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P16098

- AMYB_HORVU

UniProt

P16098 - AMYB_HORVU

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Protein

Beta-amylase

Gene

BMY1

Organism
Hordeum vulgare (Barley)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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

        10         20         30         40         50
MEVNVKGNYV QVYVMLPLDA VSVNNRFEKG DELRAQLRKL VEAGVDGVMV
60 70 80 90 100
DVWWGLVEGK GPKAYDWSAY KQLFELVQKA GLKLQAIMSF HQCGGNVGDA
110 120 130 140 150
VNIPIPQWVR DVGTRDPDIF YTDGHGTRNI EYLTLGVDNQ PLFHGRSAVQ
160 170 180 190 200
MYADYMTSFR ENMKDFLDAG VIVDIEVGLG PAGEMRYPSY PQSHGWSFPG
210 220 230 240 250
IGEFICYDKY LQADFKAAAA AVGHPEWEFP NDVGQYNDTP ERTQFFRDNG
260 270 280 290 300
TYLSEKGRFF LAWYSNNLIK HGDRILDEAN KVFLGYKVQL AIKISGIHWW
310 320 330 340 350
YKVPSHAAEL TAGYYNLHDR DGYRTIARML KRHRASINFT CAEMRDLEQS
360 370 380 390 400
SQAMSAPEEL VQQVLSAGWR EGLNVACENA LPRYDPTAYN TILRNARPHG
410 420 430 440 450
INQSGPPEHK LFGFTYLRLS NQLVEGQNYV NFKTFVDRMH ANLPRDPYVD
460 470 480 490 500
PMAPLPRSGP EISIEMILQA AQPKLQPFPF QEHTDLPVGP TGGMGGQAEG
510 520 530
PTCGMGGQVK GPTGGMGGQA EDPTSGIGGE LPATM
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