ID   GLGS_SOLLC              Reviewed;         521 AA.
AC   Q42882;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic;
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: Precursor;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fruit;
RA   Chen B.-Y., Janes H.W.;
RT   "ADP-glucose pyrophosphorylase small subunit cDNA from tomato fruit.";
RL   (er) Plant Gene Register PGR95-102(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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000305}.
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DR   EMBL; L41126; AAB00482.1; -; mRNA.
DR   AlphaFoldDB; Q42882; -.
DR   SMR; Q42882; -.
DR   STRING; 4081.Solyc07g056140.2.1; -.
DR   PaxDb; Q42882; -.
DR   PRIDE; Q42882; -.
DR   eggNOG; KOG1322; Eukaryota.
DR   SABIO-RK; Q42882; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q42882; baseline and differential.
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; ATP-binding; Chloroplast; Nucleotide-binding;
KW   Nucleotidyltransferase; Plastid; Reference proteome; Starch biosynthesis;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..72
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           73..521
FT                   /note="Glucose-1-phosphate adenylyltransferase small
FT                   subunit, chloroplastic"
FT                   /id="PRO_0000011153"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   521 AA;  57370 MW;  998B47F682F0AEAC CRC64;
     MAASIGALKS SPSSHNCINE RRNDSTRAIS SRNLSFSSSH LAGDKLMPVS SLRSQGVRFN
     VRRSPLIVSP KAVSDSQNSQ TCLDPDASRS VLGIILGGGA GTRLYPLTKK RAKPAVPLGA
     NYRLIDIPVS NCLNSNISKI YVLTQFNSAS LNRHLSRAYA SNMGEYKNEG FVEVLAAQQS
     PENPDWFQGT ADAVRQYLWL FEEHNVLEYL ILAGDHLYRM DYEKFIQAHR ETDADITVAA
     LPMDEKRATA FGLMKIDEEG RIIEFAEKPQ GEQLQAMKVD TTILGLDDKR AKEMPFIASM
     GIYVISKDVM LNLLRDKFPG ANDFGSEVIP GATSLGMRVQ AYLYDGYWED IGTIEAFYNA
     NLGITKKPVP DFSFYDRSAP IYTQPRYLPP SKMLDADVTD SVIGEGCVIK NCKIHHSVVG
     LRSCISEGAI IEDSLLMGAD YYETDAERKL LAAKGSVPIG IGKNCLYKRA IIDKNARIGD
     NVKIINKDNV QEAARETDGY FIKSGIVTVI KDALIPSGIV I