GLGL1_SOLTU
ID GLGL1_SOLTU Reviewed; 470 AA.
AC Q00081;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase large subunit 1;
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: Fragment;
GN Name=AGPS1;
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. Russet Burbank-0; TISSUE=Tuber;
RX PubMed=1657244; DOI=10.1007/bf00037149;
RA Nakata P.A., Greene T.W., Anderson J.M., Smith-White B.J., Okita T.W.,
RA Preiss J.;
RT "Comparison of the primary sequences of two potato tuber ADP-glucose
RT pyrophosphorylase subunits.";
RL Plant Mol. Biol. 17:1089-1093(1991).
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 -!- INTERACTION:
CC Q00081; P23509; NbExp=2; IntAct=EBI-15812120, EBI-15812097;
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: Prominently expressed in the leaves and a weaker
CC expression is seen in the tubers.
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; X61187; CAA43490.1; -; mRNA.
DR PIR; S18237; S18237.
DR AlphaFoldDB; Q00081; -.
DR SMR; Q00081; -.
DR DIP; DIP-48348N; -.
DR IntAct; Q00081; 1.
DR STRING; 4113.PGSC0003DMT400001935; -.
DR PRIDE; Q00081; -.
DR eggNOG; KOG1322; Eukaryota.
DR InParanoid; Q00081; -.
DR BRENDA; 2.7.7.27; 5757.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q00081; 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 1: Evidence at protein level;
KW Allosteric enzyme; Amyloplast; ATP-binding; Chloroplast;
KW Nucleotide-binding; Nucleotidyltransferase; Plastid; Reference proteome;
KW Starch biosynthesis; Transferase.
FT CHAIN <1..470
FT /note="Glucose-1-phosphate adenylyltransferase large
FT subunit 1"
FT /id="PRO_0000195357"
FT NON_TER 1
SQ SEQUENCE 470 AA; 52253 MW; 88ABEF77FADE0559 CRC64;
NKIKPGVAYS VITTENDTQT VFVDMPRLER RRANPKDVAA VILGGGEGTK LFPLTSRTAT
PAVPVGGCYR LIDIPMSNCI NSAINKIFVL TQYNSAPLNR HIARTYFGNG VSFGDGFVEV
LAATQTPGEA GKKWFQGTAD AVRKFIWVFE DAKNKNIENI VVLSGDHLYR MDYMELVQNH
IDRNADITLS CAPAEDSRAS DFGLVKIDSR GRVVQFAEKP KGFDLKAMQV DTTLVGLSPQ
DAKKSPYIAS MGVYVFKTDV LLKLLKWSYP TSNDFGSEII PAAIDDYNVQ AYIFKDYWED
IGTIKSFYNA SLALTQEFPE FQFYDPKTPF YTSPRFLPPT KIDNCKIKDA IISHGCFLRD
CSVEHSIVGE RSRLDCGVEL KDTFMMGADY YQTESEIASL LAEGKVPIGI GENTKIRKCI
IDKNAKIGKN VSIINKDGVQ EADRPEEGFY IRSGIIIILE KATIRDGTVI