ID AMY3E_ORYSJ Reviewed; 437 AA.
AC P27934; Q5QLB2; Q6ZDD6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 27-MAR-2024, entry version 161.
DE RecName: Full=Alpha-amylase isozyme 3E;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P00693};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
GN Name=AMY1.4; Synonyms=AMY3E;
GN OrderedLocusNames=Os08g0473600, LOC_Os08g36900;
GN ORFNames=P0013B04.34-1, P0451G12.3-1;
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=2263460; DOI=10.1093/nar/18.23.7007;
RA Huang N., Koizumi N., Reinl S.J., Rodriguez R.L.;
RT "Structural organization and differential expression of rice alpha-amylase
RT genes.";
RL Nucleic Acids Res. 18:7007-7014(1990).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P27934-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P27934-2; Sequence=VSP_016022, VSP_016023;
CC -!- TISSUE SPECIFICITY: More abundant in germinating seeds than in young
CC roots, young leaves and callus.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD73794.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD73796.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M59352; AAA33896.1; -; Genomic_DNA.
DR EMBL; AP004399; BAD09334.1; -; Genomic_DNA.
DR EMBL; AP004399; BAD73794.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP004457; BAD09374.1; -; Genomic_DNA.
DR EMBL; AP004457; BAD73796.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014964; BAT05857.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT05858.1; -; Genomic_DNA.
DR EMBL; AK064071; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK103413; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; JT0946; JT0946.
DR RefSeq; XP_015650698.1; XM_015795212.1.
DR AlphaFoldDB; P27934; -.
DR SMR; P27934; -.
DR STRING; 39947.P27934; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; 39947-P27934; -.
DR EnsemblPlants; Os08t0473600-01; Os08t0473600-01; Os08g0473600. [P27934-1]
DR EnsemblPlants; Os08t0473600-02; Os08t0473600-02; Os08g0473600. [P27934-2]
DR GeneID; 4345812; -.
DR Gramene; Os08t0473600-01; Os08t0473600-01; Os08g0473600. [P27934-1]
DR Gramene; Os08t0473600-02; Os08t0473600-02; Os08g0473600. [P27934-2]
DR KEGG; osa:4345812; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_030069_1_0_1; -.
DR InParanoid; P27934; -.
DR OMA; PCELACT; -.
DR OrthoDB; 201664at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR ExpressionAtlas; P27934; baseline and differential.
DR Genevisible; P27934; 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 CDD; cd11314; AmyAc_arch_bac_plant_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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 PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF48; ALPHA-AMYLASE ISOZYME 3C; 1.
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; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Carbohydrate metabolism; Glycosidase;
KW Hydrolase; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..437
FT /note="Alpha-amylase isozyme 3E"
FT /id="PRO_0000001416"
FT ACT_SITE 204
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT ACT_SITE 229
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 69..71
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 76..77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 166
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 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 202..207
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P04063"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 298..300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 396
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 401..403
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 413..419
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT SITE 312
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00693"
FT VAR_SEQ 224..233
FT /note="TFVVGEIWSS -> ASWGGCPIRP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_016022"
FT VAR_SEQ 234..437
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_016023"
SQ SEQUENCE 437 AA; 48708 MW; C0E8276CCEA16602 CRC64;
MGKHHVTLCC VVFAVLCLAS SLAQAQVLFQ GFNWESWRKQ GGWYNFLHEK VEEIASTGAT
HVWLPPPSHS VSPQGYMPGR LYDLDASKYG TEAELKSLIE AFHDKNVECL ADIVINHRCA
DYKDSRGVYC VFEGGTPDGR LDWGPDMICS DDTQYSNGRG HRDTGAGFGA APDIDHLNPR
VQRELTDWLN WLRTDLGFDG WRLDFAKGYS APLARIYVDN TNPTFVVGEI WSSLIYNGDG
KPSTNQDADR QELVNWVEGV GKPATAFDFT TKGILQAAVQ GELWRLHDGN GKAPGLMGWM
PDQAVTFVDN HDTGSTQSLW PFPSDKVMQG YAYILTHPGI PCIFYDHVFD WNLQHEIATL
AEIRSRNGIH AESTLDILKA EGDIYVAMID GKVITKLGPR YDAGGIIPSD FHVVAHGNDY
CVWEKEGLRV PAGRKHY
//
