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Protein

Beta-amylase

Gene

BMY1

Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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

PTM databases

iPTMnetiP10538

Interactioni

Subunit structurei

Monomer.

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

InterProiView protein in InterPro
IPR001554 Glyco_hydro_14
IPR018238 Glyco_hydro_14_CS
IPR001371 Glyco_hydro_14B_pln
IPR017853 Glycoside_hydrolase_SF
PANTHERiPTHR31352 PTHR31352, 1 hit
PfamiView protein in Pfam
PF01373 Glyco_hydro_14, 1 hit
PRINTSiPR00750 BETAAMYLASE
PR00842 GLHYDLASE14B
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS00506 BETA_AMYLASE_1, 1 hit
PS00679 BETA_AMYLASE_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiAMYB_SOYBN
AccessioniPrimary (citable) accession number: P10538
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 128 of the entry and version 3 of the sequence. See 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

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