GLGL3_SOLTU
ID GLGL3_SOLTU Reviewed; 483 AA.
AC P55243;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase large subunit 3, 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=AGPS3;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Desiree; TISSUE=Leaf;
RX PubMed=7700228; DOI=10.1007/bf00298960;
RA la Cognata U., Willmitzer L., Mueller-Roeber B.;
RT "Molecular cloning and characterization of novel isoforms of potato ADP-
RT glucose pyrophosphorylase.";
RL Mol. Gen. Genet. 246:538-548(1995).
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: Tubers.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; X76136; CAA53741.1; -; mRNA.
DR PIR; S53992; S53992.
DR RefSeq; NP_001275395.1; NM_001288466.1.
DR AlphaFoldDB; P55243; -.
DR SMR; P55243; -.
DR STRING; 4113.PGSC0003DMT400023304; -.
DR PRIDE; P55243; -.
DR ProMEX; P55243; -.
DR GeneID; 102582750; -.
DR KEGG; sot:102582750; -.
DR eggNOG; KOG1322; Eukaryota.
DR InParanoid; P55243; -.
DR OrthoDB; 806744at2759; -.
DR BRENDA; 2.7.7.27; 5757.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P55243; 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.
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..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..483
FT /note="Glucose-1-phosphate adenylyltransferase large
FT subunit 3, chloroplastic/amyloplastic"
FT /id="PRO_0000011168"
SQ SEQUENCE 483 AA; 53602 MW; CBFC4A94C01A8848 CRC64;
MGKKLKYTKF QLRSNVVKPN ICMSLTTDIA GEAKLKDLER QKKGDARTVV AIILGGGAGT
RLFPLTKRRA KPAVPMGGAY RLIDVPMSNC INSGINKVYI LTQFNSASLN RHIARAYNFG
NGVTFESGYV EVLAATQTPG ELGKRWFQGT AHAVRQFHWL FEDARSKDIE DVLILSGDHL
YRMDYLHFVQ SHRQSGADIT ISSLPIDDSR ASDFGLMKID DTGRVMSFSE KPKGDDLKAM
AVDTTVLGLS PEEAKEKPYI ASIGKVYVFK KDILLNLLRW RFPTANDFGS EIIPASTKEF
CVKAYLFNDY WEDIGTIRSF FRANLALTEH PPRFSFYDAT KPIYTSRRNL PPSAIDNSKI
VDSIVSHGIF LTNCFVEHSV VGIRSRIGTN VHLKDTVMLG ADYYETDAEI RSQLAEGKVP
LGIGENTRIK DCIIDKNARI GKNVVIANSE GVQEADRSSE GFYMASGITV ISKNSTIPDG
TVI