ID   GLGS1_VICFA             Reviewed;         508 AA.
AC   P52416;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Glucose-1-phosphate adenylyltransferase small subunit 1, 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;
GN   Name=AGPC;
OS   Vicia faba (Broad bean) (Faba vulgaris).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX   NCBI_TaxID=3906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Fribo; TISSUE=Cotyledon;
RX   PubMed=7766042; DOI=10.1007/bf00202592;
RA   Weber H., Heim U., Borisjuk L., Wobus U.;
RT   "Cell-type specific, coordinate expression of two ADP-glucose
RT   pyrophosphorylase genes in relation to starch biosynthesis during seed
RT   development of Vicia faba L.";
RL   Planta 195:352-361(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 {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Seeds.
CC   -!- DEVELOPMENTAL STAGE: It is present in young cotyledons at 14 days after
CC       fertilization (daf) when cells are still rapidly dividing. Levels
CC       steadily accumulate until 30 daf and with the beginning of the seeds
CC       desiccation phase at 50 daf the levels decrease to very low levels.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000305}.
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DR   EMBL; X76940; CAA54259.1; -; mRNA.
DR   PIR; S41293; S41293.
DR   AlphaFoldDB; P52416; -.
DR   SMR; P52416; -.
DR   BRENDA; 2.7.7.27; 986.
DR   UniPathway; UPA00152; -.
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; Starch biosynthesis; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..59
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           60..508
FT                   /note="Glucose-1-phosphate adenylyltransferase small
FT                   subunit 1, chloroplastic"
FT                   /id="PRO_0000011156"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   508 AA;  55627 MW;  2B95F93CBC14D9F2 CRC64;
     MSSIVTSGVI NVPRSSSSSK NLSFSSSSQL SGNKILTVSG NGAPRGRCTL KHVFLTPKAV
     SDSQNSQTCL DPDASRSVLG IILGGGAGTR LYPLTKKRAK PAVPLGANYR LIDIPVSNCL
     NSNISKIYVL TQFNSASLNR HLSRAYASNL GGYKNEGFVE VLAAQQSPEN PNWFQGTADA
     VRQYLWLFEE HNVLEYLILA GDHLYRMDYE KFIQAHRESD ADITVAALPM DEKRATAFGL
     MKIDEEGRII EFAEKPKGEQ LKAMKVDTTI LGLDDERAKE MPFIASMGIY VISKNVMLDL
     LRDKFPGAND FGSEVIPGAT SIGMRVQAYL YDGYWEDIGT IEAFYNANLG ITKKPVPDFS
     FYDRSSPIYT QPRYLPPSKM LDADITDSVI GEGCVIKNCK IFHSVVGLRS CISEGAIIED
     TLLMGADYYE TEADKRFLAA KGSVPIGIGK NSHIKRAIVD KNARIGENVK IINSDNVQEA
     ARETEGYFIK SGIVTIIKDA LIPSGTVL