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Reviewed, UniProtKB/Swiss-Prot P10537 (AMYB_IPOBA)

Last modified June 16, 2009. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Beta-amylase
    EC=3.2.1.2
Alternative name(s):
    1,4-alpha-D-glucan maltohydrolase
Gene names
Name: BMY1
Synonyms: AMYB
OrganismIpomoea batatas (Sweet potato) (Batate)
Taxonomic identifier4120 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Convolvulaceae › Ipomoeeae › Ipomoea

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Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the glycosyl hydrolase 14 family.

biophysicochemical properties

pH dependence:

Optimum pH is 5-6.

Temperature dependence:

Optimum temperature is 50-55 degrees Celsius.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processpolysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbeta-amylase activity

Inferred from electronic annotation. Source: EC

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 499498Beta-amylase
PRO_0000153934

Sites

Active site1881 Ref.3
Active site3831 By similarity

Experimental info

Sequence conflict2381A → T in BAA02286. Ref.2
Sequence conflict257 – 2648YKTDMGKF → LQDGYGQV in BAA00828. Ref.1
Sequence conflict372 – 3743SGW → RQV in BAA00828. Ref.1
Sequence conflict3971M → I in BAA02286. Ref.2
Sequence conflict400 – 4012NV → KL in BAA00828. Ref.1

Secondary structure

1 ................................................................................... 499
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P10537-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: B1F47E9D0FEA92F1

FASTA49956,080
        10         20         30         40         50         60 
MAPIPGVMPI GNYVSLYVML PLGVVNADNV FPDKEKVEDE LKQVKAGGCD GVMVDVWWGI 

        70         80         90        100        110        120 
IEAKGPKQYD WSAYRELFQL VKKCGLKIQA IMSFHQCGGN VGDAVFIPIP QWILQIGDKN 

       130        140        150        160        170        180 
PDIFYTNRAG NRNQEYLSLG VDNQRLFQGR TALEMYRDFM ESFRDNMADF LKAGDIVDIE 

       190        200        210        220        230        240 
VGCGAAGELR YPSYPETQGW VFPGIGEFQC YDKYMVADWK EAVKQAGNAD WEMPGKGAGT 

       250        260        270        280        290        300 
YNDTPDKTEF FRPNGTYKTD MGKFFLTWYS NKLIIHGDQV LEEANKVFVG LRVNIAAKVS 

       310        320        330        340        350        360 
GIHWWYNHVS HAAELTAGFY NVAGRDGYRP IARMLARHHA TLNFTCLEMR DSEQPAEAKS 

       370        380        390        400        410        420 
APQELVQQVL SSGWKEYIDV AGENALPRYD ATAYNQMLLN VRPNGVNLNG PPKLKMSGLT 

       430        440        450        460        470        480 
YLRLSDDLLQ TDNFELFKKF VKKMHADLDP SPNAISPAVL ERSNSAITID ELMEATKGSR 

       490 
PFPWYDVTDM PVDGSNPFD

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References

[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: 1837016] [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: 1383095] [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: 8103452] [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: 7777485] [Abstract]
Cited for: CRYSTALLIZATION, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

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Cross-references

Sequence databases

D01022 mRNA. Translation: BAA00828.1.
D12882 Genomic DNA. Translation: BAA02286.1.
PIRJC1447.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1FA2X-ray2.30A2-499[»]
ModBaseSearch...

Protein family/group databases

CAZyGH14. Glycoside Hydrolase Family 14.

Enzyme and pathway databases

BRENDA3.2.1.2. 21210.

Family and domain databases

InterProIPR001554. Glyco_hydro_14.
IPR018238. Glyco_hydro_14_CS.
IPR001371. Glyco_hydro_14B_pln.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF01373. Glyco_hydro_14. 1 hit.
[Graphical view]
PRINTSPR00750. BETAAMYLASE.
PR00842. GLHYDLASE14B.
PROSITEPS00506. BETA_AMYLASE_1. 1 hit.
PS00679. BETA_AMYLASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAMYB_IPOBA
AccessionPrimary (citable) accession number: P10537
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 85 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents