ID   GLGS_BETVU              Reviewed;         489 AA.
AC   P55232;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic/amyloplastic;
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; Fragment;
GN   Name=AGPB1;
OS   Beta vulgaris (Sugar beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=161934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Zuchtlinie 5S0026; TISSUE=Tap root;
RX   PubMed=7865789; DOI=10.1007/bf00019190;
RA   Mueller-Roeber B., Nast G., Willmitzer L.;
RT   "Isolation and expression analysis of cDNA clones encoding a small and a
RT   large subunit of ADP-glucose pyrophosphorylase from sugar beet.";
RL   Plant Mol. Biol. 27:191-197(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: Prominently expressed in the leaves. A lower level
CC       expression is seen in the roots.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000305}.
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DR   EMBL; X78899; CAA55515.1; -; mRNA.
DR   PIR; S51943; S51943.
DR   AlphaFoldDB; P55232; -.
DR   SMR; P55232; -.
DR   PRIDE; P55232; -.
DR   BRENDA; 2.7.7.27; 836.
DR   UniPathway; UPA00152; -.
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..52
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           53..489
FT                   /note="Glucose-1-phosphate adenylyltransferase small
FT                   subunit, chloroplastic/amyloplastic"
FT                   /id="PRO_0000011150"
FT   NON_TER         1
SQ   SEQUENCE   489 AA;  53796 MW;  7460A8748711C36D CRC64;
     ITVPSTSSKN LQNSLAFSSS SLSGDKIQTT SFLNRRYCRI SSRAPIVVSP KAVSDSKNSQ
     TCLDPEASRS VLGIILGGGA GTRLYPLTKK RAKPAVPLGA NYRLIDIPVS NCLNSNISKI
     YVLTQFNSAS LNRHLSRAYA SNMGGYKNEG FVEVLAAQQS PENPNWFQGT ADAVRQYLWL
     FEEHNVLEYL ILAGDHLYRM DYERFVQAHR ETDADITVAA LPMDEKRATA FGLMKIDEEG
     RIIEFAEKPK GEQLKAMKVD TTILGLDDER AKEMPFIASM GIYVISKDVM LNLLREQFPG
     ANDFGSEVIP GATSIGLRVQ AYLYDGYWED IGTIEAFYNA NLGITKKPVP DFSFYDRSSP
     IYTQPRYLPP SKMLDADITD SVIGEGCVIK NCKIHHSVIG LRSCISEGAI IEDTLLMGAD
     YYETDADRKF LAAKGSVPIG IGNARIGDDV KIINSDNVQE AARETDGYFI KSGIVTIIKD
     AMIPSGTVI