GLGL1_HORVU
ID GLGL1_HORVU Reviewed; 523 AA.
AC P30524;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase large subunit 1, 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 AltName: Full=BEPL;
DE Flags: Precursor;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Bomi; TISSUE=Endosperm;
RX PubMed=16653175; DOI=10.1104/pp.100.3.1617;
RA Villand P., Olsen O.-A., Kilian A., Kleczkowski L.A.;
RT "ADP-glucose pyrophosphorylase large subunit cDNA from barley endosperm.";
RL Plant Physiol. 100:1617-1618(1992).
RN [2]
RP SEQUENCE REVISION.
RA Villand P.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 267-480.
RC STRAIN=cv. Bomi; TISSUE=Seed;
RX PubMed=1320425; DOI=10.1007/bf00023385;
RA Villand P., Aalen R., Olsen O.-A., Luethi E., Loenneborg A.,
RA Kleczkowski L.A.;
RT "PCR amplification and sequences of cDNA clones for the small and large
RT subunits of ADP-glucose pyrophosphorylase from barley tissues.";
RL Plant Mol. Biol. 19:381-389(1992).
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: Highly active without 3'phosphoglycerate, and is
CC only slightly affected by the activator 3'phosphoglycerate and
CC inhibitor 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: Starchy endosperm and roots.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; X67151; CAA47626.1; -; mRNA.
DR EMBL; X62242; CAB37841.1; -; mRNA.
DR PIR; S24984; S24984.
DR AlphaFoldDB; P30524; -.
DR SMR; P30524; -.
DR EnsemblPlants; HORVU.MOREX.r2.1HG0075760.1; HORVU.MOREX.r2.1HG0075760.1; HORVU.MOREX.r2.1HG0075760.
DR EnsemblPlants; HORVU.MOREX.r2.1HG0075760.1.mrna1; HORVU.MOREX.r2.1HG0075760.1.mrna1; HORVU.MOREX.r2.1HG0075760.1.
DR Gramene; HORVU.MOREX.r2.1HG0075760.1; HORVU.MOREX.r2.1HG0075760.1; HORVU.MOREX.r2.1HG0075760.
DR Gramene; HORVU.MOREX.r2.1HG0075760.1.mrna1; HORVU.MOREX.r2.1HG0075760.1.mrna1; HORVU.MOREX.r2.1HG0075760.1.
DR BRENDA; 2.7.7.27; 2687.
DR SABIO-RK; P30524; -.
DR UniPathway; UPA00152; -.
DR ExpressionAtlas; P30524; baseline and differential.
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; Starch biosynthesis;
KW Transferase; Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..523
FT /note="Glucose-1-phosphate adenylyltransferase large
FT subunit 1, chloroplastic/amyloplastic"
FT /id="PRO_0000011164"
FT CONFLICT 472..474
FT /note="CII -> SYY (in Ref. 2; CAB37841)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 57933 MW; 483A444CC6028523 CRC64;
MSSMQFSSVL PLEGKACVSP VRREGSACER LKIGDSSSIR HERASRRMCN GGARGPAATG
AQCVLTSDAS PADTLVLRTS FRRNYADPNE VAAVILGGGT GTQLFPLTST RATPAVPIGG
CYRLIDIPMS NCFNSGINKI FVMTQFNSAS LNRHIHRTYL GGGINFTDGS VEVLAATQMP
GEAAGWFRGT ADAVRKFIWV LEDYYKHKSI EHILILSGDQ LYRMDYMELV QKHVDDNADI
TLSCAPVGES RASEYGLVKF DSSGRVIQFS EKPKGDDLEA MKVDTSFLNF AIDDPAKYPY
IASMGVYVFK RDVLLNLLKS RYAELHDFGS EILPRALHDH NVQAYVFTDY WEDIGTIRSF
FDANMALCEQ PPKFEFYDPK TPFFTSPRYL PPTKSDKCRI KEAIISHGCF LRECKIEHSI
IGVRSRLNSG SELKNAMMMG ADSYETEDEI SRLMSEGKVP IGVGENTKIS NCIIDMNARI
GRDVVISNKE GVQEADRPEE GYYIRSGIVV IQKNATIKDG TVV
