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Database: UniProt
Entry: A0A0D9V396_9ORYZ
LinkDB: A0A0D9V396_9ORYZ
Original site: A0A0D9V396_9ORYZ 
ID   A0A0D9V396_9ORYZ        Unreviewed;       476 AA.
AC   A0A0D9V396;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=glucose-1-phosphate adenylyltransferase {ECO:0000256|ARBA:ARBA00012460};
DE            EC=2.7.7.27 {ECO:0000256|ARBA:ARBA00012460};
OS   Leersia perrieri.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX   NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR01G20380.1, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR01G20380.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:LPERR01G20380.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA   Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA   Zhang J., Wing R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:LPERR01G20380.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   AlphaFoldDB; A0A0D9V396; -.
DR   STRING; 77586.A0A0D9V396; -.
DR   EnsemblPlants; LPERR01G20380.1; LPERR01G20380.1; LPERR01G20380.
DR   EnsemblPlants; LPERR01G20380.2; LPERR01G20380.2; LPERR01G20380.
DR   Gramene; LPERR01G20380.1; LPERR01G20380.1; LPERR01G20380.
DR   Gramene; LPERR01G20380.2; LPERR01G20380.2; LPERR01G20380.
DR   eggNOG; KOG1322; Eukaryota.
DR   HOGENOM; CLU_029499_14_4_1; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000032180; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
DR   GO; GO:0010170; C:glucose-1-phosphate adenylyltransferase complex; IEA:EnsemblPlants.
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; 2.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR   PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1.
DR   PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW   Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922}.
FT   DOMAIN          88..275
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          278..322
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   476 AA;  52630 MW;  4474DF6416CC6245 CRC64;
     MQFMMPLDTN SCAQPMRRAG ESAGTDRLME RLNIGGMTQE KALRKRCFGD GVAGTARCVF
     TSDADADSLH LRTQSSRKNY ADASRVSAVI LGGGTGAKLF PLTSTRATPA VPVGGCYRLI
     DIPMSNCFNS GINKIFVMTQ FNSASLNRHI HCTYLGGGIN FTDGSVQVLA ATQMPEEPAG
     WFQGTADAIR KFMWILEDYY NQNDIEHIII LNGDQFYRMN YMELVQKHVD DNADITISCA
     PVEGSRASEY GLVKFDSSGR VIQFFEKPEG ADLESMVLND FGSEILPRAV LEHNAKACVF
     TEYWEDIGTI KSFFDANLAL TEQPPKFEFY DPKTPFFTSP RYLPPARLEK CKIKDAIISD
     GCSFSECTIE HSVIGICSRI SIGCELKDTM MMGSDLYETE EETSKLLLEG KVPIGIGKNT
     KIRNCIIDMN ARIGRNVVIA NTEGVQEADH PEEGYYIRSG IVVILKNATI KDGSVI
//
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