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Database: UniProt
Entry: K4A9S0_SETIT
LinkDB: K4A9S0_SETIT
Original site: K4A9S0_SETIT 
ID   K4A9S0_SETIT            Unreviewed;       456 AA.
AC   K4A9S0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=glucose-1-phosphate adenylyltransferase {ECO:0000256|ARBA:ARBA00012460};
DE            EC=2.7.7.27 {ECO:0000256|ARBA:ARBA00012460};
OS   Setaria italica (Foxtail millet) (Panicum italicum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX   NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQK87239, ECO:0000313|Proteomes:UP000004995};
RN   [1] {ECO:0000313|EnsemblPlants:KQK87239, ECO:0000313|Proteomes:UP000004995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK87239,
RC   ECO:0000313|Proteomes:UP000004995};
RX   PubMed=22580951; DOI=10.1038/nbt.2196;
RA   Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA   Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA   Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA   Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA   Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA   Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT   "Reference genome sequence of the model plant Setaria.";
RL   Nat. Biotechnol. 30:555-561(2012).
RN   [2] {ECO:0000313|EnsemblPlants:KQK87239}
RP   IDENTIFICATION.
RC   STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK87239};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) 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   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443}.
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DR   EMBL; AGNK02005377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; K4A9S0; -.
DR   EnsemblPlants; KQK87239; KQK87239; SETIT_034768mg.
DR   Gramene; KQK87239; KQK87239; SETIT_034768mg.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000004995; Chromosome IX.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:InterPro.
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   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   PANTHER; PTHR43523:SF12; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE LARGE SUBUNIT 1, CHLOROPLASTIC; 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   PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 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   Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW   Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          174..451
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   456 AA;  49861 MW;  04475B1E26371EBE CRC64;
     MPSPPGAKLR NEQSRSVAGC PARPCGGPVQ SHGHERHGSF QSEKERGKEQ RATDGRERRH
     ATPAASLSLS LSLSLSLSLS LPLSRKRAQE RRVQRRLSAM MDLRVAAAAP AGTGVRVLGG
     SVARVPPRPW ALRGKRRLSV RMSVATTEAA TAATAVGASE DQVLESRNAK TVVAVILGGG
     AGTRLFPLTK RRAKPAVPIG GSYRLIDVPM SNCINSGINK VYILTQFNSM SLNRHLSKAY
     DFSNGVAFGN GFVEVLAATQ RPGSEGKRWF QGTADAVRQF DWLFDDAKAK DIEDVLILSG
     DHLYRMDYMD FVQSHRQRGA GISICCLPID GSRASDFGLM KIDDTGRVIS FSEKPKGDEL
     NAMQVDTTVL GLSKEEAEQK PYIASMGVYI FKKDILLNLL RWRFPTANDF GSEIIPASAK
     EINVKAYLFN DYWEDIGTIK SFFEANLALT EQVCLL
//
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