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Database: UniProt/SWISS-PROT
Entry: AMY3C_ORYSJ
LinkDB: AMY3C_ORYSJ
Original site: AMY3C_ORYSJ 
ID   AMY3C_ORYSJ             Reviewed;         437 AA.
AC   P27939; A0A0P0XPD0; Q0J182; Q67U02;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   23-MAY-2018, entry version 133.
DE   RecName: Full=Alpha-amylase isozyme 3C;
DE            EC=3.2.1.1 {ECO:0000250|UniProtKB:P00693};
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Precursor;
GN   Name=AMY1.7; Synonyms=AMY3B;
GN   OrderedLocusNames=Os09g0457800, LOC_Os09g28420, LOC_Os09g28430;
GN   ORFNames=B1045B05.11, OsJ_29632;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; 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 [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=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   [4]
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.,
RA   McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
RA   Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
RA   Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
RA   Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using
RT   next generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
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.,
RA   Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
RA   Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
RA   Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
RA   Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
RA   Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
RA   Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
RA   Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
RA   Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
RA   Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
RA   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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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: Endohydrolysis of (1->4)-alpha-D-glucosidic
CC       linkages in polysaccharides containing three or more (1->4)-alpha-
CC       linked D-glucose units. {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.
CC       {ECO:0000250|UniProtKB:P00693};
CC   -!- SUBUNIT: Monomer.
CC   -!- TISSUE SPECIFICITY: Germinating seeds.
CC   -!- DEVELOPMENTAL STAGE: Expressed at a high level during germination
CC       in the aleurones cells under the control of the plant hormone
CC       gibberellic acid and in the developing grains at a low level.
CC   -!- MISCELLANEOUS: Binds starch not only at the active site, but also
CC       via accessory binding sites on the protein surface that are
CC       important for efficient binding to starch granules and thereby
CC       increase enzyme activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000305}.
DR   EMBL; X56338; CAA39778.1; -; Genomic_DNA.
DR   EMBL; AP005891; BAD38369.1; -; Genomic_DNA.
DR   EMBL; AP008215; BAF25283.1; -; Genomic_DNA.
DR   EMBL; AP014965; BAT08444.1; -; Genomic_DNA.
DR   EMBL; CM000146; EAZ44990.1; -; Genomic_DNA.
DR   EMBL; AK101358; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; S14956; S14956.
DR   RefSeq; XP_015612114.1; XM_015756628.1.
DR   UniGene; Os.79418; -.
DR   ProteinModelPortal; P27939; -.
DR   SMR; P27939; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; P27939; -.
DR   EnsemblPlants; Os09t0457800-01; Os09t0457800-01; Os09g0457800.
DR   GeneID; 4347265; -.
DR   Gramene; Os09t0457800-01; Os09t0457800-01; Os09g0457800.
DR   KEGG; osa:4347265; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   eggNOG; COG0366; LUCA.
DR   KO; K01176; -.
DR   OMA; NAADECA; -.
DR   OrthoDB; EOG093600FS; -.
DR   Proteomes; UP000059680; Chromosome 9.
DR   ExpressionAtlas; P27939; differential.
DR   Genevisible; P27939; OS.
DR   GO; GO:0004556; F:alpha-amylase activity; IEP:Gramene.
DR   GO; GO:0103025; F:alpha-amylase activity (releasing maltohexaose); IEA:UniProtKB-EC.
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; Complete proteome; Glycosidase;
KW   Hydrolase; Metal-binding; Reference proteome; Signal.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   CHAIN        27    437       Alpha-amylase isozyme 3C.
FT                                /FTId=PRO_0000001414.
FT   REGION       70     72       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   REGION       77     78       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   REGION      203    208       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   REGION      299    301       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   REGION      402    404       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   REGION      414    420       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   ACT_SITE    205    205       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   ACT_SITE    230    230       Proton donor.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   METAL       117    117       Calcium 1.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   METAL       134    134       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   METAL       137    137       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   METAL       139    139       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   METAL       143    143       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   METAL       153    153       Calcium 3.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   METAL       164    164       Calcium 1.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   METAL       167    167       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   METAL       168    168       Calcium 3.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   METAL       169    169       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   METAL       172    172       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   METAL       174    174       Calcium 1.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   METAL       174    174       Calcium 3.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   METAL       209    209       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   BINDING     232    232       Substrate.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   BINDING     234    234       Substrate.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   BINDING     252    252       Substrate.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   BINDING     293    293       Substrate.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   BINDING     312    312       Substrate.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   BINDING     318    318       Substrate.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   BINDING     397    397       Substrate.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   BINDING     424    424       Substrate.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   SITE        313    313       Transition state stabilizer.
FT                                {ECO:0000250|UniProtKB:P00693}.
FT   CONFLICT     39     39       K -> N (in Ref. 1; CAA39778).
FT                                {ECO:0000305}.
FT   CONFLICT     54     54       D -> Y (in Ref. 1; CAA39778).
FT                                {ECO:0000305}.
FT   CONFLICT     66     66       P -> S (in Ref. 6; AK101358).
FT                                {ECO:0000305}.
FT   CONFLICT    331    331       G -> R (in Ref. 1; CAA39778).
FT                                {ECO:0000305}.
SQ   SEQUENCE   437 AA;  48504 MW;  62BBDEF45C14AC78 CRC64;
     MAKHSTTMSC LLFFVLLCLG SHLAQAQVLF QGFNWESWKK QGGWYNFLHS HVDDIAATGV
     THVWLPPPSH SVAPQGYMPG RLYDLDASKY GTGAELRSLI AAFHSKSIKC VADIVINHRC
     ADYKDSRGIY CIFEGGTPDS RLDWGPDMIC SDDTQYSNGR GHRDTGADFG AAPDIDHLNT
     RVQTELSDWL NWLKSDVGFD GWRLDFAKGY SATVAKTYVD NTDPSFVVAE IWSNMRYDGN
     GEPSWNQDGD RQELVNWAQA VGGPASAFDF TTKGELQAAV QGELWRMKDG NGKAPGMIGW
     LPEKAVTFID NHDTGSTQNS WPFPSDKVMQ GYAYILTHPG VPCIFYDHVF DWNLKQEIST
     LAAVRSRNGI HPGSKLNILA ADGDVYVAMI DDKVITKIGT RYDVGNLIPS DFHVVAHGNN
     YCVWEKSGLR VPAGRRH
//
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