P00690 (AMYP_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Sus scrofa (Pig) [Complete proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular 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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Chloride Metal-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate catabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	extracellular space Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	alpha-amylase activity Inferred from sequence or structural similarity. Source: UniProtKB calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB chloride ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 15

15

Ref.2

Chain

16 – 511

496

Pancreatic alpha-amylase

PRO_0000001399

Sites

Active site

212

1

Nucleophile

Active site

248

1

Proton donor

Metal binding

115

1

Calcium

Metal binding

173

1

Calcium; via carbonyl oxygen

Metal binding

182

1

Calcium

Metal binding

216

1

Calcium; via carbonyl oxygen

Binding site

210

1

Chloride

Binding site

313

1

Chloride

Binding site

352

1

Chloride

Site

315

1

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

16

1

Pyrrolidone carboxylic acid

Glycosylation

427

1

N-linked (GlcNAc...)

Disulfide bond

43 ↔ 101

Ref.2 Ref.3

Disulfide bond

85 ↔ 130

Ref.2 Ref.3

Disulfide bond

156 ↔ 175

Ref.2 Ref.3

Disulfide bond

393 ↔ 399

Ref.2 Ref.3

Disulfide bond

465 ↔ 477

Ref.2 Ref.3

Experimental info

Sequence conflict

138

1

N → S AA sequence Ref.2

Sequence conflict

367

1

Q → E AA sequence Ref.2

Sequence conflict

405

1

Q → E AA sequence Ref.2

Sequence conflict

419

1

Q → E AA sequence Ref.2

Sequence conflict

426

1

A → D AA sequence Ref.2

Secondary structure

1

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511

Helix Strand Turn

Details...

Beta strand

27 – 31

5

Helix

36 – 45

10

Turn

46 – 51

6

Beta strand

54 – 57

4

Turn

67 – 70

4

Helix

73 – 77

5

Beta strand

78 – 80

3

Helix

91 – 103

13

Beta strand

107 – 112

6

Beta strand

115 – 119

5

Beta strand

128 – 130

3

Helix

136 – 138

3

Turn

142 – 145

4

Helix

148 – 150

3

Turn

153 – 155

3

Helix

169 – 174

6

Beta strand

175 – 177

3

Beta strand

180 – 183

4

Helix

188 – 204

17

Beta strand

208 – 211

4

Helix

214 – 216

3

Helix

219 – 226

8

Turn

234 – 236

3

Beta strand

244 – 247

4

Beta strand

253 – 257

5

Helix

259 – 262

4

Turn

263 – 265

3

Beta strand

266 – 269

4

Helix

272 – 281

10

Helix

289 – 294

6

Helix

297 – 299

3

Helix

304 – 306

3

Beta strand

307 – 309

3

Helix

316 – 318

3

Helix

324 – 326

3

Helix

330 – 332

3

Helix

333 – 345

13

Beta strand

348 – 355

8

Turn

369 – 372

4

Beta strand

375 – 378

4

Helix

400 – 402

3

Helix

404 – 415

12

Turn

416 – 418

3

Beta strand

421 – 426

6

Beta strand

428 – 436

9

Turn

437 – 439

3

Beta strand

440 – 445

6

Beta strand

447 – 449

3

Beta strand

451 – 456

6

Beta strand

461 – 465

5

Turn

467 – 469

3

Beta strand

476 – 479

4

Beta strand

481 – 484

4

Beta strand

488 – 494

7

Beta strand

502 – 506

5

Helix

507 – 509

3

Sequences

	Sequence		Length	Mass (Da)
	P00690 [UniParc]. Last modified August 15, 2003. Version 3. Checksum: 117489E020807378	FASTA	511	57,086
	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

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: 10082956] [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: 3484639] [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: 6188459] [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: 3502087] [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: 8515451] [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: 8193143] [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: 7897663] [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: 8757803] [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: 8681972] [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: 8994970] [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: 9385631] [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: 11412124] [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: 11960990] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF064742 mRNA. Translation: AAF02828.1.

PIR

ALPGP. A25412.

RefSeq

NP_999360.1. NM_214195.1.

UniGene

Ssc.94418.

3D structure databases

PDBe
RCSB PDB
PDBj

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	17-511	[»]
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	16-496	[»]
1VAH	X-ray	2.40	A	16-511	[»]
1WO2	X-ray	2.01	A	17-511	[»]
3L2L	X-ray	2.11	A	17-511	[»]
3L2M	X-ray	1.97	A	17-511	[»]

ProteinModelPortal

P00690.

SMR

P00690. Positions 16-511.

ModBase

Search...

Protein-protein interaction databases

STRING

P00690.

Protein family/group databases

Allergome

970. Sus s Amylase.

CAZy

GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

397397.

KEGG

ssc:397397.

Organism-specific databases

CTD

497039.

Phylogenomic databases

GeneTree

ENSGT00390000002882.

HOVERGEN

HBG000061.

OrthoDB

EOG4RV2R1.

Family and domain databases

InterPro

IPR006048. A-amylase_b_C.
IPR015902. Alpha_amylase.
IPR006046. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

KO

K01176.

PANTHER

PTHR10357. Alpha_amylase. 1 hit.

Pfam

PF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]

PRINTS

PR00110. ALPHAAMYLASE.

SMART

SM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Entry information

Entry name

AMYP_PIG

Accession

Primary (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:	December 14, 2011
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program