ID A0A1S4D6R7_TOBAC Unreviewed; 528 AA.
AC A0A1S4D6R7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
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 Name=LOC107826565 {ECO:0000313|RefSeq:XP_016509038.1,
GN ECO:0000313|RefSeq:XP_016509039.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016509038.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016509038.1, ECO:0000313|RefSeq:XP_016509039.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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 RefSeq; XP_016509038.1; XM_016653552.1.
DR RefSeq; XP_016509039.1; XM_016653553.1.
DR STRING; 4097.A0A1S4D6R7; -.
DR PaxDb; 4097-A0A1S4D6R7; -.
DR GeneID; 107826565; -.
DR KEGG; nta:107826565; -.
DR OMA; SHCRIID; -.
DR OrthoDB; 601725at2759; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000084051; Unplaced.
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|RuleBase:RU362093};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362093};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU362093,
KW ECO:0000313|RefSeq:XP_016509038.1};
KW Plastid {ECO:0000256|RuleBase:RU362093};
KW Reference proteome {ECO:0000313|Proteomes:UP000084051};
KW Starch biosynthesis {ECO:0000256|RuleBase:RU362093};
KW Transferase {ECO:0000256|RuleBase:RU362093}.
FT DOMAIN 98..373
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 528 AA; 58367 MW; DA28908A87F7D823 CRC64;
MDTCFVALKS TAHLGRVSKG GFENGEKEFL GEQIRGSLNN NNLRVNNLSK SLKLEKKESK
IKPGVAFSVI TTENGKETLT VEAPRFDRRR ANPKNVASVI LGGGAGTKLF PLTSRAATPA
VPVGGCYRLI DIPMSNCINS GINKIFVLTQ YNSAPLNRHI ARTYFGNGVS FGDGFVEVLA
ATQTPGETGK KWFQGTADAV RQFIWVFEDA KNKDVDNILI LSGDHLYRMD YMDLVQNHID
RNSDITLSCA PACDSRASDF GLVKIDSRGR VVQFAEKPKG FDLKAMQVDT TLIGLSPQEA
KRSPYIASMG VYVFKTDVLL KLLKWRYPTA NDFGSEIIPA AINEHNVQAY IFRDYWEDIG
TIKSFYDANL ALTAESPKFE FYDPKTPFYT SPRFLPPTKI DNCKIKDAII SHGCFLRECS
VDHSIVGERS RLDCGVELKD TLMMGADYYQ TESEIASLLA EGKVPIGVGE NTKIRNCIID
KNAKIGKDVV IMNKDGVQEA DRPEEGFYIR AGLTIVAEKA TIKDGTVI
//