Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P00693

- AMY1_HORVU

UniProt

P00693 - AMY1_HORVU

Protein

Alpha-amylase type A isozyme

Gene

AMY1.1

Organism
Hordeum vulgare (Barley)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.3 Publications

    Cofactori

    Binds 3 calcium ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi116 – 1161Calcium 1
    Metal bindingi133 – 1331Calcium 2
    Metal bindingi136 – 1361Calcium 2; via carbonyl oxygen
    Metal bindingi138 – 1381Calcium 2; via carbonyl oxygen
    Metal bindingi142 – 1421Calcium 2
    Metal bindingi152 – 1521Calcium 3
    Metal bindingi163 – 1631Calcium 1
    Metal bindingi166 – 1661Calcium 1; via carbonyl oxygen
    Metal bindingi167 – 1671Calcium 3
    Metal bindingi168 – 1681Calcium 3; via carbonyl oxygen
    Metal bindingi171 – 1711Calcium 3; via carbonyl oxygen
    Metal bindingi173 – 1731Calcium 1
    Metal bindingi173 – 1731Calcium 3
    Active sitei204 – 2041Nucleophile1 Publication
    Metal bindingi208 – 2081Calcium 1; via carbonyl oxygen
    Active sitei229 – 2291Proton donor1 Publication
    Binding sitei231 – 2311Substrate
    Binding sitei233 – 2331Substrate
    Binding sitei251 – 2511Substrate
    Binding sitei258 – 2581Substrate
    Binding sitei295 – 2951Substrate
    Binding sitei314 – 3141Substrate
    Sitei315 – 3151Transition state stabilizer
    Binding sitei320 – 3201Substrate
    Binding sitei399 – 3991Substrate
    Binding sitei426 – 4261Substrate

    GO - Molecular functioni

    1. alpha-amylase activity Source: UniProtKB-EC
    2. calcium ion binding Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW
    2. response to abscisic acid Source: EnsemblPlants/Gramene
    3. response to gibberellin Source: EnsemblPlants/Gramene

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Germination

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.2.1.1. 2687.

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-amylase type A isozyme (EC:3.2.1.1)
    Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase
    AMY1
    Low pI alpha-amylase
    Gene namesi
    Name:AMY1.1
    OrganismiHordeum vulgare (Barley)
    Taxonomic identifieri4513 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

    Organism-specific databases

    GrameneiP00693.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi117 – 1171H → N: 20-fold decrease in activity. 1 Publication
    Mutagenesisi129 – 1291Y → A: Reduces affinity for starch granules 3-fold. 1 Publication
    Mutagenesisi204 – 2041D → A or N: Loss of activity. 2 Publications
    Mutagenesisi229 – 2291E → Q: Loss of activity. 1 Publication
    Mutagenesisi302 – 3021W → A: Over 10-fold decrease in affinity for starch granules. Abolishes binding of starch granules and reduces activity towards starch granules by 99%; when associated with A-303 and A-404. 1 Publication
    Mutagenesisi303 – 3031W → A: Over 10-fold decrease in affinity for starch granules. Abolishes binding of starch granules and reduces activity towards starch granules by 99%; when associated with A-302 and A-404. 2 Publications
    Mutagenesisi314 – 3141H → N: 10-fold decrease in activity. 1 Publication
    Mutagenesisi315 – 3151D → N: Loss of activity. 1 Publication
    Mutagenesisi404 – 4041Y → A: Reduces affinity for starch granules 9-fold and reduces activity by 90%. Abolishes binding of starch granules and reduces activity towards starch granules by 99%; when associated with A-302 and A-303. 3 Publications
    Mutagenesisi404 – 4041Y → M: Abolishes binding to cyclodextrin-Sepharose and strongly reduces enzyme activity. 3 Publications
    Mutagenesisi419 – 4191H → A: Slightly decreased catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Add
    BLAST
    Chaini25 – 438414Alpha-amylase type A isozymePRO_0000001404Add
    BLAST

    Expressioni

    Developmental stagei

    Production of alpha-amylase is hormonally regulated. Germinating embryos produce the hormone gibberellic acid, which within 10 hours stimulates the aleurone cells covering the endosperm of the seed to produce alpha-amylase. The enzyme then degrades the starch within the endosperm for use by the developing plant embryo.

