SSG1_ORYSJ
ID SSG1_ORYSJ Reviewed; 609 AA.
AC Q0DEV5; P19395; Q1ZZT5; Q43012; Q43013; Q71F57; Q8GZD6; Q8S9C4; Q94LY7;
AC Q9S7R1; Q9S7U4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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;
GN OrderedLocusNames=Os06g0133000, LOC_Os06g04200;
GN ORFNames=134P10.7, P0679C08.19;
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 [MRNA].
RC TISSUE=Seed;
RX PubMed=1377969; DOI=10.1007/bf00023402;
RA Okagaki R.J.;
RT "Nucleotide sequence of a long cDNA from the rice waxy gene.";
RL Plant Mol. Biol. 19:513-516(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Taichung 65; TISSUE=Seedling;
RA Hirano H.Y., Sano Y.;
RT "Molecular characterization of the waxy locus of rice (Oryza sativa).";
RL Plant Cell Physiol. 32:989-997(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Hanfeng;
RX PubMed=2216792; DOI=10.1093/nar/18.19.5898;
RA Wang Z.Y., Wu Z.L., Xing Y.Y., Zheng F.G., Guo X.L., Zhang W.G., Hong M.M.;
RT "Nucleotide sequence of rice waxy gene.";
RL Nucleic Acids Res. 18:5898-5898(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Lemont;
RX PubMed=9747848; DOI=10.1023/a:1006021807799;
RA Frances H., Bligh J., Larkin P.D., Roach P.S., Jones C.A., Fu H.,
RA Park W.D.;
RT "Use of alternate splice sites in granule-bound starch synthase mRNA from
RT low-amylose rice varieties.";
RL Plant Mol. Biol. 38:407-415(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Jodon, and cv. Rexmont;
RA Larkin P.D., McClung A.M., Ayres N.M., Park W.D.;
RT "The Wx locus (granule bound starch synthase) is strongly associated with
RT pasting curve characteristics in rice (Oryza sativa L.).";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Koshihikari, and cv. Milky Queen;
RA Sato H., Suzuki Y., Sakai M., Imbe T.;
RT "Molecular characterization of Wx-mq, a novel mutant gene for low-amylose
RT content in endosperm of rice (Oryza sativa L.).";
RL Breed. Sci. 52:131-135(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. L202, cv. Lemont, cv. Rexmont, and cv. Toro-2;
RA Larkin P.D., McClung A.M., Park W.D.;
RT "Association of single nucleotide polymorphism in the waxy locus with
RT starch viscosity characteristics in rice, Oryza sativa L.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RA Ma J., SanMiguel P.J., Dubcovsky J., Shiloff B.A., Rostoks N., Jiang Z.,
RA Busso C.S., Kleinhofs A., Devos K.M., Ramakrishna W., Bennetzen J.L.;
RT "Comparative sequence analysis of homologous Wx1 regions in barley, maize,
RT pearl millet, rice, sorghum and diploid wheat.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
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 [10]
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 [11]
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 [12]
RP PROTEIN SEQUENCE OF 78-94.
RX PubMed=8595054; DOI=10.1007/bf00553625;
RA Taira T., Fujita N., Takaoka K., Uematsu M., Wadano A., Kozaki S.,
RA Okabe S.;
RT "Variation in the primary structure of waxy proteins (granule-bound starch
RT synthase) in diploid cereals.";
RL Biochem. Genet. 33:269-281(1995).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 153-343.
RX PubMed=2016064; DOI=10.1016/0378-1119(91)90180-j;
RA Shimada H., Tada Y.;
RT "Rapid isolation of a rice waxy sequence: a simple PCR method for the
RT analysis of recombinant plasmids from intact Escherichia coli cells.";
RL Gene 98:243-248(1991).
RN [14]
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).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 83-609 IN COMPLEX WITH ADP, AND
RP DISULFIDE BONDS.
RX PubMed=22878205; DOI=10.1271/bbb.120305;
RA Momma M., Fujimoto Z.;
RT "Interdomain disulfide bridge in the rice granule bound starch synthase I
RT catalytic domain as elucidated by X-ray structure analysis.";
RL Biosci. Biotechnol. Biochem. 76:1591-1595(2012).
CC -!- FUNCTION: Required for the synthesis of amylose in endosperm.
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.
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; X62134; CAA44065.1; -; mRNA.
DR EMBL; X58228; CAA41186.1; -; Genomic_DNA.
DR EMBL; X53694; CAA37732.1; -; Genomic_DNA.
DR EMBL; AF031162; AAC61675.2; -; Genomic_DNA.
DR EMBL; AF141954; AAF72561.1; -; Genomic_DNA.
DR EMBL; AF141955; AAF72562.1; -; Genomic_DNA.
