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P27939 (AMY3C_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 3C
EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:AMY1.7
Synonyms:AMY3B
Ordered Locus Names:Os09g0457800, LOC_Os09g28420, LOC_Os09g28430
ORF Names:B1045B05.11, OsJ_29632
OrganismOryza sativa subsp. japonica (Rice)
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length437 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 – 437411Alpha-amylase isozyme 3C
PRO_0000001414

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

Experimental info

Sequence conflict391K → N in CAA39778. Ref.1
Sequence conflict541D → Y in CAA39778. Ref.1
Sequence conflict661P → S in AK101358. Ref.5
Sequence conflict3311G → R in CAA39778. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P27939 [UniParc].

Last modified October 25, 2005. Version 2.
Checksum: 62BBDEF45C14AC78

FASTA43748,504
        10         20         30         40         50         60 
MAKHSTTMSC LLFFVLLCLG SHLAQAQVLF QGFNWESWKK QGGWYNFLHS HVDDIAATGV 

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

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

       190        200        210        220        230        240 
RVQTELSDWL NWLKSDVGFD GWRLDFAKGY SATVAKTYVD 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 
LAAVRSRNGI HPGSKLNILA ADGDVYVAMI DDKVITKIGT RYDVGNLIPS DFHVVAHGNN 

       430 
YCVWEKSGLR VPAGRRH

« 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]"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.
[3]"The rice annotation project database (RAP-DB): 2008 update."
The rice annotation project (RAP)
Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed: 18089549] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: cv. Nipponbare.
[4]"The genomes of Oryza sativa: a history of duplications."
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. expand/collapse author list , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
PLoS Biol. 3:266-281(2005) [PubMed: 15685292] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[5]"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."
The rice full-length cDNA consortium
Science 301:376-379(2003) [PubMed: 12869764] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Nipponbare.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X56338 Genomic DNA. Translation: CAA39778.1.
AP005891 Genomic DNA. Translation: BAD38369.1.
AP008215 Genomic DNA. Translation: BAF25283.1.
CM000146 Genomic DNA. Translation: EAZ44990.1.
AK101358 mRNA. No translation available.
PIRS14956.
RefSeqNP_001063369.1. NM_001069904.1.
UniGeneOs.79418.

3D structure databases

ProteinModelPortalP27939.
SMRP27939. Positions 27-426.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PRIDEP27939.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4347265.
KEGGosa:4347265.

Organism-specific databases

GrameneP27939.

Phylogenomic databases

GeneTreeEPGT00070000028585.
PhylomeDBP27939.
ProtClustDBCLSN2697397.

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 nameAMY3C_ORYSJ
AccessionPrimary (citable) accession number: P27939
Secondary accession number(s): Q0J182, Q67U02
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 25, 2005
Last modified: December 14, 2011
This is version 92 of the entry and version 2 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

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