AMY3B_ORYSJ
ID AMY3B_ORYSJ Reviewed; 438 AA.
AC P27937; A0A0N7KQX6; A3BZJ9; Q67U03;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Alpha-amylase isozyme 3B;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P00693};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
GN Name=AMY1.6; Synonyms=AMY3B;
GN OrderedLocusNames=Os09g0457600 {ECO:0000305}, LOC_Os09g28420 {ECO:0000305};
GN ORFNames=B1045B05.10, OsJ_29630 {ECO:0000312|EMBL:EAZ44988.1};
OS Oryza sativa subsp. japonica (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=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. M202; TISSUE=Etiolated leaf;
RX PubMed=1714318; DOI=10.1007/bf00023423;
RA Sutliff T.D., Huang N., Litts J.C., Rodriguez R.L.;
RT "Characterization of an alpha-amylase multigene cluster in rice.";
RL Plant Mol. Biol. 16:579-591(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sutliff T.D., Huang N., Rodriguez R.L.;
RT "Isolation and characterization of a rice alpha-amylase multigene locus.";
RL Submitted (MAY-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
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).
RN [7]
RP NUCLEOTIDE SEQUENCE OF 372-438.
RX PubMed=1339378; DOI=10.1016/0378-1119(92)90212-8;
RA Yu S.M., Tzou W.S., Lo W.S., Kuo Y.H., Lee H.T., Wu R.;
RT "Regulation of alpha-amylase-encoding gene expression in germinating seeds
RT and cultured cells of rice.";
RL Gene 122:247-253(1992).
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; Evidence={ECO:0000250|UniProtKB:P00693};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P00693};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:P00693};
CC -!- SUBUNIT: Monomer.
CC -!- TISSUE SPECIFICITY: Germinating seeds.
CC -!- DEVELOPMENTAL STAGE: Expressed at a high level during germination in
CC the aleurones cells under the control of the plant hormone gibberellic
CC acid and in the developing grains at a low level.
CC -!- MISCELLANEOUS: Binds starch not only at the active site, but also via
CC accessory binding sites on the protein surface that are important for
CC efficient binding to starch granules and thereby increase enzyme
CC activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; X56337; CAA39777.1; -; Genomic_DNA.
DR EMBL; M24941; AAA33897.1; -; Genomic_DNA.
DR EMBL; AP005891; BAD38368.1; -; Genomic_DNA.
DR EMBL; AP008215; BAH94599.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT08442.1; -; Genomic_DNA.
DR EMBL; CM000146; EAZ44988.1; -; Genomic_DNA.
DR PIR; S14957; S14957.
DR RefSeq; XP_015612113.1; XM_015756627.1.
DR AlphaFoldDB; P27937; -.
DR SMR; P27937; -.
DR STRING; 4530.OS09T0457600-00; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; P27937; -.
DR PRIDE; P27937; -.
DR EnsemblPlants; Os09t0457600-00; Os09t0457600-00; Os09g0457600.
DR GeneID; 9271949; -.
DR Gramene; Os09t0457600-00; Os09t0457600-00; Os09g0457600.
DR KEGG; osa:9271949; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_030069_1_0_1; -.
DR InParanoid; P27937; -.
DR OMA; HPFGLAC; -.
DR OrthoDB; 665362at2759; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000007752; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR ExpressionAtlas; P27937; differential.
DR Genevisible; P27937; OS.
DR GO; GO:0004556; F:alpha-amylase activity; ISS:Gramene.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005983; P:starch catabolic process; ISS:Gramene.
DR GO; GO:0005987; P:sucrose catabolic process; ISS:Gramene.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR012850; A-amylase_bs_C.
DR InterPro; IPR013775; A-amylase_pln.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF07821; Alpha-amyl_C2; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001028; Alph-amls_plant; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00810; Alpha-amyl_C2; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..438
FT /note="Alpha-amylase isozyme 3B"
FT /id="PRO_0000001413"
FT ACT_SITE 205
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT ACT_SITE 230
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 70..72
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 77..78
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 203..208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 299..301
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 402..404
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 414..420
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 424
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT SITE 313
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00693"
SQ SEQUENCE 438 AA; 48592 MW; B9DE0DB5ABC63F9C CRC64;
MAKRIASMSS LLLIALLCLS SHLAQAQVLF QGFNWESWKK QGGWYNFLHG HVDDIAATGV
THVWLPPPSH SVAPQGYMPG RLYDLDASKY GTGAELRSLI AAFHSKGIKC VADIVINHRC
ADYKDSRGIY CIFEGGTPDS RLDWGPDMIC SDDTQYSNGR GHRDTGADFG AAPDIDHLNT
RVQTELSDWL NWLKSDVGFD GWRLDFAKGY SAAVAKTYVD NTDPSFVVAE IWSNMRYDGN
GEPSWNQDGD RQELVNWAQA VGGPASAFDF TTKGELQAAV QGELWRMKDG NGKAPGMIGW
LPEKAVTFID NHDTGSTQNS WPFPSDKVMQ GYAYILTHPG VPCIFYDHVF DWNLKQEIST
LAAVRSRNEI HPGSKLKILA AEGDVYVAMI DDKVITKIGT RYDVGNLIPS DFHVVAHGNN
YCIWEKSGLR VPAGRHHY
