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Protein

Beta-amylase

Gene

BMY1

Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei51SubstrateBy similarity1
Binding sitei91SubstrateBy similarity1
Binding sitei99SubstrateBy similarity1
Active sitei184Proton donorPROSITE-ProRule annotation1
Binding sitei293SubstrateBy similarity1
Binding sitei298SubstrateBy similarity1
Binding sitei340SubstrateBy similarity1
Active sitei378Proton acceptorBy similarity1
Binding sitei418SubstrateBy similarity1

GO - Molecular functioni

  • beta-amylase activity Source: UniProtKB-EC
  • identical protein binding Source: IntAct

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

BRENDAi3.2.1.2. 2687.

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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

Pathology & Biotechi

Protein family/group databases

Allergomei420. Hor v 17.

Chemistry databases

ChEMBLiCHEMBL4371.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001539331 – 535Beta-amylaseAdd BLAST535

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

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

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

MINTiMINT-8307128.

Chemistry databases

BindingDBiP16098.

Structurei

Secondary structure

1535
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 8Combined sources3
Beta strandi11 – 15Combined sources5
Helixi30 – 42Combined sources13
Beta strandi47 – 53Combined sources7
Helixi54 – 57Combined sources4
Helixi68 – 79Combined sources12
Beta strandi83 – 89Combined sources7
Beta strandi93 – 96Combined sources4
Helixi107 – 115Combined sources9
Helixi117 – 119Combined sources3
Beta strandi120 – 122Combined sources3
Beta strandi128 – 133Combined sources6
Helixi135 – 137Combined sources3
Turni142 – 144Combined sources3
Helixi148 – 168Combined sources21
Beta strandi172 – 177Combined sources6
Helixi181 – 183Combined sources3
Beta strandi184 – 186Combined sources3
Turni193 – 195Combined sources3
Helixi209 – 221Combined sources13
Helixi240 – 242Combined sources3
Turni244 – 246Combined sources3
Helixi251 – 253Combined sources3
Helixi255 – 283Combined sources29
Beta strandi289 – 293Combined sources5
Turni299 – 302Combined sources4
Helixi307 – 312Combined sources6
Beta strandi318 – 320Combined sources3
Helixi324 – 331Combined sources8
Turni332 – 334Combined sources3
Beta strandi336 – 339Combined sources4
Helixi346 – 348Combined sources3
Helixi351 – 353Combined sources3
Helixi357 – 370Combined sources14
Beta strandi375 – 378Combined sources4
Helixi386 – 396Combined sources11
Beta strandi403 – 405Combined sources3
Beta strandi412 – 417Combined sources6
Turni421 – 424Combined sources4
Helixi426 – 439Combined sources14
Turni440 – 442Combined sources3
Beta strandi447 – 450Combined sources4
Helixi464 – 468Combined sources5
Helixi469 – 471Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16098.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati489 – 4991Add BLAST11
Repeati500 – 5102Add BLAST11
Repeati511 – 5213Add BLAST11
Repeati522 – 5324; approximateAdd BLAST11

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni379 – 380Substrate bindingBy similarity2
Regioni489 – 5324 X 11 AA tandem repeatsAdd BLAST44

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)DescriptionActionsGraphical viewLength
Sequence conflicti233V → A in BAA08741 (PubMed:8534999).Curated1
Sequence conflicti233V → A in BAA04815 (PubMed:8188635).Curated1
Sequence conflicti347L → S in BAA08741 (PubMed:8534999).Curated1
Sequence conflicti347L → S in BAA04815 (PubMed:8188635).Curated1
Sequence conflicti527I → M in BAA08741 (PubMed:8534999).Curated1
Sequence conflicti527I → M in BAA04815 (PubMed:8188635).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
X52321 mRNA. Translation: CAA36556.1.
D49999 Genomic DNA. Translation: BAA08741.1.
D21349 mRNA. Translation: BAA04815.1.
PIRiS00222.
UniGeneiHv.2064.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-8307128.

Chemistry databases

BindingDBiP16098.
ChEMBLiCHEMBL4371.

Protein family/group databases

Allergomei420. Hor v 17.
CAZyiGH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.2. 2687.

Miscellaneous databases

EvolutionaryTraceiP16098.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 107 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.