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Protein

Beta-amylase

Gene

BMY1

Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei54Substrate1 Publication1
Binding sitei94Substrate1 Publication1
Binding sitei102Substrate1 Publication1
Active sitei187Proton donorPROSITE-ProRule annotation4 Publications1
Binding sitei296Substrate1 Publication1
Binding sitei301Substrate1 Publication1
Binding sitei343Substrate1 Publication1
Active sitei381Proton acceptor2 Publications1
Binding sitei421Substrate1 Publication1

GO - Molecular functioni

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. 2483.

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
Proteomesi
  • UP000008827 Componenti: Unplaced

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi102D → N or E: Loss of activity. 1 Publication1
Mutagenesisi187E → Q or D: Loss of activity. 2 Publications1
Mutagenesisi343T → A: Reduces activity 1700-fold. 1
Mutagenesisi343T → S: Reduces activity 360-fold. 1
Mutagenesisi343T → V: Reduces activity 16-fold. 1
Mutagenesisi381E → Q: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001539382 – 496Beta-amylaseAdd BLAST495

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP10538.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi3847.GLYMA06G45700.1.

Structurei

Secondary structure

1496
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 9Combined sources5
Beta strandi15 – 18Combined sources4
Beta strandi23 – 25Combined sources3
Turni26 – 28Combined sources3
Helixi33 – 45Combined sources13
Beta strandi50 – 56Combined sources7
Helixi57 – 60Combined sources4
Helixi71 – 82Combined sources12
Beta strandi86 – 92Combined sources7
Beta strandi96 – 99Combined sources4
Helixi110 – 118Combined sources9
Helixi120 – 122Combined sources3
Beta strandi123 – 125Combined sources3
Beta strandi131 – 136Combined sources6
Helixi138 – 140Combined sources3
Helixi151 – 165Combined sources15
Helixi167 – 171Combined sources5
Beta strandi175 – 180Combined sources6
Helixi184 – 186Combined sources3
Beta strandi187 – 189Combined sources3
Helixi195 – 197Combined sources3
Beta strandi201 – 203Combined sources3
Helixi212 – 224Combined sources13
Beta strandi234 – 236Combined sources3
Helixi243 – 245Combined sources3
Turni247 – 249Combined sources3
Helixi254 – 256Combined sources3
Helixi258 – 285Combined sources28
Turni286 – 288Combined sources3
Beta strandi292 – 296Combined sources5
Turni302 – 305Combined sources4
Helixi310 – 315Combined sources6
Helixi327 – 334Combined sources8
Turni335 – 337Combined sources3
Beta strandi339 – 342Combined sources4
Helixi349 – 351Combined sources3
Helixi354 – 356Combined sources3
Helixi360 – 373Combined sources14
Beta strandi378 – 381Combined sources4
Helixi389 – 399Combined sources11
Beta strandi406 – 409Combined sources4
Beta strandi415 – 420Combined sources6
Helixi424 – 427Combined sources4
Helixi429 – 442Combined sources14
Turni443 – 445Combined sources3
Helixi452 – 455Combined sources4
Helixi471 – 476Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP10538.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni382 – 383Substrate binding1 Publication2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 14 family.Curated

Phylogenomic databases

eggNOGiENOG410IJER. Eukaryota.
ENOG410XNXS. LUCA.
InParanoidiP10538.

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

        10         20         30         40         50
MATSDSNMLL NYVPVYVMLP LGVVNVDNVF EDPDGLKEQL LQLRAAGVDG
60 70 80 90 100
VMVDVWWGII ELKGPKQYDW RAYRSLFQLV QECGLTLQAI MSFHQCGGNV
110 120 130 140 150
GDIVNIPIPQ WVLDIGESNH DIFYTNRSGT RNKEYLTVGV DNEPIFHGRT
160 170 180 190 200
AIEIYSDYMK SFRENMSDFL ESGLIIDIEV GLGPAGELRY PSYPQSQGWE
210 220 230 240 250
FPRIGEFQCY DKYLKADFKA AVARAGHPEW ELPDDAGKYN DVPESTGFFK
260 270 280 290 300
SNGTYVTEKG KFFLTWYSNK LLNHGDQILD EANKAFLGCK VKLAIKVSGI
310 320 330 340 350
HWWYKVENHA AELTAGYYNL NDRDGYRPIA RMLSRHHAIL NFTCLEMRDS
360 370 380 390 400
EQPSDAKSGP QELVQQVLSG GWREDIRVAG ENALPRYDAT AYNQIILNAK
410 420 430 440 450
PQGVNNNGPP KLSMFGVTYL RLSDDLLQKS NFNIFKKFVL KMHADQDYCA
460 470 480 490
NPQKYNHAIT PLKPSAPKIP IEVLLEATKP TLPFPWLPET DMKVDG
Length:496
Mass (Da):56,143
Last modified:January 23, 2007 - v3
Checksum:iFB87917244FEF798
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9L → G AA sequence (PubMed:2430952).Curated1
Sequence conflicti184 – 190PAGELRY → QQESSDT in AAA33941 (Ref. 3) Curated7
Sequence conflicti203R → G in AAA33941 (Ref. 3) Curated1
Sequence conflicti400K → R in AAA33941 (Ref. 3) Curated1
Sequence conflicti473 – 474VL → FF in AAA33941 (Ref. 3) Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
X71419 mRNA. Translation: CAA50551.1.
M92090 mRNA. Translation: AAA33941.1. Frameshift.
PIRiA29291. A60473.
RefSeqiNP_001236247.1. NM_001249318.1.
UniGeneiGma.595.

3D structure databases

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

Protein-protein interaction databases

STRINGi3847.GLYMA06G45700.1.

Protein family/group databases

CAZyiGH14. Glycoside Hydrolase Family 14.

Proteomic databases

PRIDEiP10538.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi547931.
KEGGigmx:547931.

Phylogenomic databases

eggNOGiENOG410IJER. Eukaryota.
ENOG410XNXS. LUCA.
InParanoidiP10538.

Enzyme and pathway databases

BRENDAi3.2.1.2. 2483.

Miscellaneous databases

EvolutionaryTraceiP10538.

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_SOYBN
AccessioniPrimary (citable) accession number: P10538
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 123 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

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.