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P16098

- AMYB_HORVU

UniProt

P16098 - AMYB_HORVU

Protein

Beta-amylase

Gene

BMY1

Organism
Hordeum vulgare (Barley)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei51 – 511SubstrateBy similarity
    Binding sitei91 – 911SubstrateBy similarity
    Binding sitei99 – 991SubstrateBy similarity
    Active sitei184 – 1841Proton donorPROSITE-ProRule annotation
    Binding sitei293 – 2931SubstrateBy similarity
    Binding sitei298 – 2981SubstrateBy similarity
    Binding sitei340 – 3401SubstrateBy similarity
    Active sitei378 – 3781Proton acceptorPROSITE-ProRule annotation
    Binding sitei418 – 4181SubstrateBy similarity

    GO - Molecular functioni

    1. beta-amylase activity Source: UniProtKB-EC
    2. identical protein binding Source: IntAct

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Protein family/group databases

    CAZyiGH14. Glycoside Hydrolase Family 14.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-amylase (EC:3.2.1.2)
    Alternative name(s):
    1,4-alpha-D-glucan maltohydrolase
    Gene namesi
    Name:BMY1
    Synonyms:AMYB
    OrganismiHordeum vulgare (Barley)
    Taxonomic identifieri4513 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

    Organism-specific databases

    GrameneiP16098.

    Pathology & Biotechi

    Protein family/group databases

    Allergomei420. Hor v 17.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 535535Beta-amylasePRO_0000153933Add
    BLAST

    Expressioni

    Gene expression databases

    GenevestigatoriP16098.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-7799617,EBI-7799617

    Protein-protein interaction databases

    MINTiMINT-8307128.

    Structurei

    Secondary structure

    1
    535
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 83
    Beta strandi11 – 155
    Helixi30 – 4213
    Beta strandi47 – 537
    Helixi54 – 574
    Helixi68 – 7912
    Beta strandi83 – 897
    Beta strandi93 – 964
    Helixi107 – 1159
    Helixi117 – 1193
    Beta strandi120 – 1223
    Beta strandi128 – 1336
    Helixi135 – 1373
    Turni142 – 1443
    Helixi148 – 16821
    Beta strandi172 – 1776
    Helixi181 – 1833
    Beta strandi184 – 1863
    Turni193 – 1953
    Helixi209 – 22113
    Helixi240 – 2423
    Turni244 – 2463
    Helixi251 – 2533
    Helixi255 – 28329
    Beta strandi289 – 2935
    Turni299 – 3024
    Helixi307 – 3126
    Beta strandi318 – 3203
    Helixi324 – 3318
    Turni332 – 3343
    Beta strandi336 – 3394
    Helixi346 – 3483
    Helixi351 – 3533
    Helixi357 – 37014
    Beta strandi375 – 3784
    Helixi386 – 39611
    Beta strandi403 – 4053
    Beta strandi412 – 4176
    Turni421 – 4244
    Helixi426 – 43914
    Turni440 – 4423
    Beta strandi447 – 4504
    Helixi464 – 4685
    Helixi469 – 4713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B1YX-ray2.50A6-504[»]
    2XFFX-ray1.31A1-535[»]
    2XFRX-ray0.97A1-535[»]
    2XFYX-ray1.21A1-535[»]
    2XG9X-ray1.80A1-535[»]
    2XGBX-ray1.20A1-535[»]
    2XGIX-ray1.30A1-535[»]
    ProteinModelPortaliP16098.
    SMRiP16098. Positions 5-504.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16098.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati489 – 499111Add
    BLAST
    Repeati500 – 510112Add
    BLAST
    Repeati511 – 521113Add
    BLAST
    Repeati522 – 532114; approximateAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni379 – 3802Substrate bindingBy similarity
    Regioni489 – 532444 X 11 AA tandem repeatsAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 14 family.Curated

