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P00690

- AMYP_PIG

UniProt

P00690 - AMYP_PIG

Protein

Pancreatic alpha-amylase

Gene

AMY2

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 3 (15 Aug 2003)
      Previous versions | rss
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    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 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

    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

    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 – 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.
    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.
    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

    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:
    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...
    MobiDBi 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: October 1, 2014
    This is version 134 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