A2YGY2 (AMY2A_ORYSI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-amylase isozyme 2A
EC=3.2.1.1

Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Alpha-amylase isozyme C2

Gene names

Name:	AMYC2
Synonyms:	AMY1.5, AMY2A
ORF Names:	OsI_023575

Organism

Oryza sativa subsp. indica (Rice)

Taxonomic identifier

39946 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	446 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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.
Sequence caution	The sequence CAA45903.1 differs from that shown. Reason: Frameshift at position 428.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 446	425	Alpha-amylase isozyme 2A		PRO_0000291430
Regions
	Region	73 – 74	2	Substrate binding By similarity
	Region	200 – 205	6	Substrate binding By similarity
	Region	300 – 302	3	Substrate binding By similarity
	Region	403 – 405	3	Substrate binding By similarity
Sites
	Active site	202	1	Nucleophile By similarity
	Active site	228	1	Proton donor By similarity
	Metal binding	113	1	Calcium 1 By similarity
	Metal binding	130	1	Calcium 2 By similarity
	Metal binding	133	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	135	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	139	1	Calcium 2 By similarity
	Metal binding	149	1	Calcium 3 By similarity
	Metal binding	160	1	Calcium 1 By similarity
	Metal binding	163	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	164	1	Calcium 3 By similarity
	Metal binding	165	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	168	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	170	1	Calcium 1 By similarity
	Metal binding	170	1	Calcium 3 By similarity
	Metal binding	206	1	Calcium 1; via carbonyl oxygen By similarity
	Binding site	230	1	Substrate By similarity
	Binding site	232	1	Substrate By similarity
	Binding site	250	1	Substrate By similarity
	Binding site	257	1	Substrate By similarity
	Binding site	294	1	Substrate By similarity
	Binding site	313	1	Substrate By similarity
	Binding site	319	1	Substrate By similarity
	Binding site	398	1	Substrate By similarity
	Binding site	425	1	Substrate By similarity
	Site	314	1	Transition state stabilizer By similarity
Experimental info
	Sequence conflict	2	1	A → R in CAA45903. Ref.1
	Sequence conflict	416 – 421	6	AAHGNG → RPWP in CAA45903. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	A2YGY2 [UniParc]. Last modified March 20, 2007. Version 1. Checksum: EA5876EDC6DB0051	FASTA	446	48,741
	10 20 30 40 50 60 MATGRRLSMI LLLLLLGLAS GDKILFQGFN WESWRQSGGW YNLLMGKVDD IVAAGVTHVW 70 80 90 100 110 120 LPPPSHSVST QGYMPGRLYD LDASRYGTSM ELKSLISALH GKGIQAIADV VINHRCADYK 130 140 150 160 170 180 DSRGIYCIFE GGTPDGRLDW GPHMICRDDT QFSDGTGNLD TGADFAAAPD IDHLNGVVQR 190 200 210 220 230 240 ELTDWLLWLK SDEVGFDAWR LDFARGYSPE VAKVYIEGTT PVGLAVAELW DSMAYGGDGK 250 260 270 280 290 300 PEYNQDAHRQ ALVDWVDRVG GTASAGMVFD FTTKGIMNTA VEGELWRLID QQGKAPGVIG 310 320 330 340 350 360 WWPAKAVTFV DNHDTGSTQQ MWPFPSDKVM QGYAYILTHP GNPCIFYDHF FDWGLKEQIA 370 380 390 400 410 420 ALVAVRQRNG VTATSSLKIM LHDADAYVAE IDGKVVMKIG SRYDVSSLIP PGFHLAAHGN 430 440 GYAVWEKSAA AAAAAADHRT SSSASL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Goldman S., Mawal Y., Wu R. Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. IR26. Tissue: Seed.
[2]	"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. , 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. 93-11.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X64619 mRNA. Translation: CAA45903.1. Frameshift. CM000131 Genomic DNA. Translation: EAZ02343.1.
PIR	S19990.
UniGene	Os.50953.
3D structure databases
ProteinModelPortal	A2YGY2.
SMR	A2YGY2. Positions 23-427.
ModBase	Search...
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
Gramene	P27935.
Phylogenomic databases
GeneTree	EPGT00070000028585.
HOGENOM	HBG318585.
PhylomeDB	A2YGY2.
Family and domain databases
InterPro	IPR012850. 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]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHER	PTHR10357. Alpha_amylase. 1 hit.
Pfam	PF07821. Alpha-amyl_C2. 1 hit. PF00128. Alpha-amylase. 1 hit. [Graphical view]
PIRSF	PIRSF001028. Alph-amls_plant. 1 hit.
PRINTS	PR00110. ALPHAAMYLASE.
SMART	SM00642. Aamy. 1 hit. SM00810. Alpha-amyl_C2. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AMY2A_ORYSI

Accession

Primary (citable) accession number: A2YGY2
Secondary accession number(s): P27935, P27941, Q5Z7T8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	March 20, 2007
Last modified:	December 14, 2011
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program