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P56634

- AMY_TENMO

UniProt

P56634 - AMY_TENMO

Protein

Alpha-amylase

Gene
N/A
Organism
Tenebrio molitor (Yellow mealworm beetle)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (15 Dec 1998)
      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 bindingi98 – 981Calcium
    Metal bindingi146 – 1461Calcium; via carbonyl oxygen
    Metal bindingi155 – 1551Calcium
    Binding sitei183 – 1831Chloride
    Active sitei185 – 1851Nucleophile
    Metal bindingi189 – 1891Calcium; via carbonyl oxygen
    Active sitei222 – 2221Proton donor
    Binding sitei285 – 2851Chloride
    Sitei287 – 2871Transition state stabilizerBy similarity
    Binding sitei321 – 3211Chloride

    GO - Molecular functioni

    1. alpha-amylase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Calcium, Chloride, Metal-binding

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-amylase (EC:3.2.1.1)
    Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase
    OrganismiTenebrio molitor (Yellow mealworm beetle)
    Taxonomic identifieri7067 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaColeopteraPolyphagaCucujiformiaTenebrionidaeTenebrio

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 471471Alpha-amylasePRO_0000054290Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11Pyrrolidone carboxylic acid1 Publication
    Disulfide bondi28 ↔ 84
    Disulfide bondi134 ↔ 148
    Disulfide bondi354 ↔ 360
    Disulfide bondi425 ↔ 437

    Keywords - PTMi

    Disulfide bond, Pyrrolidone carboxylic acid

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    MINTiMINT-88080.

    Structurei

    Secondary structure

    1
    471
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 166
    Helixi21 – 3010
    Turni31 – 366
    Beta strandi37 – 415
    Helixi56 – 605
    Beta strandi61 – 633
    Beta strandi67 – 693
    Helixi74 – 8613
    Beta strandi90 – 956
    Beta strandi105 – 1073
    Beta strandi112 – 1143
    Turni115 – 1184
    Turni121 – 1244
    Helixi127 – 1293
    Helixi142 – 1476
    Beta strandi148 – 1503
    Helixi161 – 17616
    Beta strandi181 – 1844
    Helixi187 – 1893
    Helixi192 – 2009
    Helixi207 – 2093
    Beta strandi218 – 2225
    Beta strandi227 – 2304
    Helixi233 – 2353
    Turni236 – 2383
    Beta strandi239 – 2435
    Helixi245 – 25511
    Turni256 – 2583
    Helixi261 – 2666
    Helixi269 – 2713
    Helixi276 – 2783
    Beta strandi279 – 2813
    Helixi288 – 2914
    Beta strandi292 – 2965
    Helixi302 – 31413
    Beta strandi317 – 3248
    Beta strandi329 – 3324
    Beta strandi335 – 3373
    Beta strandi338 – 3403
    Beta strandi347 – 3493
    Turni350 – 3523
    Beta strandi353 – 3553
    Helixi361 – 3633
    Helixi365 – 37612
    Turni377 – 3793
    Beta strandi382 – 3876
    Beta strandi389 – 3979
    Turni398 – 4003
    Beta strandi401 – 4099
    Beta strandi411 – 4166
    Beta strandi421 – 4255
    Turni427 – 4293
    Beta strandi436 – 4394
    Beta strandi441 – 4444
    Beta strandi448 – 4547
    Beta strandi461 – 4666
    Helixi467 – 4693

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CLVX-ray2.00A1-471[»]
    1JAEX-ray1.65A2-471[»]
    1TMQX-ray2.50A1-471[»]
    1VIWX-ray3.00A2-471[»]
    ProteinModelPortaliP56634.
    SMRiP56634. Positions 1-471.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56634.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    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.

    P56634-1 [UniParc]FASTAAdd to Basket

    « Hide

    QKDANFASGR NSIVHLFEWK WNDIADECER FLQPQGFGGV QISPPNEYLV    50
    ADGRPWWERY QPVSYIINTR SGDESAFTDM TRRCNDAGVR IYVDAVINHM 100
    TGMNGVGTSG SSADHDGMNY PAVPYGSGDF HSPCEVNNYQ DADNVRNCEL 150
    VGLRDLNQGS DYVRGVLIDY MNHMIDLGVA GFRVDAAKHM SPGDLSVIFS 200
    GLKNLNTDYG FADGARPFIY QEVIDLGGEA ISKNEYTGFG CVLEFQFGVS 250
    LGNAFQGGNQ LKNLANWGPE WGLLEGLDAV VFVDNHDNQR TGGSQILTYK 300
    NPKPYKMAIA FMLAHPYGTT RIMSSFDFTD NDQGPPQDGS GNLISPGIND 350
    DNTCSNGYVC EHRWRQVYGM VGFRNAVEGT QVENWWSNDD NQIAFSRGSQ 400
    GFVAFTNGGD LNQNLNTGLP AGTYCDVISG ELSGGSCTGK SVTVGDNGSA 450
    DISLGSAEDD GVLAIHVNAK L 471
    Length:471
    Mass (Da):51,240
    Last modified:December 15, 1998 - v1
    Checksum:i9C3D48933D6C24C8
    GO

    Sequence databases

    PIRiS75702.

    Cross-referencesi

    Sequence databases

    PIRi S75702.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CLV X-ray 2.00 A 1-471 [» ]
    1JAE X-ray 1.65 A 2-471 [» ]
    1TMQ X-ray 2.50 A 1-471 [» ]
    1VIW X-ray 3.00 A 2-471 [» ]
    ProteinModelPortali P56634.
    SMRi P56634. Positions 1-471.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-88080.

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P56634.

    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. "The alpha-amylase from the yellow meal worm: complete primary structure, crystallization and preliminary X-ray analysis."
      Strobl S., Gomis-Rueth F.-X., Maskos K., Frank G., Huber R., Glockshuber R.
      FEBS Lett. 409:109-114(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    2. "Crystal structure of yellow meal worm alpha-amylase at 1.64-A resolution."
      Strobl S., Maskos K., Betz M., Wiegand G., Huber R., Gomis-Rueth F.-X., Glockshuber R.
      J. Mol. Biol. 278:617-628(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
    3. "A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5-A resolution."
      Strobl S., Maskos K., Wiegand G., Huber R., Gomis-Rueth F.-X., Glockshuber R.
      Structure 6:911-921(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    4. "Specific inhibition of insect alpha-amylases: yellow meal worm alpha-amylase in complex with the amaranth alpha-amylase inhibitor at 2.0 A resolution."
      Pereira P.J., Lozanov V., Patthy A., Huber R., Bode W., Pongor S., Strobl S.
      Structure 7:1079-1088(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiAMY_TENMO
    AccessioniPrimary (citable) accession number: P56634
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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