GLGS_HORVU
ID GLGS_HORVU Reviewed; 513 AA.
AC P55238;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
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;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Bomi; TISSUE=Leaf, and Starchy endosperm;
RX PubMed=8546676; DOI=10.1042/bj3130149;
RA Thorbjoernsen T., Villand P., Kleczkowski L.A., Olsen O.-A.;
RT "A single gene encodes two different transcripts for the ADP-glucose
RT pyrophosphorylase small subunit from barley (Hordeum vulgare).";
RL Biochem. J. 313:149-154(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 285-470.
RC STRAIN=cv. Bomi; TISSUE=Seed;
RX PubMed=1320425; DOI=10.1007/bf00023385;
RA Villand P., Aalen R., Olsen O.-A., Luethi E., Loenneborg A.,
RA Kleczkowski L.A.;
RT "PCR amplification and sequences of cDNA clones for the small and large
RT subunits of ADP-glucose pyrophosphorylase from barley tissues.";
RL Plant Mol. Biol. 19:381-389(1992).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P55238-1; Sequence=Displayed;
CC Name=2; Synonyms=BEPSF1;
CC IsoId=P55238-2; Sequence=VSP_001752;
CC -!- TISSUE SPECIFICITY: Leaves and starchy endosperm.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; Z48563; CAA88450.1; -; mRNA.
DR EMBL; Z48562; CAA88449.1; -; mRNA.
DR EMBL; Z48578; CAA88462.1; -; Genomic_DNA.
DR EMBL; Z48578; CAA88461.1; -; Genomic_DNA.
DR EMBL; X62241; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S22524; S22524.
DR PIR; S61478; S61478.
DR PIR; S61479; S61479.
DR AlphaFoldDB; P55238; -.
DR SMR; P55238; -.
DR BRENDA; 2.7.7.27; 2687.
DR SABIO-RK; P55238; -.
DR UniPathway; UPA00152; -.
DR ExpressionAtlas; P55238; 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 2: Evidence at transcript level;
KW Allosteric enzyme; Alternative splicing; Amyloplast; ATP-binding;
KW Chloroplast; Nucleotide-binding; Nucleotidyltransferase; Plastid;
KW Starch biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..64
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 65..513
FT /note="Glucose-1-phosphate adenylyltransferase small
FT subunit, chloroplastic/amyloplastic"
FT /id="PRO_0000011152"
FT VAR_SEQ 1..81
FT /note="MAMAAAASPSKILIPPHRASAVTAAASTSCDSLRLLCAPRGRPGPRGLVARP
FT VPRRPFFFSPRAVSDSKSSQTCLDPDAST -> MDVPLASKVPLPSPSKHEQCNVYSHK
FT SSSKHADLNPHAID (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8546676"
FT /id="VSP_001752"
FT CONFLICT 285..286
FT /note="EM -> KY (in Ref. 2; X62241)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="S -> G (in Ref. 2; X62241)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="T -> A (in Ref. 2; X62241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 56049 MW; 2314BFB79D521818 CRC64;
MAMAAAASPS KILIPPHRAS AVTAAASTSC DSLRLLCAPR GRPGPRGLVA RPVPRRPFFF
SPRAVSDSKS SQTCLDPDAS TSVLGIILGG GAGTRLYPLT KKRAKPAVPL GANYRLIDIP
VSNCLNSNIS KIYVLTQFNS ASLNRHLSRA YGSNIGGYKN EGFVEVLAAQ QSPDNPDWFQ
GTADAVRQYL WLFEEHNVME YLILAGDHLY RMDYEKFIQA HRETDADITV AALPMDEERA
TAFGLMKIDE EGRIIEFAEK PKGEQLKAMM VDTTILGLED ARAKEMPYIA SMGIYVISKH
VMLQLLREQF PGANDFGSEV IPGATSTGMR VQAYLYDGYW EDIGTIEAFY NANLGITKKP
IPDFSFYDRS APIYTQPRHL PPSKVLDADV TDSVIGEGCV IKNCKIHHSV VGLRSCISEG
AIIEDTLLMG ADYYETEADK KLLAEKGGIP IGIGKNSHIK RAIIDKNARI GDNVMIINVD
NVQEAARETD GYFIKSGIVT VIKDALLPSG TVI