    Gene expression databases

    GenevestigatoriP00693.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Structurei

    Secondary structure

    1
    438
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 303
    Helixi36 – 383
    Helixi43 – 486
    Helixi51 – 566
    Beta strandi61 – 644
    Beta strandi70 – 723
    Beta strandi75 – 784
    Helixi84 – 863
    Helixi92 – 10413
    Beta strandi108 – 1136
    Beta strandi121 – 1233
    Beta strandi129 – 1313
    Beta strandi135 – 1395
    Helixi145 – 1473
    Turni153 – 1553
    Helixi179 – 19416
    Beta strandi200 – 2034
    Helixi206 – 2083
    Helixi211 – 22111
    Beta strandi226 – 2283
    Beta strandi240 – 2423
    Helixi247 – 26014
    Helixi262 – 2643
    Beta strandi265 – 2706
    Helixi272 – 28110
    Turni282 – 2843
    Helixi286 – 2894
    Helixi299 – 3024
    Helixi304 – 3063
    Beta strandi307 – 3115
    Turni314 – 3163
    Turni318 – 3203
    Helixi327 – 3293
    Helixi330 – 33910
    Beta strandi340 – 3478
    Helixi348 – 3525
    Beta strandi353 – 3553
    Helixi357 – 36913
    Beta strandi378 – 3847
    Beta strandi387 – 3926
    Turni393 – 3953
    Beta strandi396 – 4027
    Helixi407 – 4093
    Beta strandi415 – 4206
    Beta strandi423 – 4275

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HT6X-ray1.50A25-429[»]
    1P6WX-ray2.00A25-429[»]
    1RP8X-ray2.00A25-429[»]
    1RP9X-ray2.00A25-429[»]
    1RPKX-ray2.00A25-429[»]
    2QPSX-ray2.20A25-429[»]
    2QPUX-ray1.70A/B/C25-429[»]
    3BSGX-ray1.95A25-438[»]
    3BSHX-ray3.00A25-438[»]
    ProteinModelPortaliP00693.
    SMRiP00693. Positions 25-428.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00693.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni69 – 713Substrate binding
    Regioni76 – 772Substrate binding
    Regioni202 – 2076Substrate binding
    Regioni301 – 3033Substrate binding
    Regioni404 – 4063Substrate binding
    Regioni416 – 4227Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR012850. A-amylase_bs_C.
    IPR013775. A-amylase_pln.
    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.
    PfamiPF07821. Alpha-amyl_C2. 1 hit.
    PF00128. Alpha-amylase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001028. Alph-amls_plant. 1 hit.
    PRINTSiPR00110. ALPHAAMYLASE.
    SMARTiSM00642. Aamy. 1 hit.
    SM00810. Alpha-amyl_C2. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00693-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKNGSLCCF SLLLLLLLAG LASGHQVLFQ GFNWESWKQS GGWYNMMMGK    50
    VDDIAAAGVT HVWLPPPSHS VSNEGYMPGR LYDIDASKYG NAAELKSLIG 100
    ALHGKGVQAI ADIVINHRCA DYKDSRGIYC IFEGGTSDGR LDWGPHMICR 150
    DDTKYSDGTA NLDTGADFAA APDIDHLNDR VQRELKEWLL WLKSDLGFDA 200
    WRLDFARGYS PEMAKVYIDG TSPSLAVAEV WDNMATGGDG KPNYDQDAHR 250
    QNLVNWVDKV GGAASAGMVF DFTTKGILNA AVEGELWRLI DPQGKAPGVM 300
    GWWPAKAATF VDNHDTGSTQ AMWPFPSDKV MQGYAYILTH PGIPCIFYDH 350
    FFNWGFKDQI AALVAIRKRN GITATSALKI LMHEGDAYVA EIDGKVVVKI 400
    GSRYDVGAVI PAGFVTSAHG NDYAVWEKNG AAATLQRS 438
    Length:438
    Mass (Da):47,796
    Last modified:July 21, 1986 - v1
    Checksum:i2393FDAC51E80F51
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01236 mRNA. Translation: AAA32929.1.
    PIRiA00846. ALBH.
    UniGeneiHv.68.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01236 mRNA. Translation: AAA32929.1 .
    PIRi A00846. ALBH.
    UniGenei Hv.68.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HT6 X-ray 1.50 A 25-429 [» ]
    1P6W X-ray 2.00 A 25-429 [» ]
    1RP8 X-ray 2.00 A 25-429 [» ]
    1RP9 X-ray 2.00 A 25-429 [» ]
    1RPK X-ray 2.00 A 25-429 [» ]
    2QPS X-ray 2.20 A 25-429 [» ]
    2QPU X-ray 1.70 A/B/C 25-429 [» ]
    3BSG X-ray 1.95 A 25-438 [» ]
    3BSH X-ray 3.00 A 25-438 [» ]
    ProteinModelPortali P00693.
    SMRi P00693. Positions 25-428.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei P00693.

