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P27937 (AMY3B_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-amylase isozyme 3B

EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:AMY1.6
Synonyms:AMY3B
Ordered Locus Names:Os09g0457600, LOC_Os09g28420
ORF Names:B1045B05.10
OrganismOryza sativa subsp. japonica (Rice)
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Important for breakdown of endosperm starch during germination.

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

Cofactor

Binds 3 calcium ions per subunit By similarity.

Subunit structure

Monomer.

Tissue specificity

Germinating seeds.

Developmental stage

Expressed at a high level during germination in the aleurones cells under the control of the plant hormone gibberellic acid and in the developing grains at a low level.

Miscellaneous

Binds starch not only at the active site, but also via accessory binding sites on the protein surface that are important for efficient binding to starch granules and thereby increase enzyme activity By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalpha-amylase activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 438412Alpha-amylase isozyme 3B
PRO_0000001413

Regions

Region77 – 782Substrate binding By similarity
Region203 – 2086Substrate binding By similarity
Region299 – 3013Substrate binding By similarity
Region402 – 4043Substrate binding By similarity

Sites

Active site2051Nucleophile By similarity
Active site2301Proton donor By similarity
Metal binding1171Calcium 1 By similarity
Metal binding1341Calcium 2 By similarity
Metal binding1371Calcium 2; via carbonyl oxygen By similarity
Metal binding1391Calcium 2; via carbonyl oxygen By similarity
Metal binding1431Calcium 2 By similarity
Metal binding1531Calcium 3 By similarity
Metal binding1641Calcium 1 By similarity
Metal binding1671Calcium 1; via carbonyl oxygen By similarity
Metal binding1681Calcium 3 By similarity
Metal binding1691Calcium 3; via carbonyl oxygen By similarity
Metal binding1721Calcium 3; via carbonyl oxygen By similarity
Metal binding1741Calcium 1 By similarity
Metal binding1741Calcium 3 By similarity
Metal binding2091Calcium 1; via carbonyl oxygen By similarity
Binding site2321Substrate By similarity
Binding site2341Substrate By similarity
Binding site2521Substrate By similarity
Binding site2931Substrate By similarity
Binding site3121Substrate By similarity
Binding site3181Substrate By similarity
Binding site3971Substrate By similarity
Binding site4241Substrate By similarity
Site3131Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
P27937 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: B9DE0DB5ABC63F9C

FASTA43848,592
        10         20         30         40         50         60 
MAKRIASMSS LLLIALLCLS SHLAQAQVLF QGFNWESWKK QGGWYNFLHG HVDDIAATGV 

        70         80         90        100        110        120 
THVWLPPPSH SVAPQGYMPG RLYDLDASKY GTGAELRSLI AAFHSKGIKC VADIVINHRC 

       130        140        150        160        170        180 
ADYKDSRGIY CIFEGGTPDS RLDWGPDMIC SDDTQYSNGR GHRDTGADFG AAPDIDHLNT 

       190        200        210        220        230        240 
RVQTELSDWL NWLKSDVGFD GWRLDFAKGY SAAVAKTYVD NTDPSFVVAE IWSNMRYDGN 

       250        260        270        280        290        300 
GEPSWNQDGD RQELVNWAQA VGGPASAFDF TTKGELQAAV QGELWRMKDG NGKAPGMIGW 

       310        320        330        340        350        360 
LPEKAVTFID NHDTGSTQNS WPFPSDKVMQ GYAYILTHPG VPCIFYDHVF DWNLKQEIST 

       370        380        390        400        410        420 
LAAVRSRNEI HPGSKLKILA AEGDVYVAMI DDKVITKIGT RYDVGNLIPS DFHVVAHGNN 

       430 
YCIWEKSGLR VPAGRHHY 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of an alpha-amylase multigene cluster in rice."
Sutliff T.D., Huang N., Litts J.C., Rodriguez R.L.
Plant Mol. Biol. 16:579-591(1991) [PubMed: 1714318] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. M202.
Tissue: Etiolated leaf.
[2]"Isolation and characterization of a rice alpha-amylase multigene locus."
Sutliff T.D., Huang N., Rodriguez R.L.
Submitted (MAY-1989) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The map-based sequence of the rice genome."
International rice genome sequencing project (IRGSP)
Nature 436:793-800(2005) [PubMed: 16100779] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[4]"Regulation of alpha-amylase-encoding gene expression in germinating seeds and cultured cells of rice."
Yu S.M., Tzou W.S., Lo W.S., Kuo Y.H., Lee H.T., Wu R.
Gene 122:247-253(1992) [PubMed: 1339378] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 372-438.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56337 Genomic DNA. Translation: CAA39777.1.
M24941 Genomic DNA. Translation: AAA33897.1.
AP005891 Genomic DNA. Translation: BAD38368.1.
PIRS14957.
RefSeqNP_001175871.1. NM_001188942.1.
UniGeneOs.87660.

3D structure databases

ProteinModelPortalP27937.
SMRP27937. Positions 27-426.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID9271949.
KEGGosa:9271949.

Organism-specific databases

GrameneP27937.

Phylogenomic databases

PhylomeDBP27937.

Family and domain databases

InterProIPR012850. A-amylase_bs_C.
IPR013775. A-amylase_pln.
IPR015902. Alpha_amylase.
IPR006046. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PfamPF07821. Alpha-amyl_C2. 1 hit.
PF00128. Alpha-amylase. 1 hit.
[Graphical view]
PIRSFPIRSF001028. Alph-amls_plant. 1 hit.
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
SM00810. Alpha-amyl_C2. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMY3B_ORYSJ
AccessionPrimary (citable) accession number: P27937
Secondary accession number(s): Q67U03
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: December 14, 2011
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

SIMILARITY comments

Index of protein domains and families