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Database: UniProt
Entry: B8XEC9_ORYSI
LinkDB: B8XEC9_ORYSI
Original site: B8XEC9_ORYSI 
ID   B8XEC9_ORYSI            Unreviewed;       518 AA.
AC   B8XEC9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=glucose-1-phosphate adenylyltransferase {ECO:0000256|ARBA:ARBA00012460};
DE            EC=2.7.7.27 {ECO:0000256|ARBA:ARBA00012460};
GN   Name=AGPase {ECO:0000313|EMBL:ACJ71341.1};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946 {ECO:0000313|EMBL:ACJ71341.1};
RN   [1] {ECO:0000313|EMBL:ACJ71341.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ma K.-H., Lee G.-A., Gwag J.-G., Lee S.-Y., Lee J.-R., Kim T.-S.,
RA   Park Y.-J.;
RT   "Development of SNP-based CAPS and dCAPS markers in eight different genes
RT   involved in starch biosynthesis in rice.";
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00000956};
CC   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004727}.
CC   -!- SUBUNIT: Heterotetramer composed of two small and two large subunits.
CC       {ECO:0000256|ARBA:ARBA00011822}.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443}.
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DR   EMBL; FJ235704; ACJ71341.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8XEC9; -.
DR   UniPathway; UPA00152; -.
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   CDD; cd02508; ADP_Glucose_PP; 1.
DR   CDD; cd04651; LbH_G1P_AT_C; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 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:SF1; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE LARGE SUBUNIT 2, CYTOSOLIC; 1.
DR   PANTHER; PTHR43523; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR   PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
DR   PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922}.
FT   DOMAIN          88..364
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   518 AA;  57564 MW;  4E1D1D3F9C19C3C3 CRC64;
     MQFMMPLDTN ACAQPMRRAG EGAGTERLME RLNIGGMTQE KALRKRCFGD GVTGTARCVF
     TSDADRDTPH LRTQSSRKNY ADASRVSAVI LGGGTGVQLF PLTSTRAAPA VPVGGCYRLI
     DIPMSNCFNS GINKIFVMTQ FNSASLNRHI HHTYLGGGIN FTDGSVQVLA ATQMPDEPAG
     WFQGTADAIR KFMWILEDHY NQNNIEHVVI LCGDQLYRMN YMELVQKHVD DNADITISCA
     PIDGSRASDY GLVKFDDSGR VIQFLEKPEG ADLESMKVDT SFLSYAIDDK QKYPYIASMG
     IYVLKKDVLL DILKSKYAHL QDFGSEILPR AVLEHNVKAC VFTEYWEDIG TIKSFFDANL
     ALTEQPPKFE FYDPKTPFFT SPRYLPPARL EKCKIKDAII SDGCSFSECT IEHSVIGISS
     RVSIGCELKD TMMMGADQYE TEEETSKLLF EGKVPIGIGE NTKIRNCIID MNARIGRNVI
     IANTQGVQES DHPEEGYYIR SGIVVILKNA TIKDGTVI
//
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