    Enzyme and pathway databases

    BRENDAi 3.2.1.1. 2687.

    Miscellaneous databases

    EvolutionaryTracei P00693.

    Gene expression databases

    Genevestigatori P00693.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR012850. A-amylase_bs_C.
    IPR013775. A-amylase_pln.
    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 PF07821. Alpha-amyl_C2. 1 hit.
    PF00128. Alpha-amylase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001028. Alph-amls_plant. 1 hit.
    PRINTSi PR00110. ALPHAAMYLASE.
    SMARTi SM00642. Aamy. 1 hit.
    SM00810. Alpha-amyl_C2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and sequence analysis of a barley alpha-amylase cDNA clone."
      Rogers J.C., Milliman C.
      J. Biol. Chem. 258:8169-8174(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Himalaya.
      Tissue: Aleurone.
    2. "Site-directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, histidine 290, and aspartic acid 291 at the active site and tryptophan 279 at the raw starch binding site in barley alpha-amylase 1."
      Sogaard M., Kadziola A., Haser R., Svensson B.
      J. Biol. Chem. 268:22480-22484(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-117; ASP-204; GLU-229; TRP-303; HIS-314 AND ASP-315, CATALYTIC ACTIVITY, ACTIVE SITE.
    3. "Two secondary carbohydrate binding sites on the surface of barley alpha-amylase 1 have distinct functions and display synergy in hydrolysis of starch granules."
      Nielsen M.M., Bozonnet S., Seo E.S., Motyan J.A., Andersen J.M., Dilokpimol A., Abou Hachem M., Gyemant G., Naested H., Kandra L., Sigurskjold B.W., Svensson B.
      Biochemistry 48:7686-7697(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TRP-302; TRP-303 AND TYR-404.
    4. "The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs."
      Robert X., Haser R., Gottschalk T.E., Ratajczak F., Driguez H., Svensson B., Aghajari N.
      Structure 11:973-984(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-428 IN COMPLEX WITH CALCIUM IONS.
    5. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 25-429 IN COMPLEXES WITH CALCIUM IONS; ACARBOSE AND MALTOHEPTAOSE, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-204.
    6. "The 'pair of sugar tongs' site on the non-catalytic domain C of barley alpha-amylase participates in substrate binding and activity."
      Bozonnet S., Jensen M.T., Nielsen M.M., Aghajari N., Jensen M.H., Kramhoeft B., Willemoes M., Tranier S., Haser R., Svensson B.
      FEBS J. 274:5055-5067(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 25-429 IN COMPLEX WITH CALCIUM IONS AND ACARBOSE, MUTAGENESIS OF TYR-404.
    7. "Multi-site substrate binding and interplay in barley alpha-amylase 1."
      Nielsen M.M., Seo E.S., Bozonnet S., Aghajari N., Robert X., Haser R., Svensson B.
      FEBS Lett. 582:2567-2571(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEXES WITH CALCIUM IONS AND GLUCOSE, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-129; TYR-404 AND HIS-419.

    Entry informationi

    Entry nameiAMY1_HORVU
    AccessioniPrimary (citable) accession number: P00693
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are at least 4 types of alpha-amylase in barley.
    Mutagenesis experiments indicate that His-117 and His-314 participate in transition state stabilization but not directly in catalysis.
    Binds starch not only at the active site, but also via accessory binding sites on the protein surface that are important for efficient binding to starch granules and thereby increase enzyme activity.

    Keywords - Technical termi

    3D-structure

    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