ID B6VCL9_AEGSP Unreviewed; 189 AA.
AC B6VCL9;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 45.
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};
DE Flags: Fragment;
OS Aegilops speltoides (Goatgrass) (Triticum speltoides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=4573 {ECO:0000313|EMBL:ACJ06618.1};
RN [1] {ECO:0000313|EMBL:ACJ06618.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18289404; DOI=10.1017/S0016672307009032;
RA Haudry A., Cenci A., Guilhaumon C., Paux E., Poirier S., Santoni S.,
RA David J., Glemin S.;
RT "Mating system and recombination affect molecular evolution in four
RT Triticeae species.";
RL Genet. Res. 90:97-109(2008).
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 -!- SUBCELLULAR LOCATION: Plastid, amyloplast
CC {ECO:0000256|ARBA:ARBA00004602}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443}.
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DR EMBL; FJ374556; ACJ06618.1; -; Genomic_DNA.
DR AlphaFoldDB; B6VCL9; -.
DR UniPathway; UPA00152; -.
DR GO; GO:0009501; C:amyloplast; 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 GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
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:SF29; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE LARGE SUBUNIT 2, 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; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
DR PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1.
PE 3: Inferred from homology;
KW Amyloplast {ECO:0000256|ARBA:ARBA00023234};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000313|EMBL:ACJ06618.1};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922};
KW Transferase {ECO:0000313|EMBL:ACJ06618.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 1..186
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACJ06618.1"
FT NON_TER 189
FT /evidence="ECO:0000313|EMBL:ACJ06618.1"
SQ SEQUENCE 189 AA; 21327 MW; 3DD2E98E69696384 CRC64;
INKIFVMTQF NSASLNRHIH RTYLGGGINF TDGSVEVLAA TQMPGEAAGW FRGTADAVRK
FIWVLEDYYK NKSIEHILIL SGDQLYRMDY MELVQKHVDD NADITLSCAP VGESRASEYG
LVKFDSSGRV VQFSEKPKGA DLEAMKVDTS FLNFAIDDTD KYPYIASMGV YVFKRDVLLN
LLKSRYAEL
//
