GLGS_MAIZE
ID GLGS_MAIZE Reviewed; 125 AA.
AC P55240;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase small subunit;
DE EC=2.7.7.27;
DE AltName: Full=ADP-glucose pyrophosphorylase;
DE AltName: Full=ADP-glucose synthase;
DE AltName: Full=AGPase B;
DE AltName: Full=Alpha-D-glucose-1-phosphate adenyl transferase;
DE Flags: Fragment;
GN Name=GLG1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. F7.F2; TISSUE=Leaf;
RX PubMed=8115545; DOI=10.1104/pp.104.1.179;
RA Prioul J.-L., Jeannette E., Reyss A., Gregory N., Giroux M., Hannah L.C.,
RA Causse M.;
RT "Expression of ADP-glucose pyrophosphorylase in maize (Zea mays L.) grain
RT and source leaf during grain filling.";
RL Plant Physiol. 104:179-187(1994).
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: Activated by 3'phosphoglycerate, inhibited by
CC orthophosphate. Allosteric regulation.
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: Leaves.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S72425; AAB29961.1; -; mRNA.
DR PIR; T01750; T01750.
DR AlphaFoldDB; P55240; -.
DR SMR; P55240; -.
DR STRING; 4577.GRMZM2G163437_P01; -.
DR PaxDb; P55240; -.
DR PRIDE; P55240; -.
DR MaizeGDB; 113182; -.
DR eggNOG; KOG1322; Eukaryota.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P55240; 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 InterPro; IPR011831; ADP-Glc_PPase.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43523; PTHR43523; 1.
DR SUPFAM; SSF51161; SSF51161; 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.
FT CHAIN <1..125
FT /note="Glucose-1-phosphate adenylyltransferase small
FT subunit"
FT /id="PRO_0000195354"
FT NON_TER 1
SQ SEQUENCE 125 AA; 13246 MW; 25E1690B7FA9F1BE CRC64;
VTDSVIGEGC VIKNCKIHHS VVGLRSCISE GAIIEDTLLM GADYYAETEA DKKLLAENGG
IPIGIGKNSH IRKAIIDKNA RIGDNVKILN ADNVQEAARE TDGYFIKGGI VTVIKDALLP
SGTVI
