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Database: UniProt
Entry: A0A1S4D6R7_TOBAC
LinkDB: A0A1S4D6R7_TOBAC
Original site: A0A1S4D6R7_TOBAC 
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
//
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