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SSG1_ORYSI
ID   SSG1_ORYSI              Reviewed;         609 AA.
AC   A2Y8X2; P19395; Q1ZZT5; Q43012; Q43013; Q71F57; Q8GZD6; Q8S9C4; Q94LY7;
AC   Q9S7R1; Q9S7U4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Granule-bound starch synthase 1, chloroplastic/amyloplastic;
DE            EC=2.4.1.242;
DE   AltName: Full=Granule-bound starch synthase I;
DE            Short=GBSS-I;
DE   AltName: Allergen=Ory s GBSS_I;
DE   Flags: Precursor;
GN   Name=WAXY; Synonyms=WX, WX-B; ORFNames=OsI_020765;
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].
RA   Wang Z.Y., Zheng F.Q., Gao J.P., Wang X.Q., Wu M., Zhang J.L., Hong M.M.;
RT   "Identification of two transposon-like elements in rice Wx gene.";
RL   Sci. China, Ser. B, Chem. Life Sci. Earth Sci. 37:437-447(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Haomuxi;
RA   Sun H.Q., Luo K.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RX   PubMed=24016103; DOI=10.1021/jf402759f;
RA   Golias J., Humlova Z., Halada P., Habova V., Janatkova I., Tuckova L.;
RT   "Identification of rice proteins recognized by the IgE antibodies of
RT   patients with food allergies.";
RL   J. Agric. Food Chem. 61:8851-8860(2013).
CC   -!- FUNCTION: Required for the synthesis of amylose in endosperm.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + an NDP-alpha-D-glucose =
CC         [(1->4)-alpha-D-glucosyl](n+1) + a ribonucleoside 5'-diphosphate +
CC         H(+); Xref=Rhea:RHEA:15873, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9587,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, ChEBI:CHEBI:57930,
CC         ChEBI:CHEBI:76533; EC=2.4.1.242;
CC   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast.
CC       Note=Amyloplast or chloroplast, granule-bound. {ECO:0000250}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|PubMed:24016103}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
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DR   EMBL; X65183; CAA46294.1; -; Genomic_DNA.
DR   EMBL; DQ415640; ABD77490.1; -; Genomic_DNA.
DR   EMBL; CM000131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A2Y8X2; -.
DR   SMR; A2Y8X2; -.
DR   STRING; 39946.A2Y8X2; -.
DR   Allergome; 11008; Ory s GBSS_I.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   EnsemblPlants; BGIOSGA022241-TA; BGIOSGA022241-PA; BGIOSGA022241.
DR   Gramene; BGIOSGA022241-TA; BGIOSGA022241-PA; BGIOSGA022241.
DR   HOGENOM; CLU_009583_18_2_1; -.
DR   OMA; EMGPAKN; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000007015; Chromosome 6.
DR   ExpressionAtlas; A2Y8X2; differential.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0043531; F:ADP binding; IEA:EnsemblPlants.
DR   GO; GO:0102502; F:ADP-glucose-starch glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR   GO; GO:0019863; F:IgE binding; IDA:UniProtKB.
DR   GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00484; Glycogen_synth; 1.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR011835; GS/SS.
DR   InterPro; IPR013534; Starch_synth_cat_dom.
DR   Pfam; PF08323; Glyco_transf_5; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   TIGRFAMs; TIGR02095; glgA; 1.
PE   1: Evidence at protein level;
KW   Allergen; Amyloplast; Chloroplast; Disulfide bond; Glycosyltransferase;
KW   Plastid; Reference proteome; Starch biosynthesis; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..77
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           78..609
FT                   /note="Granule-bound starch synthase 1,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000295649"
FT   REGION          29..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         97
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6U8"
FT   BINDING         100
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q0DEV5"
FT   BINDING         408
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q0DEV5"
FT   BINDING         413
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q0DEV5"
FT   BINDING         462
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q0DEV5"
FT   BINDING         493
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:Q0DEV5"
FT   DISULFID        337..529
FT                   /evidence="ECO:0000250|UniProtKB:Q0DEV5"
FT   VARIANT         415
FT                   /note="P -> S (in strain: cv. Haomuxi)"
FT   CONFLICT        166
FT                   /note="D -> G (in Ref. 2; ABD77490)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   609 AA;  66476 MW;  C225DBF6F12072C5 CRC64;
     MSALTTSQLA TSATGFGIAD RSAPSSLLRH GFQGLKPRSP AGGDATSLSV TTSARATPKQ
     QRSVQRGSRR FPSVVVYATG AGMNVVFVGA EMAPWSKTGG LGDVLGGLPP AMAANGHRVM
     VISPRYDQYK DAWDTSVVAE IKVADRYERV RFFHCYKRGV DRVFIDHPSF LEKVWGKTGE
     KIYGPDTGVD YKDNQMRFSL LCQAALEAPR ILNLNNNPYF KGTYGEDVVF VCNDWHTGPL
     ASYLKNNYQP NGIYRNAKVA FCIHNISYQG RFAFEDYPEL NLSERFRSSF DFIDGYDTPV
     EGRKINWMKA GILEADRVLT VSPYYAEELI SGIARGCELD NIMRLTGITG IVNGMDVSEW
     DPSKDKYITA KYDATTAIEA KALNKEALQA EAGLPVDRKI PLIAFIGRLE EQKGPDVMAA
     AIPELMQEDV QIVLLGTGKK KFEKLLKSME EKYPGKVRAV VKFNAPLAHL IMAGADVLAV
     PSRFEPCGLI QLQGMRYGTP CACASTGGLV DTVIEGKTGF HMGRLSVDCK VVEPSDVKKV
     AATLKRAIKV VGTPAYEEMV RNCMNQDLSW KGPAKNWENV LLGLGVAGSA PGIEGDEIAP
     LAKENVAAP
 
 
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