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Database: UniProt
Entry: K3YHE6_SETIT
LinkDB: K3YHE6_SETIT
Original site: K3YHE6_SETIT 
ID   K3YHE6_SETIT            Unreviewed;       479 AA.
AC   K3YHE6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000256|ARBA:ARBA00012460, ECO:0000256|RuleBase:RU362093};
DE            EC=2.7.7.27 {ECO:0000256|ARBA:ARBA00012460, ECO:0000256|RuleBase:RU362093};
DE   AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000256|RuleBase:RU362093};
GN   Name=101759783 {ECO:0000313|EnsemblPlants:KQL01483};
GN   ORFNames=SETIT_6G120500v2 {ECO:0000313|EMBL:RCV30753.1};
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:KQL01483, ECO:0000313|Proteomes:UP000004995};
RN   [1] {ECO:0000313|EMBL:RCV30753.1, ECO:0000313|Proteomes:UP000004995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQL01483,
RC   ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC   {ECO:0000313|EMBL:RCV30753.1};
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|EMBL:RCV30753.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Yugu1 {ECO:0000313|EMBL:RCV30753.1};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQL01483}
RP   IDENTIFICATION.
RC   STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQL01483};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
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. {ECO:0000256|RuleBase:RU362093}.
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         ECO:0000256|RuleBase:RU362093};
CC   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004727, ECO:0000256|RuleBase:RU362093}.
CC   -!- SUBUNIT: Heterotetramer. {ECO:0000256|RuleBase:RU362093}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|RuleBase:RU362093}.
CC   -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC       adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443,
CC       ECO:0000256|RuleBase:RU362093}.
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DR   EMBL; AGNK02003745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM003533; RCV30753.1; -; Genomic_DNA.
DR   AlphaFoldDB; K3YHE6; -.
DR   SMR; K3YHE6; -.
DR   EnsemblPlants; KQL01483; KQL01483; SETIT_013574mg.
DR   EnsemblPlants; KQL01484; KQL01484; SETIT_013574mg.
DR   Gramene; KQL01483; KQL01483; SETIT_013574mg.
DR   Gramene; KQL01484; KQL01484; SETIT_013574mg.
DR   HOGENOM; CLU_029499_14_4_1; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000004995; Chromosome VI.
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   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   NCBIfam; TIGR02091; glgC; 1.
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   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 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, ECO:0000256|RuleBase:RU362093};
KW   Chloroplast {ECO:0000256|RuleBase:RU362093};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362093};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU362093};
KW   Plastid {ECO:0000256|RuleBase:RU362093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW   Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922,
KW   ECO:0000256|RuleBase:RU362093};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362093}.
FT   DOMAIN          51..324
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  52593 MW;  BAEFC8837CD72486 CRC64;
     MDVALASKGF PSPSNATMEQ PISKRDKAVA NDSSASKHTY LDPNANDSVL GIILGGGAGT
     RLYPLTKKRA KPAVPLGANY RLIDIPVSNC LNSNISKIYV LTQFNSASLN RHLSRAYGSN
     IGGYKNEGFV EVLAAQQSPD NPNWFQGTAD AVRQYLWLFE EHNVMEFIIL AGDHLYRMDY
     EKFIQAHRET DADITVAALP MDEKRATAFG LMKIDEEGRI IEFAEKPKGD QLKAMMVDTT
     ILGLDDVRAK EMPYIASMGI YVFSKDVMLQ LLREQFPGAN DFGSEVIPGA TSIGKRVQAY
     LYDGYWEDIG TIEAFYNANL GITKKPIPDF SFYDRSAPIY TQPRHLPPSK ILDADVTDSV
     IGEGCVIKNC KIHHSVVGLR SCISEGAIIE DTLLMGADYY ETEADKKLLA ENGGIPIGIG
     KNSHIRRAII DKNARIGDNV KIINADNVQE AARETDGYFI KGGIVTVIKD ALLPSGTVI
//
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