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P00690

- AMYP_PIG

UniProt

P00690 - AMYP_PIG

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Protein
Pancreatic alpha-amylase
Gene
AMY2
Organism
Sus scrofa (Pig)
Status
Reviewed - 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

Binds 1 calcium ion per subunit.
Binds 1 chloride 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 stabilizer By 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
Complete GO annotation...

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 Publication
Add
BLAST
Chaini16 – 511496Pancreatic alpha-amylase
PRO_0000001399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Pyrrolidone carboxylic acid
Disulfide bondi43 ↔ 1012 Publications
Disulfide bondi85 ↔ 1302 Publications
Disulfide bondi156 ↔ 1752 Publications
Disulfide bondi393 ↔ 3992 Publications
Glycosylationi427 – 4271N-linked (GlcNAc...)
Disulfide bondi465 ↔ 4772 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiP00690.

Interactioni

Protein-protein interaction databases

MINTiMINT-1510713.
STRINGi9823.ENSSSCP00000007308.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP00690.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0366.
HOGENOMiHOG000253313.
HOVERGENiHBG000061.
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

MKLFLLLSAF GFCWAQYAPQ TQSGRTSIVH LFEWRWVDIA LECERYLGPK    50
GFGGVQVSPP NENIVVTNPS RPWWERYQPV SYKLCTRSGN ENEFRDMVTR 100
CNNVGVRIYV DAVINHMCGS GAAAGTGTTC GSYCNPGNRE FPAVPYSAWD 150
FNDGKCKTAS GGIESYNDPY QVRDCQLVGL LDLALEKDYV RSMIADYLNK 200
LIDIGVAGFR IDASKHMWPG DIKAVLDKLH NLNTNWFPAG SRPFIFQEVI 250
DLGGEAIQSS EYFGNGRVTE FKYGAKLGTV VRKWSGEKMS YLKNWGEGWG 300
FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKVAV GFMLAHPYGF 350
TRVMSSYRWA RNFVNGQDVN DWIGPPNNNG VIKEVTINAD TTCGNDWVCE 400
HRWRQIRNMV WFRNVVDGQP FANWWANGSN QVAFGRGNRG FIVFNNDDWQ 450
LSSTLQTGLP GGTYCDVISG DKVGNSCTGI KVYVSSDGTA QFSISNSAED 500
PFIAIHAESK L 511
Length:511
Mass (Da):57,086
Last modified:August 15, 2003 - v3
Checksum:i117489E020807378
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381N → S AA sequence 1 Publication
Sequence conflicti367 – 3671Q → E AA sequence 1 Publication
Sequence conflicti405 – 4051Q → E AA sequence 1 Publication
Sequence conflicti419 – 4191Q → E AA sequence 1 Publication
Sequence conflicti426 – 4261A → D AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF064742 mRNA. Translation: AAF02828.1 .
PIRi A25412. ALPGP.
RefSeqi NP_999360.1. NM_214195.1.
UniGenei Ssc.94418.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P00690.
SMRi P00690. Positions 16-511.
ModBasei Search...

Protein-protein interaction databases

MINTi MINT-1510713.
STRINGi 9823.ENSSSCP00000007308.

Chemistry

ChEMBLi CHEMBL5730.

Protein family/group databases

Allergomei 970. Sus s Amylase.
CAZyi GH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEi P00690.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 397397.
KEGGi ssc:397397.

Organism-specific databases

CTDi 397397.

Phylogenomic databases

eggNOGi COG0366.
HOGENOMi HOG000253313.
HOVERGENi HBG000061.
KOi K01176.

Enzyme and pathway databases

SABIO-RK P00690.

Miscellaneous databases

EvolutionaryTracei P00690.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR006048. 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 ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view ]
PRINTSi PR00110. ALPHAAMYLASE.
SMARTi SM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

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: July 9, 2014
This is version 133 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 1 Publication, 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