ID V7C6W6_PHAVU Unreviewed; 521 AA.
AC V7C6W6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 ORFNames=PHAVU_003G076500g {ECO:0000313|EMBL:ESW25917.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW25917.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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 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|RuleBase:RU362093};
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004727, ECO:0000256|RuleBase:RU362093}.
CC -!- SUBUNIT: Heterotetramer. {ECO:0000256|ARBA:ARBA00011680,
CC ECO:0000256|RuleBase:RU362093}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229, 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; CM002290; ESW25917.1; -; Genomic_DNA.
DR RefSeq; XP_007153923.1; XM_007153861.1.
DR AlphaFoldDB; V7C6W6; -.
DR STRING; 3885.V7C6W6; -.
DR EnsemblPlants; ESW25917; ESW25917; PHAVU_003G076500g.
DR GeneID; 18634207; -.
DR Gramene; ESW25917; ESW25917; PHAVU_003G076500g.
DR KEGG; pvu:PHAVU_003G076500g; -.
DR eggNOG; KOG1322; Eukaryota.
DR OMA; YRMDFSQ; -.
DR OrthoDB; 601725at2759; -.
DR PhylomeDB; V7C6W6; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000000226; Chromosome 3.
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|ARBA:ARBA00022528, 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:UP000000226};
KW Starch biosynthesis {ECO:0000256|RuleBase:RU362093};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362093}.
FT DOMAIN 90..367
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 521 AA; 57840 MW; C5E186D6E4917725 CRC64;
MAASAVGQIT VSSVQLHGMG CGRNWKLVKF CNGELMGRKV QLKTGASRSA YTKNVKPQHR
ICMSLTADLS TESKLRDLEM ERRNARTVLA VILGGGAGTR LFPLTKRRAK PAVPIGGAYR
LIDVPMSNCI NSGINKVYIL TQYNSASLNR HIARAYNSGN GVTFGDGYVE VLAATQTPGE
AGKKWFQGTA DAVRQFHWLF EDPRSKGIED VLILSGDHLY RMDYMDFVRN HRESGADITL
SCLPMDDSRA SDFGLMKIDN KGRILSFSEK PKGEELKAMQ VDTTVLGLSK DEAQKKPYIA
SMGVYVFKKE ILLNLLRWRF PTANDFGSEV IPASAREYYM KAYLFNDYWE DIGTIRSFFE
ANLALTEHPS RFSFYDAAKP MYTSRRNLPP SKIDNSKIVD SIISHGSFLN NSLIEHSVVG
IRSRINSNVH LKDTVMLGAD FYETDAEVAE LLAEGRVPIG IGENTKIKDC IIDKNARIGK
NVVIANSEGI QEADRSSEGF YIRSGVTIVL KNSVIEDGLI I
//
