AMYC1_ORYSI
ID AMYC1_ORYSI Reviewed; 348 AA.
AC A2WPU3; P27940; Q5ZBK1;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Alpha-amylase isozyme C;
DE EC=3.2.1.1;
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE AltName: Full=Alpha-amylase isozyme 1B;
GN Name=AMYC; Synonyms=AMY1B; ORFNames=OsI_001836;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. IR26; TISSUE=Leaf;
RX PubMed=1731997; DOI=10.1007/bf00034966;
RA Kim J.-K., Wu R.;
RT "Nucleotide sequence of a high-pI rice (Oryza sativa) -amylase gene.";
RL Plant Mol. Biol. 18:399-402(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Important for breakdown of endosperm starch during
CC germination.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA36485.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA36485.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; X52240; CAA36485.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S19142; ALRZOC.
DR AlphaFoldDB; A2WPU3; -.
DR SMR; A2WPU3; -.
DR STRING; 39946.A2WPU3; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR Proteomes; UP000007015; Chromosome 1.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..348
FT /note="Alpha-amylase isozyme C"
FT /id="PRO_0000291431"
FT REGION 126..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..159
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87..88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 182..187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 289..291
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 303
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 348 AA; 38508 MW; 63D5C04555DCE02B CRC64;
MQVPIEHNGG EQTLLVPFRA HRPPRPLLQL GSRASPVSGF QLGVVEGEWR VVQPAYGQAR
WTTSPPPASP TSGSLRRPTL SASKATCWGG CTIWTRPIIE AFHGKGVQVI ADIVINHRTA
EHKDSRGIYC RLPPRLGPAH DLPRRPLRRR HRKPGHRRRT STTSTSASSG SSSAGSTGSR
WTSASTRGAS TSPRATPPTW QRSTSMPPSR ASPWPRYGRR WRTAGTASRT TTRTRTGRSW
STGSIVSAAP TAMPRRSTSP PRASSTSPWR AIELWRLRGE DGKAPGMIGW WPAKATTFVD
NHDTGNPCIF YDHFFDWGLK DEIERLVSIR NRQGIHPAWG RCCWLLPS
