GLGL2_WHEAT
ID GLGL2_WHEAT Reviewed; 522 AA.
AC P12299;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase large subunit, chloroplastic/amyloplastic;
DE EC=2.7.7.27;
DE AltName: Full=ADP-glucose pyrophosphorylase;
DE AltName: Full=ADP-glucose synthase;
DE AltName: Full=AGPase S;
DE AltName: Full=Alpha-D-glucose-1-phosphate adenyl transferase;
DE Flags: Precursor;
GN Name=AGP-L; Synonyms=AGA.3;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Chinese Spring;
RX PubMed=7580858; DOI=10.1007/bf00239933;
RA Ainsworth C., Hosein F., Tarvis M., Weir F., Burrell M., Devos K.M.,
RA Gale M.D.;
RT "Adenosine diphosphate glucose pyrophosphorylase genes in wheat:
RT differential expression and gene mapping.";
RL Planta 197:1-10(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 227-522.
RC STRAIN=cv. Mardler; TISSUE=Endosperm;
RA Olive M.R., Ellis R.J., Schuch W.W.;
RT "Isolation and nucloetide sequences of cDNA clones encoding ADP-glucose
RT pyrophosphorylase polypeptides from wheat leaf and endosperm.";
RL Plant Mol. Biol. 12:525-538(1989).
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.
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 -!- ACTIVITY REGULATION: Insensitive to 3'phosphoglycerate and
CC orthophosphate.
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC -!- SUBUNIT: Heterotetramer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast.
CC Note=Found in the chloroplast in leaf. Found in the plastid in the
CC developing endosperm.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the whole grains, a
CC slightly less abundant expression is seen in leaves, while a low level
CC expression is seen in the roots. A greater expression is seen in the
CC endosperm than in the embryo and pericarp layers.
CC -!- DEVELOPMENTAL STAGE: Is not expressed until 10 dpa (days post
CC anthesis), accumulates to the highest levels between 20 and 35 dpa and
CC levels decrease after 35 dpa.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
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DR EMBL; Z21969; CAA79980.1; -; Genomic_DNA.
DR EMBL; X14349; CAA32532.1; -; mRNA.
DR PIR; S05078; S05078.
DR PIR; S60572; S60572.
DR AlphaFoldDB; P12299; -.
DR SMR; P12299; -.
DR STRING; 4565.Traes_1DL_844FE40E6.1; -.
DR PRIDE; P12299; -.
DR EnsemblPlants; TraesCAD_scaffold_026862_01G000200.1; TraesCAD_scaffold_026862_01G000200.1; TraesCAD_scaffold_026862_01G000200.
DR EnsemblPlants; TraesCLE_scaffold_021123_01G000200.1; TraesCLE_scaffold_021123_01G000200.1; TraesCLE_scaffold_021123_01G000200.
DR EnsemblPlants; TraesCS1D02G427400.1; TraesCS1D02G427400.1; TraesCS1D02G427400.
DR EnsemblPlants; TraesPAR_scaffold_099662_01G000100.1; TraesPAR_scaffold_099662_01G000100.1; TraesPAR_scaffold_099662_01G000100.
DR EnsemblPlants; TraesROB_scaffold_095547_01G000200.1; TraesROB_scaffold_095547_01G000200.1; TraesROB_scaffold_095547_01G000200.
DR EnsemblPlants; TraesWEE_scaffold_083408_01G000100.1; TraesWEE_scaffold_083408_01G000100.1; TraesWEE_scaffold_083408_01G000100.
DR Gramene; TraesCAD_scaffold_026862_01G000200.1; TraesCAD_scaffold_026862_01G000200.1; TraesCAD_scaffold_026862_01G000200.
DR Gramene; TraesCLE_scaffold_021123_01G000200.1; TraesCLE_scaffold_021123_01G000200.1; TraesCLE_scaffold_021123_01G000200.
DR Gramene; TraesCS1D02G427400.1; TraesCS1D02G427400.1; TraesCS1D02G427400.
DR Gramene; TraesPAR_scaffold_099662_01G000100.1; TraesPAR_scaffold_099662_01G000100.1; TraesPAR_scaffold_099662_01G000100.
DR Gramene; TraesROB_scaffold_095547_01G000200.1; TraesROB_scaffold_095547_01G000200.1; TraesROB_scaffold_095547_01G000200.
DR Gramene; TraesWEE_scaffold_083408_01G000100.1; TraesWEE_scaffold_083408_01G000100.1; TraesWEE_scaffold_083408_01G000100.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_14_4_1; -.
DR SABIO-RK; P12299; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P12299; baseline and differential.
DR Genevisible; P12299; TA.
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 2: Evidence at transcript level;
KW Allosteric enzyme; Amyloplast; ATP-binding; Chloroplast;
KW Nucleotide-binding; Nucleotidyltransferase; Plastid; Reference proteome;
KW Starch biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..522
FT /note="Glucose-1-phosphate adenylyltransferase large
FT subunit, chloroplastic/amyloplastic"
FT /id="PRO_0000011169"
FT REGION 28..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 365
FT /note="A -> S (in Ref. 2; CAA32532)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="S -> L (in Ref. 2; CAA32532)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="R -> P (in Ref. 2; CAA32532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 57809 MW; 1E16AB72BE1C55C5 CRC64;
MSSMQFSSVL PLEGKACISP VRREGSASER LKVGDSSSIR HERASRRMCN GGRGPAATGA
QCVLTSDASP ADTLVLRTSF RRNYADPNEV AAVILGGGTG TQLFPLTSTR ATPAVPIGGC
YRLIDIPMSN CFNSGINKIF VMTQFNSASL NRHIHRTYLG GGINFTDGSV EVLAATQMPG
EAAGWFRGTA DAVRKFIWVL EDYYKNKSIE HILILSGDQL YRMDYMELVQ KHVDDNADIT
LSCAPVGESR ASEYGLVKFD SSGRVVQFSE KPKGDDLEAM KVDTSFLNFA IDDPAKYPYI
ASMGVYVFKR DVLLNLLKSR YAELHDFGSE ILPRALHDHN VQAYVFTDYW EDIGTIRSFF
DANMALCEQP PKFEFYDPKT PFFTSPRYLP PTKSDKCRIK EAIISHGCFL RECKIEHSII
GVRSRLNSGS ELKNAMMMGA DSYETEDEIS RLMSEGKVPI GVGENTKISN CIIDMNARIG
RDVVISNKEG VQEADRPEEG YYIRSGIVVI QKNATIKDGT VV
