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Protein

Pancreatic alpha-amylase

Gene

AMY2

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 1 Ca2+ ion per subunit.
  • chlorideNote: Binds 1 Cl(-) ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi115 – 1151Calcium
Metal bindingi173 – 1731Calcium; via carbonyl oxygen
Metal bindingi182 – 1821Calcium
Binding sitei210 – 2101Chloride
Active sitei212 – 2121Nucleophile
Metal bindingi216 – 2161Calcium; via carbonyl oxygen
Active sitei248 – 2481Proton donor
Binding sitei313 – 3131Chloride
Sitei315 – 3151Transition state stabilizerBy similarity
Binding sitei352 – 3521Chloride

GO - Molecular functioni

  1. alpha-amylase activity Source: UniProtKB
  2. calcium ion binding Source: UniProtKB
  3. chloride ion binding Source: UniProtKB

GO - Biological processi

  1. carbohydrate catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Chloride, Metal-binding

Enzyme and pathway databases

SABIO-RKP00690.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Pancreatic alpha-amylase (EC:3.2.1.1)
Short name:
PA
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene namesi
Name:AMY2
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei970. Sus s Amylase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 15151 PublicationAdd
BLAST
Chaini16 – 511496Pancreatic alpha-amylasePRO_0000001399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Pyrrolidone carboxylic acid
Disulfide bondi43 ↔ 101
Disulfide bondi85 ↔ 130
Disulfide bondi156 ↔ 175
Disulfide bondi393 ↔ 399
Glycosylationi427 – 4271N-linked (GlcNAc...)
Disulfide bondi465 ↔ 477

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiP00690.

Interactioni

Protein-protein interaction databases

MINTiMINT-1510713.
STRINGi9823.ENSSSCP00000007308.

Structurei

Secondary structure

1
511
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 315Combined sources
Helixi36 – 4510Combined sources
Turni46 – 516Combined sources
Beta strandi54 – 574Combined sources
Turni67 – 704Combined sources
Helixi73 – 775Combined sources
Beta strandi78 – 803Combined sources
Beta strandi84 – 863Combined sources
Helixi91 – 10313Combined sources
Beta strandi107 – 1126Combined sources
Beta strandi115 – 1195Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi128 – 1303Combined sources
Helixi136 – 1383Combined sources
Turni142 – 1454Combined sources
Helixi148 – 1503Combined sources
Turni153 – 1553Combined sources
Beta strandi158 – 1625Combined sources
Helixi169 – 1746Combined sources
Beta strandi175 – 1773Combined sources
Beta strandi180 – 1834Combined sources
Helixi188 – 20417Combined sources
Beta strandi208 – 2114Combined sources
Helixi214 – 2163Combined sources
Helixi219 – 2268Combined sources
Turni234 – 2363Combined sources
Beta strandi244 – 2474Combined sources
Beta strandi253 – 2575Combined sources
Helixi259 – 2624Combined sources
Turni263 – 2653Combined sources
Beta strandi266 – 2694Combined sources
Helixi272 – 28110Combined sources
Helixi289 – 2946Combined sources
Helixi297 – 2993Combined sources
Helixi304 – 3063Combined sources
Beta strandi307 – 3093Combined sources
Helixi316 – 3183Combined sources
Beta strandi319 – 3213Combined sources
Helixi324 – 3263Combined sources
Helixi330 – 3323Combined sources
Helixi333 – 34513Combined sources
Beta strandi348 – 3558Combined sources
Beta strandi363 – 3664Combined sources
Turni369 – 3724Combined sources
Beta strandi375 – 3784Combined sources
Helixi400 – 4023Combined sources
Helixi404 – 41512Combined sources
Turni416 – 4183Combined sources
Beta strandi421 – 4266Combined sources
Beta strandi428 – 4369Combined sources
Turni437 – 4393Combined sources
Beta strandi440 – 4456Combined sources
Beta strandi447 – 4493Combined sources
Beta strandi451 – 4566Combined sources
Beta strandi461 – 4655Combined sources
Turni467 – 4693Combined sources
Beta strandi476 – 4794Combined sources
Beta strandi481 – 4844Combined sources
Beta strandi488 – 4947Combined sources
Beta strandi498 – 5003Combined sources
Beta strandi502 – 5065Combined sources
Helixi507 – 5093Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00690.
SMRiP00690. Positions 16-511.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00690.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0366.
HOGENOMiHOG000253313.
HOVERGENiHBG000061.
InParanoidiP00690.
KOiK01176.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P00690-1 [UniParc]FASTAAdd to Basket

« Hide

        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
Length:511
Mass (Da):57,086
Last modified:August 15, 2003 - v3
Checksum:i117489E020807378
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381N → S AA sequence (PubMed:3484639)Curated
Sequence conflicti367 – 3671Q → E AA sequence (PubMed:3484639)Curated
Sequence conflicti405 – 4051Q → E AA sequence (PubMed:3484639)Curated
Sequence conflicti419 – 4191Q → E AA sequence (PubMed:3484639)Curated
Sequence conflicti426 – 4261A → D AA sequence (PubMed:3484639)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064742 mRNA. Translation: AAF02828.1.
PIRiA25412. ALPGP.
RefSeqiNP_999360.1. NM_214195.1.
UniGeneiSsc.94418.

Genome annotation databases

GeneIDi397397.
KEGGissc:397397.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064742 mRNA. Translation: AAF02828.1.
PIRiA25412. ALPGP.
RefSeqiNP_999360.1. NM_214195.1.
UniGeneiSsc.94418.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00690.
SMRiP00690. Positions 16-511.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1510713.
STRINGi9823.ENSSSCP00000007308.

Chemistry

BindingDBiP00690.
ChEMBLiCHEMBL5730.

Protein family/group databases

Allergomei970. Sus s Amylase.
CAZyiGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEiP00690.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397397.
KEGGissc:397397.

Organism-specific databases

CTDi397397.

Phylogenomic databases

eggNOGiCOG0366.
HOGENOMiHOG000253313.
HOVERGENiHBG000061.
InParanoidiP00690.
KOiK01176.

Enzyme and pathway databases

SABIO-RKP00690.

Miscellaneous databases

EvolutionaryTraceiP00690.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  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).

Entry informationi

Entry nameiAMYP_PIG
AccessioniPrimary (citable) accession number: P00690
Secondary accession number(s): Q9TUE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 15, 2003
Last modified: January 7, 2015
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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 PubMed:10082956, it is most likely that isoform I (PPAI) and isoform II (PPAII) are two forms of the same protein.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.