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P10538

- AMYB_SOYBN

UniProt

P10538 - AMYB_SOYBN

Protein

Beta-amylase

Gene

BMY1

Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei54 – 541Substrate
    Binding sitei94 – 941Substrate
    Binding sitei102 – 1021Substrate
    Active sitei187 – 1871Proton donor1 PublicationPROSITE-ProRule annotation
    Binding sitei296 – 2961Substrate
    Binding sitei301 – 3011Substrate
    Binding sitei343 – 3431Substrate
    Active sitei381 – 3811Proton acceptor
    Binding sitei421 – 4211Substrate

    GO - Molecular functioni

    1. beta-amylase activity Source: UniProtKB-EC

    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
    OrganismiGlycine max (Soybean) (Glycine hispida)
    Taxonomic identifieri3847 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja
    ProteomesiUP000008827: Unplaced

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi102 – 1021D → N or E: Loss of activity. 1 Publication
    Mutagenesisi187 – 1871E → Q or D: Loss of activity. 2 Publications
    Mutagenesisi343 – 3431T → A: Reduces activity 1700-fold.
    Mutagenesisi343 – 3431T → S: Reduces activity 360-fold.
    Mutagenesisi343 – 3431T → V: Reduces activity 16-fold.
    Mutagenesisi381 – 3811E → Q: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 496495Beta-amylasePRO_0000153938Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Expressioni

    Gene expression databases

    GenevestigatoriP10538.

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    496
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 95
    Beta strandi15 – 184
    Beta strandi23 – 253
    Turni26 – 283
    Helixi33 – 4513
    Beta strandi50 – 567
    Helixi57 – 604
    Helixi71 – 8212
    Beta strandi86 – 927
    Beta strandi96 – 994
    Helixi110 – 1189
    Helixi120 – 1223
    Beta strandi123 – 1253
    Beta strandi131 – 1366
    Helixi138 – 1403
    Helixi151 – 16515
    Helixi167 – 1715
    Beta strandi175 – 1806
    Helixi184 – 1863
    Beta strandi187 – 1893
    Helixi195 – 1973
    Beta strandi201 – 2033
    Helixi212 – 22413
    Beta strandi234 – 2363
    Helixi243 – 2453
    Turni247 – 2493
    Helixi254 – 2563
    Helixi258 – 28528
    Turni286 – 2883
    Beta strandi292 – 2965
    Turni302 – 3054
    Helixi310 – 3156
    Helixi327 – 3348
    Turni335 – 3373
    Beta strandi339 – 3424
    Helixi349 – 3513
    Helixi354 – 3563
    Helixi360 – 37314
    Beta strandi378 – 3814
    Helixi389 – 39911
    Beta strandi406 – 4094
    Beta strandi415 – 4206
    Helixi424 – 4274
    Helixi429 – 44214
    Turni443 – 4453
    Helixi452 – 4554
    Helixi471 – 4766

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BFNX-ray2.07A2-496[»]
    1BTCX-ray2.00A6-496[»]
    1BYAX-ray2.20A2-496[»]
    1BYBX-ray1.90A2-496[»]
    1BYCX-ray2.20A2-496[»]
    1BYDX-ray2.20A2-496[»]
    1Q6CX-ray1.86A2-496[»]
    1Q6DX-ray2.00A2-496[»]
    1Q6EX-ray1.95A2-496[»]
    1Q6FX-ray2.10A2-496[»]
    1Q6GX-ray2.00A2-496[»]
    1UKOX-ray2.10A/B/C/D2-496[»]
    1UKPX-ray2.10A/B/C/D2-496[»]
    1V3HX-ray1.60A2-496[»]
    1V3IX-ray1.90A2-496[»]
    1WDPX-ray1.27A2-496[»]
    1WDQX-ray1.28A2-496[»]
    1WDRX-ray1.35A2-496[»]
    1WDSX-ray1.64A2-496[»]
    ProteinModelPortaliP10538.
    SMRiP10538. Positions 6-496.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10538.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni382 – 3832Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 14 family.Curated

    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.

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

    P10538-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATSDSNMLL NYVPVYVMLP LGVVNVDNVF EDPDGLKEQL LQLRAAGVDG    50
    VMVDVWWGII ELKGPKQYDW RAYRSLFQLV QECGLTLQAI MSFHQCGGNV 100
    GDIVNIPIPQ WVLDIGESNH DIFYTNRSGT RNKEYLTVGV DNEPIFHGRT 150
    AIEIYSDYMK SFRENMSDFL ESGLIIDIEV GLGPAGELRY PSYPQSQGWE 200
    FPRIGEFQCY DKYLKADFKA AVARAGHPEW ELPDDAGKYN DVPESTGFFK 250
    SNGTYVTEKG KFFLTWYSNK LLNHGDQILD EANKAFLGCK VKLAIKVSGI 300
    HWWYKVENHA AELTAGYYNL NDRDGYRPIA RMLSRHHAIL NFTCLEMRDS 350
    EQPSDAKSGP QELVQQVLSG GWREDIRVAG ENALPRYDAT AYNQIILNAK 400
    PQGVNNNGPP KLSMFGVTYL RLSDDLLQKS NFNIFKKFVL KMHADQDYCA 450
    NPQKYNHAIT PLKPSAPKIP IEVLLEATKP TLPFPWLPET DMKVDG 496
    Length:496
    Mass (Da):56,143
    Last modified:January 23, 2007 - v3
    Checksum:iFB87917244FEF798
    GO

    Sequence cautioni

    The sequence AAA33941.1 differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91L → G AA sequence (PubMed:2430952)Curated
    Sequence conflicti184 – 1907PAGELRY → QQESSDT in AAA33941. 1 PublicationCurated
    Sequence conflicti203 – 2031R → G in AAA33941. 1 PublicationCurated
    Sequence conflicti400 – 4001K → R in AAA33941. 1 PublicationCurated
    Sequence conflicti473 – 4742VL → FF in AAA33941. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71419 mRNA. Translation: CAA50551.1.
    M92090 mRNA. Translation: AAA33941.1. Frameshift.
    PIRiA29291. A60473.
    RefSeqiNP_001236247.1. NM_001249318.1.
    UniGeneiGma.595.

