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P00690 (AMYP_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pancreatic alpha-amylase

Short name=PA
EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:AMY2
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

Cofactor

Binds 1 calcium ion per subunit.

Binds 1 chloride ion per subunit.

Subcellular location

Secretedextracellular space.

Miscellaneous

The two forms of this enzyme, I and II, show very similar activities, molecular masses, and compositions and differ only in their isoelectric points. As no evidence for two variants were in the cDNA library of Ref.1, it is most likely that isoform I(PPAI) and isoform II(PPAII) are two forms of the same protein.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Ref.2
Chain16 – 511496Pancreatic alpha-amylase
PRO_0000001399

Sites

Active site2121Nucleophile
Active site2481Proton donor
Metal binding1151Calcium
Metal binding1731Calcium; via carbonyl oxygen
Metal binding1821Calcium
Metal binding2161Calcium; via carbonyl oxygen
Binding site2101Chloride
Binding site3131Chloride
Binding site3521Chloride
Site3151Transition state stabilizer By similarity

Amino acid modifications

Modified residue161Pyrrolidone carboxylic acid
Glycosylation4271N-linked (GlcNAc...)
Disulfide bond43 ↔ 101 Ref.2 Ref.3
Disulfide bond85 ↔ 130 Ref.2 Ref.3
Disulfide bond156 ↔ 175 Ref.2 Ref.3
Disulfide bond393 ↔ 399 Ref.2 Ref.3
Disulfide bond465 ↔ 477 Ref.2 Ref.3

Experimental info

Sequence conflict1381N → S AA sequence Ref.2
Sequence conflict3671Q → E AA sequence Ref.2
Sequence conflict4051Q → E AA sequence Ref.2
Sequence conflict4191Q → E AA sequence Ref.2
Sequence conflict4261A → D AA sequence Ref.2

Secondary structure

................................................................................................................. 511
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00690 [UniParc].

Last modified August 15, 2003. Version 3.
Checksum: 117489E020807378

FASTA51157,086
        10         20         30         40         50         60 
MKLFLLLSAF GFCWAQYAPQ TQSGRTSIVH LFEWRWVDIA LECERYLGPK GFGGVQVSPP 

        70         80         90        100        110        120 
NENIVVTNPS RPWWERYQPV SYKLCTRSGN ENEFRDMVTR CNNVGVRIYV DAVINHMCGS 

       130        140        150        160        170        180 
GAAAGTGTTC GSYCNPGNRE FPAVPYSAWD FNDGKCKTAS GGIESYNDPY QVRDCQLVGL 

       190        200        210        220        230        240 
LDLALEKDYV RSMIADYLNK LIDIGVAGFR IDASKHMWPG DIKAVLDKLH NLNTNWFPAG 

       250        260        270        280        290        300 
SRPFIFQEVI DLGGEAIQSS EYFGNGRVTE FKYGAKLGTV VRKWSGEKMS YLKNWGEGWG 

       310        320        330        340        350        360 
FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKVAV GFMLAHPYGF TRVMSSYRWA 

       370        380        390        400        410        420 
RNFVNGQDVN DWIGPPNNNG VIKEVTINAD TTCGNDWVCE HRWRQIRNMV WFRNVVDGQP 

       430        440        450        460        470        480 
FANWWANGSN QVAFGRGNRG FIVFNNDDWQ LSSTLQTGLP GGTYCDVISG DKVGNSCTGI 

       490        500        510 
KVYVSSDGTA QFSISNSAED PFIAIHAESK L 

« Hide

References

[1]"Molecular cloning and primary structure analysis of porcine pancreatic alpha-amylase."
Darnis S., Juge N., Guo X.-J., Marchis-Mouren G., Puigserver A., Chaix J.-C.
Biochim. Biophys. Acta 1430:281-289(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[2]"Complete amino acid sequence and location of the five disulfide bridges in porcine pancreatic alpha-amylase."
Pasero L., Mazzei-Pierron Y., Abadie B., Chicheportiche Y., Marchis-Mouren G.
Biochim. Biophys. Acta 869:147-157(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-511, DISULFIDE BONDS.
[3]"Localization of the two free thiol groups in the porcine pancreatic alpha-amylase I sequence."
Pasero L., Mazzei Y., Abadie B., Moinier D., Fougereau M., Marchis-Mouren G.
Biochem. Biophys. Res. Commun. 110:726-732(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[4]"The three-dimensional structure of alpha-amylase from porcine pancreas at 5-A resolution -- the active-site location."
Payan F., Haser R., Pierrot M., Frey M., Astier J.-P., Abadie B., Duee E., Buisson G.
Acta Crystallogr. B 36:416-421(1980)
Cited for: X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS).
[5]"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).
[6]"Structure and molecular model refinement of pig pancreatic alpha-amylase at 2.1-A resolution."
Qian M., Haser R., Payan F.
J. Mol. Biol. 231:785-799(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SEQUENCE REVISION.
[7]"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 (2.2 ANGSTROMS).
[8]"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 (2.5 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
[9]"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 (2.3 ANGSTROMS).
[10]"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 (2.3 ANGSTROMS), SEQUENCE REVISION.
[11]"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 COMPLEX WITH INHIBITOR.
[12]"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).
[13]"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 AN OLIGOSACCHARIDE INHIBITOR.
[14]"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 (1.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF064742 mRNA. Translation: AAF02828.1.
PIRALPGP. A25412.
RefSeqNP_999360.1. NM_214195.1.
UniGeneSsc.94418.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BVNX-ray2.50P16-511[»]
1DHKX-ray1.85A17-511[»]
1HX0X-ray1.38A16-511[»]
1JFHX-ray2.03A17-511[»]
1KXQX-ray1.60A/B/C/D16-511[»]
1KXTX-ray2.00A/C/E16-511[»]
1KXVX-ray1.60A/B16-511[»]
1OSEX-ray2.30A17-511[»]
1PIFX-ray2.30A17-511[»]
1PIGX-ray2.20A17-511[»]
1PPIX-ray2.20A16-511[»]
1UA3X-ray2.01A16-511[»]
1VAHX-ray2.40A16-511[»]
1WO2X-ray2.01A16-511[»]
3L2LX-ray2.11A16-511[»]
3L2MX-ray1.97A16-511[»]
ProteinModelPortalP00690.
SMRP00690. Positions 16-511.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1510713.
STRING9823.ENSSSCP00000007308.

Chemistry

ChEMBLCHEMBL5730.

Protein family/group databases

Allergome970. Sus s Amylase.
CAZyGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEP00690.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397397.
KEGGssc:397397.

Organism-specific databases

CTD397397.

Phylogenomic databases

eggNOGCOG0366.
HOGENOMHOG000253313.
HOVERGENHBG000061.
KOK01176.

Enzyme and pathway databases

SABIO-RKP00690.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006048. A-amylase_b_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP00690.

Entry information

Entry nameAMYP_PIG
AccessionPrimary (citable) accession number: P00690
Secondary accession number(s): Q9TUE4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 15, 2003
Last modified: July 9, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries