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Reviewed, UniProtKB/Swiss-Prot P30271 (AMYB_SECCE)

Last modified June 16, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 · Cross-references · Entry information · Relevant documents

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
OrganismSecale cereale (Rye)
Taxonomic identifier4550 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeSecale

Protein attributes

Sequence length222 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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.

Sequence similarities

Belongs to the glycosyl hydrolase 14 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 222›222Beta-amylase
PRO_0000153937

Sites

Active site741 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P30271-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 29A66E6EA5C0F718

FASTA22224,349
        10         20         30         40         50         60 
SHAAEVTAGY YNLHDRDDYR PIARMLTRHH ASLNFTCAEM RDSEQSSQAM SAPEELVQQV 

        70         80         90        100        110        120 
WSAGWREGLN IACENALPRY DPTAYNTILR NARPHGINHS SPTEHKLFGF TYLRLSNQLL 

       130        140        150        160        170        180 
EGQNYVNFKT FVDRMHANLP HDPSVDPVAP LQRSGPEIPI EVILQAAQPK LDPFPFEDHT 

       190        200        210        220 
DLPVQCLGGI GGGEVECPAG GIGGEVQQDP TGGMGGELPP AV 

« Hide

References

[1]"Characterization of cDNA clones for rye endosperm beta-amylase and analysis of beta-amylase deficiency in rye mutant lines."
Rorat T., Sadowski J., Grellet F., Daussant J., Delseny M.
Theor. Appl. Genet. 83:257-263(1991) [Agricola: IND92007634]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Endosperm.

Cross-references

Sequence databases

X56785 mRNA. Translation: CAA40105.1.
PIRS38779.

3D structure databases

HSSPHSSP built from PDB template 1B1Y based on UniProtKB P16098.
SMRP30271. Positions 1-200.
ModBaseSearch...

Protein family/group databases

CAZyGH14. Glycoside Hydrolase Family 14.

Organism-specific databases

GrameneP30271.

Enzyme and pathway databases

BRENDA3.2.1.2. 1472.

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. Partial match.
PS00679. BETA_AMYLASE_2. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMYB_SECCE
AccessionPrimary (citable) accession number: P30271
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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