ID Q7DLJ8_IPOBA Unreviewed; 302 AA. AC Q7DLJ8; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-NOV-2024, entry version 63. DE RecName: Full=glucose-1-phosphate adenylyltransferase {ECO:0000256|ARBA:ARBA00012460}; DE EC=2.7.7.27 {ECO:0000256|ARBA:ARBA00012460}; DE AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000256|ARBA:ARBA00032494}; DE AltName: Full=ADP-glucose synthase {ECO:0000256|ARBA:ARBA00030817}; DE AltName: Full=Alpha-D-glucose-1-phosphate adenyl transferase {ECO:0000256|ARBA:ARBA00030645}; OS Ipomoea batatas (Sweet potato) (Convolvulus batatas). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea. OX NCBI_TaxID=4120 {ECO:0000313|EMBL:CAA86726.1}; RN [1] {ECO:0000313|EMBL:CAA86726.1} RP NUCLEOTIDE SEQUENCE. RA Kim Y., Shin H., Lee M., Son C., Song H., Lee D., Yoo O., Liu J.; RT "cDNA Cloning and Regulation of ADP-Glucose Pyrophosphorylase Small Subunit RT Gene in Sweet Potato."; RL Plant Mol. Biol. 0:0-0(1994). 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|ARBA:ARBA00002231}. 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. {ECO:0000256|ARBA:ARBA00011680}. CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z46756; CAA86726.1; -; mRNA. DR AlphaFoldDB; Q7DLJ8; -. 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:InterPro. DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro. DR CDD; cd04651; LbH_G1P_AT_C; 1. DR FunFam; 2.160.10.10:FF:000010; Glucose-1-phosphate adenylyltransferase; 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: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; PS00810; ADP_GLC_PYROPHOSPH_3; 1. PE 2: Evidence at transcript level; KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922}. FT DOMAIN 1..147 FT /note="Nucleotidyl transferase" FT /evidence="ECO:0000259|Pfam:PF00483" SQ SEQUENCE 302 AA; 33374 MW; 3789A9AE78FD2AB6 CRC64; MDYERFIQAH RETDADITVA ALPMDEKRAT AFGLMKIDEE GRIIEFAEKP KREQLKAMKV DTTILGLDDQ RAKELPFIAS MGIYVISKNV MLNLLREKFP GANDFGSEVI PGATSIGMRV QAYLFDGYWE DIGTIEAFYN ANLGITKKPV PDFSFYDRSA PISTTPRYLP PSKMLDADVT DSVIGEGCVI KNCKIHHSVV GLRSCISEGA IIEDSLLMGA DYYETDADRR LLAAKGSVPI GIGRNSHIKR AIIHNIARIG NDVKIINNDN VQEAARETEG YFIKSGIVTI IKDALIPSGT II //