ID   GLGS2_VICFA             Reviewed;         512 AA.
AC   P52417;
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 2, 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=AGPP;
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: Leaves and 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 the end of the cell expansion phase (35-40
CC       daf) and with the beginning of the seeds desiccation phase at 50 daf,
CC       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; X76941; CAA54260.1; -; mRNA.
DR   PIR; S41292; S41292.
DR   AlphaFoldDB; P52417; -.
DR   SMR; P52417; -.
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..63
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           64..512
FT                   /note="Glucose-1-phosphate adenylyltransferase small
FT                   subunit 2, chloroplastic"
FT                   /id="PRO_0000011157"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   512 AA;  56060 MW;  060647F683526EDC CRC64;
     MAAIGVLKVP PSSSSSSSSS SSKAIARNLS FTSSHLSGDK IFTLSGRTRR TSGRNPFIVS
     PKAVSDSKNS QTCLDPDASR SVLGIILGGG AGTRLYPLTK KRAKPAVPLG ANYRLIDIPV
     SNCLNSNISK IYVLTQFNSA SLNRHLSRAY ASNLGGYKNE GFVEVLAAQQ SPENPNWFQG
     TADAVRQYLW LFEEHNVLEY LVLAGDHLYR MDYERFIQAH RESDADITVA ALPMDEARAT
     AFGLMKIDEE GRIIEFSENP KGEQLKAMKV DTTILGLDDD RAKEMPYIAS MGIYVVSKHV
     MLDLLRDKFP GANDFGSEVI PGATELGMRV QAYLYDGYWE DIGTIEAFYN ANLGITKKPV
     PDFSFYDRSS PIYTQPRYLP PSKMLDADIT DSVIGEGCVI KNCKIHHSVV GLRSCISEGA
     IIEDTLLMGA DYYETDADRR FLAAKGGVPI GIGKNSHIRR AIIDKNARIG DDVKIINSDN
     VQEAARETEG YFIKSGIVTV IKDALIPSGT VI