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P10538

- AMYB_SOYBN

UniProt

P10538 - AMYB_SOYBN

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Protein

Beta-amylase

Gene

BMY1

Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed - 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)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
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
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 – 95Combined sources
Beta strandi15 – 184Combined sources
Beta strandi23 – 253Combined sources
Turni26 – 283Combined sources
Helixi33 – 4513Combined sources
Beta strandi50 – 567Combined sources
Helixi57 – 604Combined sources
Helixi71 – 8212Combined sources
Beta strandi86 – 927Combined sources
Beta strandi96 – 994Combined sources
Helixi110 – 1189Combined sources
Helixi120 – 1223Combined sources
Beta strandi123 – 1253Combined sources
Beta strandi131 – 1366Combined sources
Helixi138 – 1403Combined sources
Helixi151 – 16515Combined sources
Helixi167 – 1715Combined sources
Beta strandi175 – 1806Combined sources
Helixi184 – 1863Combined sources
Beta strandi187 – 1893Combined sources
Helixi195 – 1973Combined sources
Beta strandi201 – 2033Combined sources
Helixi212 – 22413Combined sources
Beta strandi234 – 2363Combined sources
Helixi243 – 2453Combined sources
Turni247 – 2493Combined sources
Helixi254 – 2563Combined sources
Helixi258 – 28528Combined sources
Turni286 – 2883Combined sources
Beta strandi292 – 2965Combined sources
Turni302 – 3054Combined sources
Helixi310 – 3156Combined sources
Helixi327 – 3348Combined sources
Turni335 – 3373Combined sources
Beta strandi339 – 3424Combined sources
Helixi349 – 3513Combined sources
Helixi354 – 3563Combined sources
Helixi360 – 37314Combined sources
Beta strandi378 – 3814Combined sources
Helixi389 – 39911Combined sources
Beta strandi406 – 4094Combined sources
Beta strandi415 – 4206Combined sources
Helixi424 – 4274Combined sources
Helixi429 – 44214Combined sources
Turni443 – 4453Combined sources
Helixi452 – 4554Combined sources
Helixi471 – 4766Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

Phylogenomic databases

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

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:
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.
PIRi A29291. A60473.
RefSeqi NP_001236247.1. NM_001249318.1.
UniGenei Gma.595.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

Phylogenomic databases

InParanoidi P10538.

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: November 26, 2014
This is version 112 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