ID F6I0L5_VITVI Unreviewed; 527 AA.
AC F6I0L5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000256|RuleBase:RU362093};
DE EC=2.7.7.27 {ECO:0000256|RuleBase:RU362093};
DE AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000256|RuleBase:RU362093};
GN OrderedLocusNames=VIT_03s0038g04570 {ECO:0000313|EMBL:CCB60481.1};
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:CCB60481.1, 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|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|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; FN596508; CCB60481.1; -; Genomic_DNA.
DR RefSeq; XP_002283855.1; XM_002283819.4.
DR AlphaFoldDB; F6I0L5; -.
DR STRING; 29760.F6I0L5; -.
DR PaxDb; 29760-VIT_03s0038g04570-t01; -.
DR EnsemblPlants; Vitvi03g00304_t001; Vitvi03g00304_P001; Vitvi03g00304.
DR GeneID; 100253688; -.
DR Gramene; Vitvi03g00304_t001; Vitvi03g00304_P001; Vitvi03g00304.
DR KEGG; vvi:100253688; -.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_14_4_1; -.
DR InParanoid; F6I0L5; -.
DR OrthoDB; 601725at2759; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000009183; 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:SF4; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE LARGE SUBUNIT 3, 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|RuleBase:RU362093}.
FT DOMAIN 97..373
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 527 AA; 58541 MW; D4F96BF2A216655E CRC64;
MDSCCVTFKA KAHLAKASRG GLSNGDNEFW GERIRGSLNN SGWVSQLAKG LKTEKRPRKI
KPGVACSVIT SNNGKETVTI QAPIFERRRA DPKNVASIIL GGGAGTQLFP LTIRQATPAV
PVGGCYRLID IPMSNCINSN INKIFILTQF NSASLNRHIA RTYFGNGVNF GDGFVEVLAA
TQTPGEAGMK WFEGTADAVR KFIWVFEDAK NKNIENILIL SGDHLYRMDY MDLVQNHIDR
KADITVSCVP VGESRASDYG LLKMDNRGRI IQFAEKPKGA DLKAMKVDTT RLGLSPQEAM
KSPYIASMGV YVFKTDILLN LLRWRYPTSN DFGSEIIPLA VMEHNVEAFL FRDYWEDIGT
IKTFYEANMG LTEEFPKFEF YNPKTPIFTS PRFLPPTKIE QCQVVDAIIS HGCFLRECSV
KHSIVGERSR LDYGVELKDT LMMGADFYQT ESEIASLLAE GNVPIGIGRN TKIRNCIIDK
NAKIGKDAVI VNKDGVQEAD RPDDGFYIRS GITIILEKAT IKDGTVI
//
