INHIBITOR MAGNIFICAMIDE.
Manual assertion based on experiment ini
- Ref.16"Potent human alpha-amylase inhibition by the beta-defensin-like protein helianthamide."
Tysoe C., Williams L.K., Keyzers R., Nguyen N.T., Tarling C., Wicki J., Goddard-Borger E.D., Aguda A.H., Perry S., Foster L.J., Andersen R.J., Brayer G.D., Withers S.G.
ACS Cent. Sci. 2:154-161(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH THE SEA ANEMONE INHIBITOR HELIANTHAMIDE, SUBUNIT, INTERACTION WITH THE SEA ANEMONE INHIBITOR HELIANTHAMIDE.
Protein-protein interaction databases
Molecular INTeraction database More...MINTi | P00690 |
STRING: functional protein association networks More...STRINGi | 9823.ENSSSCP00000007308 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P00690 |
<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
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 27 – 31 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 36 – 45 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 46 – 51 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 54 – 57 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 67 – 70 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 73 – 77 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 78 – 80 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 84 – 86 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 91 – 103 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
Beta strandi | 107 – 112 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 115 – 119 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 124 – 126 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 128 – 130 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 136 – 138 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 142 – 145 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 148 – 150 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 153 – 155 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 158 – 162 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 169 – 174 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 175 – 177 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 180 – 183 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 188 – 204 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 17 | |
Beta strandi | 208 – 211 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 214 – 216 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 219 – 226 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Turni | 234 – 236 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 244 – 247 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 253 – 257 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 259 – 262 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 263 – 265 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 266 – 269 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 272 – 281 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
Helixi | 289 – 294 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 297 – 299 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 304 – 306 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 307 – 309 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 316 – 318 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 319 – 321 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 324 – 326 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 330 – 332 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 333 – 345 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
Beta strandi | 348 – 355 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 363 – 366 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 369 – 372 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 375 – 378 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 400 – 402 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 404 – 415 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
Turni | 416 – 418 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 421 – 426 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 428 – 436 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
Turni | 437 – 439 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 440 – 445 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 447 – 449 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 451 – 456 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 461 – 465 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Turni | 467 – 469 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 476 – 479 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 481 – 484 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 488 – 494 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
Beta strandi | 498 – 500 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 502 – 506 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 507 – 509 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P00690 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P00690 |
<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
Keywords - Domaini
SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2212, Eukaryota |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P00690 |
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 IPR006048, A-amylase/branching_C IPR031319, A-amylase_C IPR006046, Alpha_amylase 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 PF02806, Alpha-amylase_C, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00110, ALPHAAMYLASE |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00642, Aamy, 1 hit SM00632, Aamy_C, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.
