GLGS1_ORYSJ
ID GLGS1_ORYSJ Reviewed; 500 AA.
AC Q69T99;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase small subunit 1, chloroplastic/amyloplastic {ECO:0000305};
DE Short=OsAGPS1 {ECO:0000303|PubMed:17406793};
DE Short=OsAPS1 {ECO:0000303|PubMed:15821022};
DE EC=2.7.7.27 {ECO:0000305|PubMed:17406793};
DE AltName: Full=ADP-glucose pyrophosphorylase AGPS1 {ECO:0000305};
DE AltName: Full=ADP-glucose synthase AGPS1 {ECO:0000305};
DE Flags: Precursor;
GN Name=AGPS1 {ECO:0000303|PubMed:17406793};
GN Synonyms=APS1 {ECO:0000303|PubMed:15821022};
GN OrderedLocusNames=Os09g0298200 {ECO:0000312|EMBL:BAF24722.1},
GN LOC_Os09g12660 {ECO:0000305};
GN ORFNames=OJ1381_H04.16 {ECO:0000312|EMBL:BAD32986.1},
GN OsJ_28755 {ECO:0000312|EMBL:EEE69398.1},
GN P0592C05.40 {ECO:0000312|EMBL:BAD33225.1};
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].
RX PubMed=20018713; DOI=10.1073/pnas.0912396106;
RA Tian Z., Qian Q., Liu Q., Yan M., Liu X., Yan C., Liu G., Gao Z., Tang S.,
RA Zeng D., Wang Y., Yu J., Gu M., Li J.;
RT "Allelic diversities in rice starch biosynthesis lead to a diverse array of
RT rice eating and cooking qualities.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21760-21765(2009).
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., 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]
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., 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 [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).
RN [7]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=15821022; DOI=10.1093/pcp/pci101;
RA Akihiro T., Mizuno K., Fujimura T.;
RT "Gene expression of ADP-glucose pyrophosphorylase and starch contents in
RT rice cultured cells are cooperatively regulated by sucrose and ABA.";
RL Plant Cell Physiol. 46:937-946(2005).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17406793; DOI=10.1007/s11103-007-9153-z;
RA Lee S.K., Hwang S.K., Han M., Eom J.S., Kang H.G., Han Y., Choi S.B.,
RA Cho M.H., Bhoo S.H., An G., Hahn T.R., Okita T.W., Jeon J.S.;
RT "Identification of the ADP-glucose pyrophosphorylase isoforms essential for
RT starch synthesis in the leaf and seed endosperm of rice (Oryza sativa
RT L.).";
RL Plant Mol. Biol. 65:531-546(2007).
CC -!- FUNCTION: Involved in synthesis of starch. Catalyzes the synthesis of
CC ADP-glucose, a molecule that serves as an activated glycosyl donor for
CC alpha-1,4-glucan synthesis. Essential for starch synthesis in leaf
CC chloroplasts and endosperm amyloplasts. {ECO:0000269|PubMed:17406793}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose
CC + diphosphate; Xref=Rhea:RHEA:12120, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57498,
CC ChEBI:CHEBI:58601; EC=2.7.7.27;
CC Evidence={ECO:0000305|PubMed:17406793};
CC -!- ACTIVITY REGULATION: Activated by 3'phosphoglycerate, inhibited by
CC orthophosphate. Allosteric regulation. {ECO:0000305|PubMed:17406793}.
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Heterotetramer composed of two small and two large subunits.
CC {ECO:0000305|PubMed:17406793}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:17406793}. Plastid, amyloplast
CC {ECO:0000269|PubMed:17406793}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:15821022}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing seeds from 10 to 20 days
CC after flowering (DAF). {ECO:0000269|PubMed:15821022}.
CC -!- INDUCTION: Induced by sucrose, glucose and abscisic acid (ABA).
CC {ECO:0000269|PubMed:15821022}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; GQ150843; ACY56058.1; -; Genomic_DNA.
DR EMBL; GQ150844; ACY56059.1; -; Genomic_DNA.
DR EMBL; GQ150845; ACY56060.1; -; Genomic_DNA.
DR EMBL; GQ150846; ACY56061.1; -; Genomic_DNA.
DR EMBL; GQ150848; ACY56063.1; -; Genomic_DNA.
DR EMBL; AP004011; BAD32986.1; -; Genomic_DNA.
DR EMBL; AP004756; BAD33225.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF24722.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT07326.1; -; Genomic_DNA.
DR EMBL; CM000146; EEE69398.1; -; Genomic_DNA.
DR EMBL; AK060270; BAG87387.1; -; mRNA.
DR EMBL; AK073146; BAG93309.1; -; mRNA.
DR RefSeq; XP_015612224.1; XM_015756738.1.
DR AlphaFoldDB; Q69T99; -.
DR SMR; Q69T99; -.
DR STRING; 4530.OS09T0298200-01; -.
DR PaxDb; Q69T99; -.
DR PRIDE; Q69T99; -.
DR EnsemblPlants; Os09t0298200-01; Os09t0298200-01; Os09g0298200.
DR EnsemblPlants; Os09t0298200-02; Os09t0298200-02; Os09g0298200.
DR GeneID; 4346656; -.
DR Gramene; Os09t0298200-01; Os09t0298200-01; Os09g0298200.
DR Gramene; Os09t0298200-02; Os09t0298200-02; Os09g0298200.
DR KEGG; osa:4346656; -.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_14_4_1; -.
DR InParanoid; Q69T99; -.
DR OMA; GRNAHIR; -.
DR OrthoDB; 806744at2759; -.
DR BRENDA; 2.7.7.27; 4460.
DR PlantReactome; R-OSA-1119477; Starch biosynthesis.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000007752; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR011831; ADP-Glc_PPase.
DR InterPro; IPR005836; ADP_Glu_pyroP_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43523; PTHR43523; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR02091; glgC; 1.
DR PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1.
DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
DR PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Amyloplast; ATP-binding; Chloroplast;
KW Nucleotide-binding; Nucleotidyltransferase; Plastid; Reference proteome;
KW Starch biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..500
FT /note="Glucose-1-phosphate adenylyltransferase small
FT subunit 1, chloroplastic/amyloplastic"
FT /id="PRO_0000441123"
SQ SEQUENCE 500 AA; 54845 MW; B24B54B272BDB9FA CRC64;
MAMMAMGAAS WAPIPAPARA AAAFYPGRDL AAARRRRGAA ARRPFVFTPR AVSDSRSSQT
CLDPDASTSV LGIILGGGAG TRLYPLTKKR AKPAVPLGAN YRLIDIPVSN CLNSNVSKIY
VLTQFNSASL NRHLSRAYGN NIGGYKNEGF VEVLAAQQSP ENPNWFQGTA DAVRQYLWLF
EEHNVMEFLI LAGDHLYRMD YQKFIQAHRE TNADITVAAL PMDEERATAF GLMKIDDEGR
IIEFAEKPKG EKLKSMMVDT TILGLDTERA KELPYIASMG IYVFSKDVML KLLRQNFPAA
NDFGSEVIPG ATEIGMRVQA YLYDGYWEDI GTIEAFYNAN LGITKKPVPD FSFYDRSAAI
YTQPRYLPPS KVLDADVTDS VIGEGCVIRH CTINHSVVGL RSCISEGAVI EDSLLMGADY
YETETDKKAL SETGGIPIGI GKNAHIRKAI IDKNARIGEN VKIINVDNIQ EASRETDGYF
IKSGIVTVIK DALIPSGTVI