    Genome annotation databases

    GeneIDi547931.
    KEGGigmx:547931.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71419 mRNA. Translation: CAA50551.1 .
    M92090 mRNA. Translation: AAA33941.1 . Frameshift.
    PIRi A29291. A60473.
    RefSeqi NP_001236247.1. NM_001249318.1.
    UniGenei Gma.595.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BFN X-ray 2.07 A 2-496 [» ]
    1BTC X-ray 2.00 A 6-496 [» ]
    1BYA X-ray 2.20 A 2-496 [» ]
    1BYB X-ray 1.90 A 2-496 [» ]
    1BYC X-ray 2.20 A 2-496 [» ]
    1BYD X-ray 2.20 A 2-496 [» ]
    1Q6C X-ray 1.86 A 2-496 [» ]
    1Q6D X-ray 2.00 A 2-496 [» ]
    1Q6E X-ray 1.95 A 2-496 [» ]
    1Q6F X-ray 2.10 A 2-496 [» ]
    1Q6G X-ray 2.00 A 2-496 [» ]
    1UKO X-ray 2.10 A/B/C/D 2-496 [» ]
    1UKP X-ray 2.10 A/B/C/D 2-496 [» ]
    1V3H X-ray 1.60 A 2-496 [» ]
    1V3I X-ray 1.90 A 2-496 [» ]
    1WDP X-ray 1.27 A 2-496 [» ]
    1WDQ X-ray 1.28 A 2-496 [» ]
    1WDR X-ray 1.35 A 2-496 [» ]
    1WDS X-ray 1.64 A 2-496 [» ]
    ProteinModelPortali P10538.
    SMRi P10538. Positions 6-496.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH14. Glycoside Hydrolase Family 14.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 547931.
    KEGGi gmx:547931.

    Miscellaneous databases

    EvolutionaryTracei P10538.

    Gene expression databases

    Genevestigatori P10538.

    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. "Expression and mutation of soybean beta-amylase in Escherichia coli."
      Totsuka A., Fukazawa C.
      Eur. J. Biochem. 214:787-794(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Primary structure and function of beta-amylase."
      Mikami B., Morita Y., Fukazawa C.
      Seikagaku 60:211-216(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Nucleotide and deduced protein sequence of beta-amylase."
      Ehrlich K.C., Montalbano B.G.
      Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "N-terminal sequence of soybean beta-amylase."
      Mikami B., Nomura K., Morita Y.
      J. Biochem. 100:513-516(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-10.
    5. "Identification of glutamic acid 186 affinity-labeled by 2,3-epoxypropyl alpha-D-glucopyranoside in soybean beta-amylase."
      Nitta Y., Isoda Y., Toda H., Sakiyama F.
      J. Biochem. 105:573-576(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE GLU-187.
    6. "Residues essential for catalytic activity of soybean beta-amylase."
      Totsuka A., Nong V.H., Kadokawa H., Kim C.-S., Itoh Y., Fukazawa C.
      Eur. J. Biochem. 221:649-654(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITES, MUTAGENESIS OF ASP-102 AND GLU-187.
    7. "Three-dimensional structure of soybean beta-amylase determined at 3.0-A resolution: preliminary chain tracing of the complex with alpha-cyclodextrin."
      Mikami B., Sato M., Shibata T., Hirose M., Aibara S., Katsube Y., Morita Y.
      J. Biochem. 112:541-546(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    8. "The 2.0-A resolution structure of soybean beta-amylase complexed with alpha-cyclodextrin."
      Mikami B., Hehre E.J., Sato M., Katsube Y., Hirose M., Morita Y., Sacchettini J.C.
      Biochemistry 32:6836-6845(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    9. "Crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: active site components and their apparent roles in catalysis."
      Mikami B., Degano M., Hehre E.J., Sacchettini J.C.
      Biochemistry 33:7779-7787(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    10. "Crystal structure of recombinant soybean beta-amylase complexed with beta-cyclodextrin."
      Adachi M., Mikami B., Katsube T., Utsumi S.
      J. Biol. Chem. 273:19859-19865(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS).
    11. "The roles of Glu186 and Glu380 in the catalytic reaction of soybean beta-amylase."
      Kang Y.N., Adachi M., Utsumi S., Mikami B.
      J. Mol. Biol. 339:1129-1140(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MUTANTS GLN-187 AND GLN-381 IN COMPLEXES WITH SUBSTRATE ANALOGS, ACTIVE SITE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-187 AND GLU-381.
    12. "Structural analysis of threonine 342 mutants of soybean beta-amylase: role of a conformational change of the inner loop in the catalytic mechanism."
      Kang Y.N., Tanabe A., Adachi M., Utsumi S., Mikami B.
      Biochemistry 44:5106-5116(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) OF MUTANTS ALA/SER/VAL-343 IN COMPLEXES WITH MALTOSE.

    Entry informationi

    Entry nameiAMYB_SOYBN
    AccessioniPrimary (citable) accession number: P10538
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 110 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    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