ID Q15I66_SOLLC Unreviewed; 524 AA.
AC Q15I66;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000256|RuleBase:RU362093};
DE EC=2.7.7.27 {ECO:0000256|RuleBase:RU362093};
DE AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000256|RuleBase:RU362093};
GN Name=AgpL1 {ECO:0000313|EMBL:ABC26922.1};
GN Synonyms=544283 {ECO:0000313|EnsemblPlants:Solyc01g109790.3.1};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EMBL:ABC26922.1};
RN [1] {ECO:0000313|EMBL:ABC26922.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16770584; DOI=10.1007/s00425-006-0316-y;
RA Petreikov M., Shen S., Yeselson Y., Levin I., Bar M., Schaffer A.A.;
RT "Temporally extended gene expression of the ADP-Glc pyrophosphorylase large
RT subunit (AgpL1) leads to increased enzyme activity in developing tomato
RT fruit.";
RL Planta 224:1465-1479(2006).
RN [2] {ECO:0000313|EnsemblPlants:Solyc01g109790.3.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc01g109790.3.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [3] {ECO:0000313|EnsemblPlants:Solyc01g109790.3.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc01g109790.3.1};
RG EnsemblPlants;
RL Submitted (JAN-2019) to UniProtKB.
CC -!- FUNCTION: This protein plays a role in synthesis of starch. It
CC catalyzes the synthesis of the activated glycosyl donor, ADP-glucose
CC from Glc-1-P and ATP. {ECO:0000256|RuleBase:RU362093}.
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:0000256|RuleBase:RU362093};
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC {ECO:0000256|RuleBase:RU362093}.
CC -!- SUBUNIT: Heterotetramer. {ECO:0000256|ARBA:ARBA00011680,
CC ECO:0000256|RuleBase:RU362093}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229, ECO:0000256|RuleBase:RU362093}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443,
CC ECO:0000256|RuleBase:RU362093}.
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DR EMBL; DQ322682; ABC26921.1; -; Genomic_DNA.
DR EMBL; DQ322683; ABC26922.1; -; Genomic_DNA.
DR RefSeq; NP_001233918.2; NM_001246989.2.
DR AlphaFoldDB; Q15I66; -.
DR SMR; Q15I66; -.
DR STRING; 4081.Q15I66; -.
DR PaxDb; 4081-Solyc01g109790-2-1; -.
DR EnsemblPlants; Solyc01g109790.3.1; Solyc01g109790.3.1; Solyc01g109790.3.
DR GeneID; 544283; -.
DR Gramene; Solyc01g109790.3.1; Solyc01g109790.3.1; Solyc01g109790.3.
DR KEGG; sly:544283; -.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_14_4_1; -.
DR InParanoid; Q15I66; -.
DR OMA; NVQSYFF; -.
DR OrthoDB; 601725at2759; -.
DR BRENDA; 2.7.7.27; 3101.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000004994; Chromosome 1.
DR ExpressionAtlas; Q15I66; baseline and differential.
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 CDD; cd02508; ADP_Glucose_PP; 1.
DR CDD; cd04651; LbH_G1P_AT_C; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 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 NCBIfam; TIGR02091; glgC; 1.
DR PANTHER; PTHR43523:SF4; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE LARGE SUBUNIT 3, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43523; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE-RELATED; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362093};
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000256|RuleBase:RU362093};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362093};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU362093};
KW Plastid {ECO:0000256|RuleBase:RU362093};
KW Reference proteome {ECO:0000313|Proteomes:UP000004994};
KW Starch biosynthesis {ECO:0000256|RuleBase:RU362093};
KW Transferase {ECO:0000256|RuleBase:RU362093}.
FT DOMAIN 94..370
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 524 AA; 58152 MW; A42CEC5C0FA2F6C3 CRC64;
MDTCCAAMKS TVHLGRVSTG GFNNGEKEIF GEKIRGSLNN NLRINQLSKS LKLEKKIKPG
VAYSVITTEN DTETVFVDMP RLERRRANPK DVAAVILGGG EGTKLFPLTS RTATPAVPVG
GCYRLIDIPM SNCINSAINK IFVLTQYNSA ALNRHIARTY FGNGVSFGDG FVEVLAATQT
PGEAGKKWFQ GTADAVRKFI WVFEDAKNKN IENILVLSGD HLYRMDYMEL VQNHIDRNAD
ITLSCAPAED SRASDFGLVK IDSRGRVVQF AEKPKGFELK AMQVDTTLVG LSPQDAKKSP
YIASMGVYVF KTDVLLKLLK WSYPTSNDFG SEIIPAAIDD YNVQAYIFKD YWEDIGTIKS
FYNASLALTQ EFPEFQFYDP KTPFYTSPRF LPPTKIDNCK IKDAIISHGC FLRDCTVEHS
IVGERSRLDC GVELKDTFMM GADYYQTESE IASLLAEGKV PIGIGENTKI RKCIIDKNAK
IGKNVSIINK DGVQEADRPE EGFYIRSGII IISEKATIRD GTVI
//