DR EMBL; AB066093; BAB88209.1; -; mRNA.
DR EMBL; AB066094; BAB88210.1; -; mRNA.
DR EMBL; AF515480; AAN77100.1; -; mRNA.
DR EMBL; AF515481; AAN77101.1; -; mRNA.
DR EMBL; AF515482; AAN77102.1; -; mRNA.
DR EMBL; AF515483; AAN77103.1; -; mRNA.
DR EMBL; AF488413; AAO33149.1; -; Genomic_DNA.
DR EMBL; AP002542; BAB19379.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF18618.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS95999.1; -; Genomic_DNA.
DR EMBL; M55039; AAA33918.1; -; Genomic_DNA.
DR PIR; JQ0703; JQ0703.
DR PIR; S11481; S11481.
DR RefSeq; XP_015644490.1; XM_015789004.1.
DR RefSeq; XP_015644491.1; XM_015789005.1.
DR RefSeq; XP_015644492.1; XM_015789006.1.
DR PDB; 3VUE; X-ray; 2.70 A; A=83-609.
DR PDB; 3VUF; X-ray; 3.00 A; A=83-609.
DR PDBsum; 3VUE; -.
DR PDBsum; 3VUF; -.
DR AlphaFoldDB; Q0DEV5; -.
DR SMR; Q0DEV5; -.
DR STRING; 4530.OS06T0133000-01; -.
DR Allergome; 11008; Ory s GBSS_I.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR PaxDb; Q0DEV5; -.
DR PRIDE; Q0DEV5; -.
DR EnsemblPlants; Os06t0133000-01; Os06t0133000-01; Os06g0133000.
DR EnsemblPlants; Os06t0133000-02; Os06t0133000-02; Os06g0133000.
DR GeneID; 4340018; -.
DR Gramene; Os06t0133000-01; Os06t0133000-01; Os06g0133000.
DR Gramene; Os06t0133000-02; Os06t0133000-02; Os06g0133000.
DR KEGG; osa:4340018; -.
DR eggNOG; ENOG502QQX3; Eukaryota.
DR HOGENOM; CLU_009583_18_2_1; -.
DR InParanoid; Q0DEV5; -.
DR OMA; EMGPAKN; -.
DR OrthoDB; 1142473at2759; -.
DR PlantReactome; R-OSA-9626305; Regulatory network of nutrient accumulation.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR ExpressionAtlas; Q0DEV5; baseline and differential.
DR Genevisible; Q0DEV5; OS.
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; IDA:UniProtKB.
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 3D-structure; Allergen; Amyloplast; Chloroplast; Direct protein sequencing;
KW Disulfide bond; Glycosyltransferase; Plastid; Reference proteome;
KW Starch biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..77
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:8595054"
FT CHAIN 78..609
FT /note="Granule-bound starch synthase 1,
FT chloroplastic/amyloplastic"
FT /id="PRO_0000011132"
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:0000269|PubMed:22878205,
FT ECO:0007744|PDB:3VUF"
FT BINDING 408
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:22878205,
FT ECO:0007744|PDB:3VUF"
FT BINDING 413
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:22878205,
FT ECO:0007744|PDB:3VUF"
FT BINDING 462
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:22878205,
FT ECO:0007744|PDB:3VUF"
FT BINDING 493
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:22878205,
FT ECO:0007744|PDB:3VUF"
FT DISULFID 337..529
FT /evidence="ECO:0000269|PubMed:22878205,
FT ECO:0007744|PDB:3VUE, ECO:0007744|PDB:3VUF"
FT VARIANT 224
FT /note="Y -> S (in strain: cv. Lemont)"
FT VARIANT 415
FT /note="P -> S (in strain: cv. Rexmont)"
FT CONFLICT 158
FT /note="R -> H (in Ref. 6; BAB88209)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="Y -> H (in Ref. 6; BAB88209)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="N -> T (in Ref. 13; AAA33918)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="P -> T (in Ref. 13; AAA33918)"
FT /evidence="ECO:0000305"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:3VUE"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:3VUE"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 133..143
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:3VUE"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 193..211
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:3VUE"
FT TURN 248..252
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 274..280
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:3VUE"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 323..330
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:3VUE"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:3VUE"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:3VUE"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 377..391
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 415..425
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 440..452
FT /evidence="ECO:0007829|PDB:3VUE"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 465..474
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 476..480
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 490..496
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 508..512
FT /evidence="ECO:0007829|PDB:3VUE"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:3VUE"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 534..550
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 554..565
FT /evidence="ECO:0007829|PDB:3VUE"
FT HELIX 571..582
FT /evidence="ECO:0007829|PDB:3VUE"
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
