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Q0JMV4 (AMYC1_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 42. 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 C

EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Alpha-amylase isozyme 1B
Gene names
Name:AMY1B
Synonyms:AMYC
Ordered Locus Names:Os01g0357400, LOC_Os01g25510
ORF Names:P0025H06.22, P0514H03.1
OrganismOryza sativa subsp. japonica (Rice)
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
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 By similarity.

Tissue specificity

In callus, weakly expressed. Ref.1

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. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Sequence caution

The sequence AAA33893.1 differs from that shown. Reason: Frameshift at several positions.

The sequence AAA33893.1 differs from that shown. Reason: Sequencing errors.

The sequence BAD52958.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAD53075.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 348348Alpha-amylase isozyme C
PRO_0000054294

Regions

Region87 – 882Substrate binding By similarity
Region182 – 1876Substrate binding By similarity
Region289 – 2913Substrate binding By similarity

Sites

Metal binding1161Calcium By similarity
Metal binding1881Calcium; via carbonyl oxygen By similarity
Binding site2141Substrate By similarity
Binding site2831Substrate By similarity
Binding site3021Substrate By similarity
Binding site3441Substrate By similarity
Site3031Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0JMV4 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 63D1914555DCE02B

FASTA34838,478
        10         20         30         40         50         60 
MQVPIEHNGG EQTLLVPFRA HRPPRPLLQL GSRASPVSGF QLGVVEGEWR VVQPAYGQAR 

        70         80         90        100        110        120 
WTTSPPPASP TSGSLRRPTL SASKATCWGG CTIWTRPIIE AFHGKGVQVI ADIVINHRTA 

       130        140        150        160        170        180 
EHKDSRGIYC RLPPRLGPAH DLPRRPLRRR HRKPGHRRRT STTSTSASSG SSSAGSTGSR 

       190        200        210        220        230        240 
WTSASTRGAS TSPRATPPTW QRSTSMPPSR ASPWPRYGRR WRTAGTASRT TTRTRTGRSW 

       250        260        270        280        290        300 
STGSIVSAAP TAMPRRSTSP PRASSTSPWR AIELWRLRGE DGKAPGMIGW WPAKATTFVD 

       310        320        330        340 
NHDTGNPCIF YDHFFDWGLK DEIERLVSIR NRQGIHPARG RCCWLLPS 

« Hide

References

« Hide 'large scale' references
[1]"Structural organization and differential expression of rice alpha-amylase genes."
Huang N., Koizumi N., Reinl S.J., Rodriguez R.L.
Nucleic Acids Res. 18:7007-7014(1990) [PubMed: 2263460] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: cv. M202.
Tissue: Etiolated leaf.
[2]"The genome sequence and structure of rice chromosome 1."
Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y., Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H., Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M. expand/collapse author list , Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S., Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H., Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S., Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y., Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S., Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H., Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.
Nature 420:312-316(2002) [PubMed: 12447438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[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]"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.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59350 Genomic DNA. Translation: AAA33893.1. Sequence problems.
AP003275 Genomic DNA. Translation: BAD52958.1. Sequence problems.
AP003312 Genomic DNA. Translation: BAD53075.1. Sequence problems.
AP008207 Genomic DNA. Translation: BAF04924.1.
AK063489 mRNA. No translation available.
RefSeqNP_001043010.1. NM_001049545.1.
UniGeneOs.79285.

3D structure databases

ProteinModelPortalQ0JMV4.
SMRQ0JMV4. Positions 96-130, 273-336.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4326017.
KEGGosa:4326017.

Organism-specific databases

GrameneP27940.

Phylogenomic databases

PhylomeDBQ0JMV4.

Family and domain databases

InterProIPR015902. Alpha_amylase.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMYC1_ORYSJ
AccessionPrimary (citable) accession number: Q0JMV4
Secondary accession number(s): P27940, Q5ZBK1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: October 3, 2006
Last modified: December 14, 2011
This is version 42 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