10 20 30 40 50
MKLFLLLSAF GFCWAQYAPQ TQSGRTSIVH LFEWRWVDIA LECERYLGPK
60 70 80 90 100
GFGGVQVSPP NENIVVTNPS RPWWERYQPV SYKLCTRSGN ENEFRDMVTR
110 120 130 140 150
CNNVGVRIYV DAVINHMCGS GAAAGTGTTC GSYCNPGNRE FPAVPYSAWD
160 170 180 190 200
FNDGKCKTAS GGIESYNDPY QVRDCQLVGL LDLALEKDYV RSMIADYLNK
210 220 230 240 250
LIDIGVAGFR IDASKHMWPG DIKAVLDKLH NLNTNWFPAG SRPFIFQEVI
260 270 280 290 300
DLGGEAIQSS EYFGNGRVTE FKYGAKLGTV VRKWSGEKMS YLKNWGEGWG
310 320 330 340 350
FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKVAV GFMLAHPYGF
360 370 380 390 400
TRVMSSYRWA RNFVNGQDVN DWIGPPNNNG VIKEVTINAD TTCGNDWVCE
410 420 430 440 450
HRWRQIRNMV WFRNVVDGQP FANWWANGSN QVAFGRGNRG FIVFNNDDWQ
460 470 480 490 500
LSSTLQTGLP GGTYCDVISG DKVGNSCTGI KVYVSSDGTA QFSISNSAED
510
PFIAIHAESK L
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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 conflicti | 138 | N → S AA sequence (PubMed:3484639).Curated | 1 | |
Sequence conflicti | 367 | Q → E AA sequence (PubMed:3484639).Curated | 1 | |
Sequence conflicti | 405 | Q → E AA sequence (PubMed:3484639).Curated | 1 | |
Sequence conflicti | 419 | Q → E AA sequence (PubMed:3484639).Curated | 1 | |
Sequence conflicti | 426 | A → D AA sequence (PubMed:3484639).Curated | 1 |
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF064742 mRNA Translation: AAF02828.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A25412, ALPGP |
NCBI Reference Sequences More...RefSeqi | NP_999360.1, NM_214195.1 |
Genome annotation databases
Database of genes from NCBI RefSeq genomes More...GeneIDi | 397397 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ssc:397397 |
<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
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P00690 | Alpha-amylase (Fragment) | 257 | UniRef100_P00690 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P00690 | Alpha-amylase (Fragment) | 257 | UniRef90_P00690 | |||
Uncharacterized protein | 511 | |||||
Alpha-amylase | 496 | |||||
Alpha-amylase | 511 | |||||
Alpha-amylase | 511 | |||||
+33 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P00690 | Pancreatic alpha-amylase | 508 | UniRef50_P00690 | |||
Alpha-amylase | ) | 512 | ||||
Alpha-amylase (Fragment) | 257 | |||||
Uncharacterized protein | 511 | |||||
Alpha-amylase | 496 | |||||
+1403 |
<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
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
Worthington enzyme manual |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF064742 mRNA Translation: AAF02828.1 |
PIRi | A25412, ALPGP |
RefSeqi | NP_999360.1, NM_214195.1 |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BVN | X-ray | 2.50 | P | 16-511 | [»] | |
1DHK | X-ray | 1.85 | A | 17-511 | [»] | |
1HX0 | X-ray | 1.38 | A | 16-511 | [»] | |
1JFH | X-ray | 2.03 | A | 17-511 | [»] | |
1KXQ | X-ray | 1.60 | A/B/C/D | 16-511 | [»] | |
1KXT | X-ray | 2.00 | A/C/E | 16-511 | [»] | |
1KXV | X-ray | 1.60 | A/B | 16-511 | [»] | |
1OSE | X-ray | 2.30 | A | 17-511 | [»] | |
1PIF | X-ray | 2.30 | A | 17-511 | [»] | |
1PIG | X-ray | 2.20 | A | 17-511 | [»] | |
1PPI | X-ray | 2.20 | A | 16-511 | [»] | |
1UA3 | X-ray | 2.01 | A | 16-511 | [»] | |
1VAH | X-ray | 2.40 | A | 16-511 | [»] | |
1WO2 | X-ray | 2.01 | A | 16-511 | [»] | |
3L2L | X-ray | 2.11 | A | 16-511 | [»] | |
3L2M | X-ray | 1.97 | A | 16-511 | [»] | |
4X0N | X-ray | 2.60 | A | 17-511 | [»] | |
SMRi | P00690 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
MINTi | P00690 |
STRINGi | 9823.ENSSSCP00000007308 |
Chemistry databases
BindingDBi | P00690 |
ChEMBLi | CHEMBL5730 |
DrugCentrali | P00690 |
Protein family/group databases
Allergomei | 970, Sus s Amylase |
CAZyi | GH13, Glycoside Hydrolase Family 13 |
Proteomic databases
PaxDbi | P00690 |
PeptideAtlasi | P00690 |
Protocols and materials databases
ABCD curated depository of sequenced antibodies More...ABCDi | P00690, 3 sequenced antibodies |
Genome annotation databases
GeneIDi | 397397 |
KEGGi | ssc:397397 |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 397397 |
Phylogenomic databases
eggNOGi | KOG2212, Eukaryota |
InParanoidi | P00690 |
Enzyme and pathway databases
BRENDAi | 3.2.1.1, 6170 |
SABIO-RKi | P00690 |
Miscellaneous databases
EvolutionaryTracei | P00690 |
Protein Ontology More...PROi | PR:P00690 |
Family and domain databases
Gene3Di | 2.60.40.1180, 1 hit |
InterProi | View protein in InterPro IPR006048, A-amylase/branching_C IPR031319, A-amylase_C IPR006046, Alpha_amylase IPR006047, Glyco_hydro_13_cat_dom IPR013780, Glyco_hydro_b IPR017853, Glycoside_hydrolase_SF |
Pfami | View protein in Pfam PF00128, Alpha-amylase, 1 hit PF02806, Alpha-amylase_C, 1 hit |
PRINTSi | PR00110, ALPHAAMYLASE |
SMARTi | View protein in SMART SM00642, Aamy, 1 hit SM00632, Aamy_C, 1 hit |
SUPFAMi | SSF51445, SSF51445, 1 hit |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | 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 namei | AMYP_PIG | |
<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>Accessioni | P00690Primary (citable) accession number: P00690 Secondary accession number(s): Q9TUE4 | |
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | August 15, 2003 | |
Last modified: | February 23, 2022 | |
This is version 176 of the entry and version 3 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata 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, Reference proteomeDocuments
- Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families