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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.By similarity

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi115Calcium8 Publications1
Metal bindingi173Calcium; via carbonyl oxygen8 Publications1
Metal bindingi182Calcium8 Publications1
Binding sitei210Chloride5 Publications1
Active sitei212Nucleophile1
Metal bindingi216Calcium; via carbonyl oxygen8 Publications1
Active sitei248Proton donor1
Binding sitei313ChlorideCurated1
Sitei315Transition state stabilizerBy similarity1
Binding sitei352Chloride5 Publications1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Chloride, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.1. 6170.
SABIO-RKP00690.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Pancreatic alpha-amylase (EC:3.2.1.1By similarity)
Short name:
PA
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene namesi
Name:AMY2
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei970. Sus s Amylase.

Chemistry databases

ChEMBLiCHEMBL5730.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 151 PublicationAdd BLAST15
ChainiPRO_000000139916 – 511Pancreatic alpha-amylaseAdd BLAST496

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei16Pyrrolidone carboxylic acid1
Disulfide bondi43 ↔ 1011 Publication8 Publications
Disulfide bondi85 ↔ 1301 Publication8 Publications
Disulfide bondi156 ↔ 1751 Publication8 Publications
Disulfide bondi393 ↔ 3991 Publication8 Publications
Glycosylationi427N-linked (GlcNAc...)1
Disulfide bondi465 ↔ 4771 Publication8 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP00690.
PeptideAtlasiP00690.
PRIDEiP00690.

Interactioni

Protein-protein interaction databases

MINTiMINT-1510713.
STRINGi9823.ENSSSCP00000026998.

Chemistry databases

BindingDBiP00690.

Structurei

Secondary structure

1511
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 31Combined sources5
Helixi36 – 45Combined sources10
Turni46 – 51Combined sources6
Beta strandi54 – 57Combined sources4
Turni67 – 70Combined sources4
Helixi73 – 77Combined sources5
Beta strandi78 – 80Combined sources3
Beta strandi84 – 86Combined sources3
Helixi91 – 103Combined sources13
Beta strandi107 – 112Combined sources6
Beta strandi115 – 119Combined sources5
Beta strandi124 – 126Combined sources3
Beta strandi128 – 130Combined sources3
Helixi136 – 138Combined sources3
Turni142 – 145Combined sources4
Helixi148 – 150Combined sources3
Turni153 – 155Combined sources3
Beta strandi158 – 162Combined sources5
Helixi169 – 174Combined sources6
Beta strandi175 – 177Combined sources3
Beta strandi180 – 183Combined sources4
Helixi188 – 204Combined sources17
Beta strandi208 – 211Combined sources4
Helixi214 – 216Combined sources3
Helixi219 – 226Combined sources8
Turni234 – 236Combined sources3
Beta strandi244 – 247Combined sources4
Beta strandi253 – 257Combined sources5
Helixi259 – 262Combined sources4
Turni263 – 265Combined sources3
Beta strandi266 – 269Combined sources4
Helixi272 – 281Combined sources10
Helixi289 – 294Combined sources6
Helixi297 – 299Combined sources3
Helixi304 – 306Combined sources3
Beta strandi307 – 309Combined sources3
Helixi316 – 318Combined sources3
Beta strandi319 – 321Combined sources3
Helixi324 – 326Combined sources3
Helixi330 – 332Combined sources3
Helixi333 – 345Combined sources13
Beta strandi348 – 355Combined sources8
Beta strandi363 – 366Combined sources4
Turni369 – 372Combined sources4
Beta strandi375 – 378Combined sources4
Helixi400 – 402Combined sources3
Helixi404 – 415Combined sources12
Turni416 – 418Combined sources3
Beta strandi421 – 426Combined sources6
Beta strandi428 – 436Combined sources9
Turni437 – 439Combined sources3
Beta strandi440 – 445Combined sources6
Beta strandi447 – 449Combined sources3
Beta strandi451 – 456Combined sources6
Beta strandi461 – 465Combined sources5
Turni467 – 469Combined sources3
Beta strandi476 – 479Combined sources4
Beta strandi481 – 484Combined sources4
Beta strandi488 – 494Combined sources7
Beta strandi498 – 500Combined sources3
Beta strandi502 – 506Combined sources5
Helixi507 – 509Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4X0NX-ray2.60A17-511[»]
ProteinModelPortaliP00690.
SMRiP00690.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00690.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2212. Eukaryota.
COG0366. LUCA.
HOGENOMiHOG000253313.
HOVERGENiHBG000061.
InParanoidiP00690.
KOiK01176.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
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)DescriptionActionsGraphical viewLength
Sequence conflicti138N → S AA sequence (PubMed:3484639).Curated1
Sequence conflicti367Q → E AA sequence (PubMed:3484639).Curated1
Sequence conflicti405Q → E AA sequence (PubMed:3484639).Curated1
Sequence conflicti419Q → E AA sequence (PubMed:3484639).Curated1
Sequence conflicti426A → D AA sequence (PubMed:3484639).Curated1

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
PDB 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[»]
4X0NX-ray2.60A17-511[»]
ProteinModelPortaliP00690.
SMRiP00690.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1510713.
STRINGi9823.ENSSSCP00000026998.

Chemistry databases

BindingDBiP00690.
ChEMBLiCHEMBL5730.

Protein family/group databases

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

Proteomic databases

PaxDbiP00690.
PeptideAtlasiP00690.
PRIDEiP00690.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397397.
KEGGissc:397397.

Organism-specific databases

CTDi397397.

Phylogenomic databases

eggNOGiKOG2212. Eukaryota.
COG0366. LUCA.
HOGENOMiHOG000253313.
HOVERGENiHBG000061.
InParanoidiP00690.
KOiK01176.

Enzyme and pathway databases

BRENDAi3.2.1.1. 6170.
SABIO-RKP00690.

Miscellaneous databases

EvolutionaryTraceiP00690.
PROiP00690.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
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...

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: November 2, 2016
This is version 153 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

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 one 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.