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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei55 – 551SubstrateBy similarity
Binding sitei95 – 951SubstrateBy similarity
Binding sitei103 – 1031SubstrateBy similarity
Active sitei188 – 1881Proton donorPROSITE-ProRule annotation
Binding sitei298 – 2981SubstrateBy similarity
Binding sitei303 – 3031SubstrateBy similarity
Binding sitei345 – 3451SubstrateBy similarity
Active sitei383 – 3831Proton acceptorBy similarity
Binding sitei423 – 4231SubstrateBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 499498Beta-amylasePRO_0000153934Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
499
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 123Combined sources
Beta strandi15 – 195Combined sources
Beta strandi27 – 293Combined sources
Helixi34 – 4613Combined sources
Beta strandi51 – 577Combined sources
Helixi58 – 614Combined sources
Helixi72 – 8312Combined sources
Beta strandi87 – 937Combined sources
Helixi111 – 1166Combined sources
Turni117 – 1193Combined sources
Helixi121 – 1233Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi132 – 1376Combined sources
Helixi139 – 1413Combined sources
Beta strandi145 – 1473Combined sources
Helixi152 – 16615Combined sources
Helixi168 – 1736Combined sources
Beta strandi176 – 1816Combined sources
Helixi185 – 1873Combined sources
Beta strandi188 – 1903Combined sources
Helixi196 – 1983Combined sources
Helixi213 – 22412Combined sources
Turni225 – 2273Combined sources
Helixi236 – 2383Combined sources
Helixi245 – 2473Combined sources
Beta strandi249 – 2524Combined sources
Helixi256 – 2583Combined sources
Helixi260 – 28829Combined sources
Beta strandi294 – 2996Combined sources
Turni304 – 3074Combined sources
Helixi312 – 3176Combined sources
Helixi329 – 3379Combined sources
Beta strandi341 – 3455Combined sources
Helixi351 – 3533Combined sources
Helixi356 – 3583Combined sources
Helixi362 – 37514Combined sources
Beta strandi380 – 3834Combined sources
Helixi391 – 40111Combined sources
Beta strandi417 – 4226Combined sources
Helixi426 – 4294Combined sources
Helixi431 – 44414Combined sources
Turni445 – 4473Combined sources
Turni452 – 4543Combined sources
Helixi471 – 4766Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FA2X-ray2.30A2-499[»]
ProteinModelPortaliP10537.
SMRiP10537. Positions 2-499.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10537.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni384 – 3852Substrate bindingBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381A → T in BAA02286 (PubMed:1383095).Curated
Sequence conflicti257 – 2648YKTDMGKF → LQDGYGQV in BAA00828 (PubMed:1837016).Curated
Sequence conflicti372 – 3743SGW → RQV in BAA00828 (PubMed:1837016).Curated
Sequence conflicti397 – 3971M → I in BAA02286 (PubMed:1383095).Curated
Sequence conflicti400 – 4012NV → KL in BAA00828 (PubMed:1837016).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1FA2X-ray2.30A2-499[»]
ProteinModelPortaliP10537.
SMRiP10537. Positions 2-499.
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...

Publicationsi

  1. "Molecular cloning and expression in Escherichia coli of cDNA encoding the subunit of sweet potato beta-amylase."
    Yoshida N., Nakamura K.
    J. Biochem. 110:196-201(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: cv. Kokei No. 14.
    Tissue: Tuberous root.
  2. "A nuclear gene encoding beta-amylase of sweet potato."
    Yoshida N., Hayashi K., Nakamura K.
    Gene 120:255-259(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sweet potato beta-amylase. Primary structure and identification of the active-site glutamyl residue."
    Toda H., Nitta Y., Asanami S., Kim J.P., Sakiyama F.
    Eur. J. Biochem. 216:25-38(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-499, ACTIVE SITE GLU-188.
    Tissue: Tuberous root.
  4. "Crystallization, molecular replacement solution, and refinement of tetrameric beta-amylase from sweet potato."
    Cheong C.G., Eom S.H., Chang C., Shin D.H., Song H.Y., Min K., Moon J.H., Kim K.K., Hwang K.Y., Suh S.W.
    Proteins 21:105-117(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

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: January 20, 2016
This is version 107 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.