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Protein

Beta-amylase

Gene

BMY1

Organism
Ipomoea batatas (Sweet potato) (Convolvulus batatas)
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.

pH dependencei

Optimum pH is 5-6.

Temperature dependencei

Optimum temperature is 50-55 degrees Celsius.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei55SubstrateBy similarity1
Binding sitei95SubstrateBy similarity1
Binding sitei103SubstrateBy similarity1
Active sitei188Proton donorPROSITE-ProRule annotation1
Binding sitei298SubstrateBy similarity1
Binding sitei303SubstrateBy similarity1
Binding sitei345SubstrateBy similarity1
Active sitei383Proton acceptorBy similarity1
Binding sitei423SubstrateBy similarity1

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. 2773.

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
OrganismiIpomoea batatas (Sweet potato) (Convolvulus batatas)
Taxonomic identifieri4120 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesConvolvulaceaeIpomoeeaeIpomoea

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001539342 – 499Beta-amylaseAdd BLAST498

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1499
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 12Combined sources3
Beta strandi15 – 19Combined sources5
Beta strandi27 – 29Combined sources3
Helixi34 – 46Combined sources13
Beta strandi51 – 57Combined sources7
Helixi58 – 61Combined sources4
Helixi72 – 83Combined sources12
Beta strandi87 – 93Combined sources7
Helixi111 – 116Combined sources6
Turni117 – 119Combined sources3
Helixi121 – 123Combined sources3
Beta strandi124 – 126Combined sources3
Beta strandi132 – 137Combined sources6
Helixi139 – 141Combined sources3
Beta strandi145 – 147Combined sources3
Helixi152 – 166Combined sources15
Helixi168 – 173Combined sources6
Beta strandi176 – 181Combined sources6
Helixi185 – 187Combined sources3
Beta strandi188 – 190Combined sources3
Helixi196 – 198Combined sources3
Helixi213 – 224Combined sources12
Turni225 – 227Combined sources3
Helixi236 – 238Combined sources3
Helixi245 – 247Combined sources3
Beta strandi249 – 252Combined sources4
Helixi256 – 258Combined sources3
Helixi260 – 288Combined sources29
Beta strandi294 – 299Combined sources6
Turni304 – 307Combined sources4
Helixi312 – 317Combined sources6
Helixi329 – 337Combined sources9
Beta strandi341 – 345Combined sources5
Helixi351 – 353Combined sources3
Helixi356 – 358Combined sources3
Helixi362 – 375Combined sources14
Beta strandi380 – 383Combined sources4
Helixi391 – 401Combined sources11
Beta strandi417 – 422Combined sources6
Helixi426 – 429Combined sources4
Helixi431 – 444Combined sources14
Turni445 – 447Combined sources3
Turni452 – 454Combined sources3
Helixi471 – 476Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FA2X-ray2.30A2-499[»]
ProteinModelPortaliP10537.
SMRiP10537.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10537.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni384 – 385Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 14 family.Curated

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.

P10537-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPIPGVMPI GNYVSLYVML PLGVVNADNV FPDKEKVEDE LKQVKAGGCD
60 70 80 90 100
GVMVDVWWGI IEAKGPKQYD WSAYRELFQL VKKCGLKIQA IMSFHQCGGN
110 120 130 140 150
VGDAVFIPIP QWILQIGDKN PDIFYTNRAG NRNQEYLSLG VDNQRLFQGR
160 170 180 190 200
TALEMYRDFM ESFRDNMADF LKAGDIVDIE VGCGAAGELR YPSYPETQGW
210 220 230 240 250
VFPGIGEFQC YDKYMVADWK EAVKQAGNAD WEMPGKGAGT YNDTPDKTEF
260 270 280 290 300
FRPNGTYKTD MGKFFLTWYS NKLIIHGDQV LEEANKVFVG LRVNIAAKVS
310 320 330 340 350
GIHWWYNHVS HAAELTAGFY NVAGRDGYRP IARMLARHHA TLNFTCLEMR
360 370 380 390 400
DSEQPAEAKS APQELVQQVL SSGWKEYIDV AGENALPRYD ATAYNQMLLN
410 420 430 440 450
VRPNGVNLNG PPKLKMSGLT YLRLSDDLLQ TDNFELFKKF VKKMHADLDP
460 470 480 490
SPNAISPAVL ERSNSAITID ELMEATKGSR PFPWYDVTDM PVDGSNPFD
Length:499
Mass (Da):56,080
Last modified:January 23, 2007 - v4
Checksum:iB1F47E9D0FEA92F1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti238A → T in BAA02286 (PubMed:1383095).Curated1
Sequence conflicti257 – 264YKTDMGKF → LQDGYGQV in BAA00828 (PubMed:1837016).Curated8
Sequence conflicti372 – 374SGW → RQV in BAA00828 (PubMed:1837016).Curated3
Sequence conflicti397M → I in BAA02286 (PubMed:1383095).Curated1
Sequence conflicti400 – 401NV → KL in BAA00828 (PubMed:1837016).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D01022 mRNA. Translation: BAA00828.1.
D12882 Genomic DNA. Translation: BAA02286.1.
PIRiJC1447.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D01022 mRNA. Translation: BAA00828.1.
D12882 Genomic DNA. Translation: BAA02286.1.
PIRiJC1447.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FA2X-ray2.30A2-499[»]
ProteinModelPortaliP10537.
SMRiP10537.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH14. Glycoside Hydrolase Family 14.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.2. 2773.

Miscellaneous databases

EvolutionaryTraceiP10537.

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_IPOBA
AccessioniPrimary (citable) accession number: P10537
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 109 of the entry and version 4 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.