ID Q6UBQ7_ORYSJ Unreviewed; 972 AA.
AC Q6UBQ7;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=Starch synthase, chloroplastic/amyloplastic {ECO:0000256|RuleBase:RU361232};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361232};
GN OrderedLocusNames=Os01g0720600 {ECO:0000313|EMBL:BAS74075.1};
GN ORFNames=OSNPB_010720600 {ECO:0000313|EMBL:BAS74075.1};
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 {ECO:0000313|EMBL:AAQ82622.1};
RN [1] {ECO:0000313|EMBL:AAQ82622.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15642712; DOI=10.1093/jxb/eri065;
RA Dian W., Jiang H., Wu P.;
RT "Evolution and expression analysis of starch synthase III and IV in rice.";
RL J. Exp. Bot. 56:623-632(2005).
RN [2] {ECO:0000313|Proteomes:UP000059680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RA Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N.,
RA Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y.,
RA Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N.,
RA Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M.,
RA Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M.,
RA Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K.,
RA Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N.,
RA Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H.,
RA Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M.,
RA Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S.,
RA Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y.,
RA Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H.,
RA Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K.,
RA Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M.,
RA Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A.,
RA Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S.,
RA Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R.,
RA Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J.,
RA Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X.,
RA Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S.,
RA Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A.,
RA Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R.,
RA Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S.,
RA Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M.,
RA Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S.,
RA Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H.,
RA Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C.,
RA Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S.,
RA Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S.,
RA Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K.,
RA Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A.,
RA Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R.,
RA Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S.,
RA Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K.,
RA Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D.,
RA Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I.,
RA Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A.,
RA Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H.,
RA Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S.,
RA Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T.,
RA Kadowaki K., Sugiura M., Burr B., Sasaki T.;
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3] {ECO:0000313|EMBL:BAS74075.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23299411; DOI=10.1093/pcp/pcs183;
RA Sakai H., Lee S.S., Tanaka T., Numa H., Kim J., Kawahara Y., Wakimoto H.,
RA Yang C.C., Iwamoto M., Abe T., Yamada Y., Muto A., Inokuchi H., Ikemura T.,
RA Matsumoto T., Sasaki T., Itoh T.;
RT "Rice Annotation Project Database (RAP-DB): an integrative and interactive
RT database for rice genomics.";
RL Plant Cell Physiol. 54:E6-E6(2013).
RN [4] {ECO:0000313|EMBL:BAS74075.1, ECO:0000313|Proteomes:UP000059680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680};
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 [5] {ECO:0000313|EMBL:BAS74075.1}
RP NUCLEOTIDE SEQUENCE.
RA Sakai H., Kawahara Y., Matsumoto T., Buell C.R., Itoh T.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004727, ECO:0000256|RuleBase:RU361232}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|RuleBase:RU361232}. Plastid, amyloplast
CC {ECO:0000256|RuleBase:RU361232}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC Bacterial/plant glycogen synthase subfamily.
CC {ECO:0000256|ARBA:ARBA00010281, ECO:0000256|RuleBase:RU361232}.
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DR EMBL; AY373257; AAQ82622.1; -; mRNA.
DR EMBL; AP014957; BAS74075.1; -; Genomic_DNA.
DR RefSeq; XP_015648277.1; XM_015792791.1.
DR AlphaFoldDB; Q6UBQ7; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR EnsemblPlants; Os01t0720600-02; Os01t0720600-02; Os01g0720600.
DR GeneID; 4324654; -.
DR Gramene; Os01t0720600-02; Os01t0720600-02; Os01g0720600.
DR HOGENOM; CLU_007243_0_0_1; -.
DR OrthoDB; 141134at2759; -.
DR BRENDA; 2.4.1.21; 4460.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000059680; Chromosome 1.
DR ExpressionAtlas; Q6UBQ7; baseline and differential.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
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 NCBIfam; TIGR02095; glgA; 1.
DR PANTHER; PTHR46083; -; 1.
DR PANTHER; PTHR46083:SF2; STARCH SYNTHASE 4, CHLOROPLASTIC_AMYLOPLASTIC-RELATED; 1.
DR Pfam; PF08323; Glyco_transf_5; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 1: Evidence at protein level;
KW Amyloplast {ECO:0000256|ARBA:ARBA00023234, ECO:0000256|RuleBase:RU361232};
KW Chloroplast {ECO:0000256|RuleBase:RU361232};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU361232};
KW Plastid {ECO:0000256|ARBA:ARBA00023234, ECO:0000256|RuleBase:RU361232};
KW Proteomics identification {ECO:0007829|ProteomicsDB:Q6UBQ7};
KW Reference proteome {ECO:0000313|Proteomes:UP000059680};
KW Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922,
KW ECO:0000256|RuleBase:RU361232};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 478..716
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 771..923
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 34..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 155..182
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 225..276
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 53..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 109572 MW; 0476330CFC1CA093 CRC64;
MAACGAAAAE YSALLSLSCG PITRRRFAVS CRARPPGNLS AQQKKKRGKN IAPKQRSSNA
KLLLTTEENG QLPSTSLRTS MERPQKSTSS EDDTNGAISQ IDEKIAAIGN EQQERSKDKH
FESDFQLEDF GEMIQNMEKN ILLLNQARLQ AIEDVDKILT EKEALQKKVD TLEMNLSKAL
ATKGNINTDI PGDHLEKFTK EILIESALSG GNPAHLCESP LFMELTVLKE ENMLLKADAQ
FLKAKIVEFA ETEEFLFKLE KERSLLDATV RELEARFLVA QTDIWKVVPL QYDVWMEKVE
NLQHMLGCLK NHVEKYAALL DQHDDLHDKI DELEASLKEG KTSEFSPYVV ELLQQKLKAA
KSHHQAGHQE TNTHIQVYQQ LTEEFQDNLG KLIEESGRLE HSANSMPSEF WSHILLMIDG
WFLERKIPNT DARMLREMAW KRDDRICEAY FACKGAKESD VMETFLKLSL SGNSSGLHIV
HIAAEMAPVA KVGGLADVVA GLGKALQTKG HLVEIVLPKY DCMQLDQITN LKVLDVVIQS
YFDGNLFSNN VWTGTVEGLP VYFIEPQHPS KFFWRAQYYG EHDDFKRYSY FSRAALELLY
QSGKKIDIIH CHDWQTAFVA PLYWDIYATR GFSSARICFT CHNFEYQGTA PAPDLSYCGL
DVEQLDRPDR MQDNAHGRIN VAKGGIVYSN IVTTVSPTYA LEVRSEGGRG LQDTLKMHSR
KFVGILNGID TGTWNPSTDR FLAVQYSATD LQGKAANKAF LRKQLGLYSE DASQPLVACI
TRLVPQKGLH LIRHAIYKTA ELGGQFVLLG SSPVPHIQRE FEGVADQFQK NNNIRLILKY
DEALSHCIYA ASDMFIIPSM FEPCGLTQMI AMRYGSVPIV RQTGGLCDSV FDFDDETIPV
ELRNGFTFAR TDEQDLSSCL ERAFSYYSRK PMVWKQLVQK DMQIDFSWDS PASQYENLYQ
SAVAQARGAA QT
//