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001554. Glyco_hydro_14.
    IPR018238. Glyco_hydro_14_CS.
    IPR001371. Glyco_hydro_14B_pln.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF01373. Glyco_hydro_14. 1 hit.
    [Graphical view]
    PRINTSiPR00750. BETAAMYLASE.
    PR00842. GLHYDLASE14B.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00506. BETA_AMYLASE_1. 1 hit.
    PS00679. BETA_AMYLASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P16098-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEVNVKGNYV QVYVMLPLDA VSVNNRFEKG DELRAQLRKL VEAGVDGVMV    50
    DVWWGLVEGK GPKAYDWSAY KQLFELVQKA GLKLQAIMSF HQCGGNVGDA 100
    VNIPIPQWVR DVGTRDPDIF YTDGHGTRNI EYLTLGVDNQ PLFHGRSAVQ 150
    MYADYMTSFR ENMKDFLDAG VIVDIEVGLG PAGEMRYPSY PQSHGWSFPG 200
    IGEFICYDKY LQADFKAAAA AVGHPEWEFP NDVGQYNDTP ERTQFFRDNG 250
    TYLSEKGRFF LAWYSNNLIK HGDRILDEAN KVFLGYKVQL AIKISGIHWW 300
    YKVPSHAAEL TAGYYNLHDR DGYRTIARML KRHRASINFT CAEMRDLEQS 350
    SQAMSAPEEL VQQVLSAGWR EGLNVACENA LPRYDPTAYN TILRNARPHG 400
    INQSGPPEHK LFGFTYLRLS NQLVEGQNYV NFKTFVDRMH ANLPRDPYVD 450
    PMAPLPRSGP EISIEMILQA AQPKLQPFPF QEHTDLPVGP TGGMGGQAEG 500
    PTCGMGGQVK GPTGGMGGQA EDPTSGIGGE LPATM 535
    Length:535
    Mass (Da):59,647
    Last modified:April 1, 1990 - v1
    Checksum:iFFDA4CED53E9A89E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti233 – 2331V → A in BAA08741. (PubMed:8534999)Curated
    Sequence conflicti233 – 2331V → A in BAA04815. (PubMed:8188635)Curated
    Sequence conflicti347 – 3471L → S in BAA08741. (PubMed:8534999)Curated
    Sequence conflicti347 – 3471L → S in BAA04815. (PubMed:8188635)Curated
    Sequence conflicti527 – 5271I → M in BAA08741. (PubMed:8534999)Curated
    Sequence conflicti527 – 5271I → M in BAA04815. (PubMed:8188635)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52321 mRNA. Translation: CAA36556.1.
    D49999 Genomic DNA. Translation: BAA08741.1.
    D21349 mRNA. Translation: BAA04815.1.
    PIRiS00222.
    UniGeneiHv.2064.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52321 mRNA. Translation: CAA36556.1 .
    D49999 Genomic DNA. Translation: BAA08741.1 .
    D21349 mRNA. Translation: BAA04815.1 .
    PIRi S00222.
    UniGenei Hv.2064.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B1Y X-ray 2.50 A 6-504 [» ]
    2XFF X-ray 1.31 A 1-535 [» ]
    2XFR X-ray 0.97 A 1-535 [» ]
    2XFY X-ray 1.21 A 1-535 [» ]
    2XG9 X-ray 1.80 A 1-535 [» ]
    2XGB X-ray 1.20 A 1-535 [» ]
    2XGI X-ray 1.30 A 1-535 [» ]
    ProteinModelPortali P16098.
    SMRi P16098. Positions 5-504.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-8307128.

    Chemistry

    BindingDBi P16098.
    ChEMBLi CHEMBL4371.

    Protein family/group databases

    Allergomei 420. Hor v 17.
    CAZyi GH14. Glycoside Hydrolase Family 14.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei P16098.

    Miscellaneous databases

    EvolutionaryTracei P16098.

    Gene expression databases

    Genevestigatori P16098.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001554. Glyco_hydro_14.
    IPR018238. Glyco_hydro_14_CS.
    IPR001371. Glyco_hydro_14B_pln.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF01373. Glyco_hydro_14. 1 hit.
    [Graphical view ]
    PRINTSi PR00750. BETAAMYLASE.
    PR00842. GLHYDLASE14B.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00506. BETA_AMYLASE_1. 1 hit.
    PS00679. BETA_AMYLASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure and differential expression of beta-amylase in normal and mutant barleys."
      Kreis M., Williamson M., Buxton B., Pywell J., Hejgaard J., Svendsen I.
      Eur. J. Biochem. 169:517-525(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Endosperm.
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Haruna Two-rows.
    3. "PCR cloning and sequencing of the beta-amylase cDNA from barley."
      Yoshigi N., Okada Y., Sahara H., Koshino S.
      J. Biochem. 115:47-51(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Haruna Two-rows.
    4. "The crystal structure of the sevenfold mutant of barley beta-amylase with increased thermostability at 2.5 A resolution."
      Mikami B., Yoon H.-J., Yoshigi N.
      J. Mol. Biol. 285:1235-1243(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 5-504.

    Entry informationi

    Entry nameiAMYB_HORVU
    AccessioniPrimary (citable) accession number: P16098
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 97 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    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