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Database: UniProt
Entry: D7TDB6_VITVI
LinkDB: D7TDB6_VITVI
Original site: D7TDB6_VITVI 
ID   D7TDB6_VITVI            Unreviewed;       509 AA.
AC   D7TDB6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 81.
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   OrderedLocusNames=VIT_12s0057g01480 {ECO:0000313|EMBL:CBI28489.3};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI28489.3, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
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; FN595759; CBI28489.3; -; Genomic_DNA.
DR   RefSeq; XP_002263255.1; XM_002263219.4.
DR   AlphaFoldDB; D7TDB6; -.
DR   STRING; 29760.D7TDB6; -.
DR   PaxDb; 29760-VIT_12s0057g01480-t01; -.
DR   EnsemblPlants; Vitvi12g00770_t001; Vitvi12g00770_P001; Vitvi12g00770.
DR   GeneID; 100240927; -.
DR   Gramene; Vitvi12g00770_t001; Vitvi12g00770_P001; Vitvi12g00770.
DR   KEGG; vvi:100240927; -.
DR   eggNOG; KOG1322; Eukaryota.
DR   HOGENOM; CLU_029499_14_4_1; -.
DR   InParanoid; D7TDB6; -.
DR   OMA; YPLTKMR; -.
DR   OrthoDB; 601725at2759; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000009183; Chromosome 12.
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:UP000009183};
KW   Starch biosynthesis {ECO:0000256|RuleBase:RU362093};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362093}.
FT   DOMAIN          81..354
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   509 AA;  55903 MW;  37E5546406288ACC CRC64;
     MASLSALGVT GVVPTSSKSR DLPSSHRTLS FSSRISGNKI TWKASLGSHR RAPVIVSPKA
     VSDSRNSQTC LDPDASRSVL GIILGGGAGT RLYPLTKKRA KPAVPLGANY RLIDIPVSNC
     LNSNISKIYV LTQFNSASLN RHLSRAYASN MGGYKNEGFV EVLAAQQSPE NPNWFQGTAD
     AVRQYLWLFE EHNVLEFLVL AGDHLYRMDY ERFIQAHRET DADITVAALP MDEKRATAFG
     LMKIDEEGRI IEFAEKPKGE QLKAMKVDTT ILGLDDERAK EMPYIASMGI YVVSKDVMLD
     LLRDQFPGAN DFGSEVIPGA TSLGLRVQAY LYDGYWEDIG TIEAFYNANL GITKKPVPDF
     SFYDRSSPIY TQPRYLPPSK MLDADVTDSV IGEGCVIKNC KIHHSVVGLR SCISEGAIIE
     DTLLMGADYY ETDADRRFLM AKGSVPIGIG KNSHIKRAII DKNARIGDNV KIINSDNVQE
     AARETDGYFI KSGIVTVIKD ALLPSGTII
//
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