ID GLGL4_ARATH Reviewed; 523 AA.
AC Q9SIK1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 159.
DE RecName: Full=Probable glucose-1-phosphate adenylyltransferase large subunit, chloroplastic;
DE EC=2.7.7.27;
DE AltName: Full=ADP-glucose pyrophosphorylase;
DE AltName: Full=ADP-glucose synthase;
DE AltName: Full=AGPase S;
DE AltName: Full=Alpha-D-glucose-1-phosphate adenyl transferase;
DE Flags: Precursor;
GN OrderedLocusNames=At2g21590; ORFNames=F2G1.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 (By similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Activated by 3'phosphoglycerate, inhibited by
CC orthophosphate. Allosteric regulation (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC -!- SUBUNIT: Heterotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; AC007119; AAD23646.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07199.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07200.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62852.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62853.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62854.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62855.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62856.1; -; Genomic_DNA.
DR EMBL; AY070429; AAL49924.1; -; mRNA.
DR EMBL; AY096657; AAM20291.1; -; mRNA.
DR PIR; A84603; A84603.
DR RefSeq; NP_001031391.1; NM_001036314.2.
DR RefSeq; NP_001324978.1; NM_001335766.1.
DR RefSeq; NP_001324979.1; NM_001335767.1.
DR RefSeq; NP_001324980.1; NM_001335768.1.
DR RefSeq; NP_001324981.1; NM_001335769.1.
DR RefSeq; NP_001324982.1; NM_001335765.1.
DR RefSeq; NP_179753.1; NM_127730.5.
DR AlphaFoldDB; Q9SIK1; -.
DR SMR; Q9SIK1; -.
DR BioGRID; 2050; 1.
DR IntAct; Q9SIK1; 1.
DR STRING; 3702.Q9SIK1; -.
DR iPTMnet; Q9SIK1; -.
DR PaxDb; 3702-AT2G21590-2; -.
DR ProteomicsDB; 220772; -.
DR EnsemblPlants; AT2G21590.1; AT2G21590.1; AT2G21590.
DR EnsemblPlants; AT2G21590.2; AT2G21590.2; AT2G21590.
DR EnsemblPlants; AT2G21590.3; AT2G21590.3; AT2G21590.
DR EnsemblPlants; AT2G21590.4; AT2G21590.4; AT2G21590.
DR EnsemblPlants; AT2G21590.5; AT2G21590.5; AT2G21590.
DR EnsemblPlants; AT2G21590.6; AT2G21590.6; AT2G21590.
DR EnsemblPlants; AT2G21590.7; AT2G21590.7; AT2G21590.
DR GeneID; 816697; -.
DR Gramene; AT2G21590.1; AT2G21590.1; AT2G21590.
DR Gramene; AT2G21590.2; AT2G21590.2; AT2G21590.
DR Gramene; AT2G21590.3; AT2G21590.3; AT2G21590.
DR Gramene; AT2G21590.4; AT2G21590.4; AT2G21590.
DR Gramene; AT2G21590.5; AT2G21590.5; AT2G21590.
DR Gramene; AT2G21590.6; AT2G21590.6; AT2G21590.
DR Gramene; AT2G21590.7; AT2G21590.7; AT2G21590.
DR KEGG; ath:AT2G21590; -.
DR Araport; AT2G21590; -.
DR TAIR; AT2G21590; APL4.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_14_4_1; -.
DR InParanoid; Q9SIK1; -.
DR OMA; QYIASMG; -.
DR OrthoDB; 601725at2759; -.
DR PhylomeDB; Q9SIK1; -.
DR BRENDA; 2.7.7.27; 399.
DR SABIO-RK; Q9SIK1; -.
DR UniPathway; UPA00152; -.
DR PRO; PR:Q9SIK1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIK1; baseline and differential.
DR Genevisible; Q9SIK1; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0010170; C:glucose-1-phosphate adenylyltransferase complex; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IDA:TAIR.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0019252; P:starch biosynthetic process; TAS:TAIR.
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:SF14; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE LARGE SUBUNIT, CHLOROPLASTIC-RELATED; 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 2: Evidence at transcript level;
KW Allosteric enzyme; ATP-binding; Chloroplast; Nucleotide-binding;
KW Nucleotidyltransferase; Plastid; Reference proteome; Starch biosynthesis;
KW Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..523
FT /note="Probable glucose-1-phosphate adenylyltransferase
FT large subunit, chloroplastic"
FT /id="PRO_0000011162"
SQ SEQUENCE 523 AA; 58205 MW; 6A53681F86129565 CRC64;
MDSSYSFALG TSSSILPKLS FRNVENRFYG EKNNNNGLCK RFGSDLGSKK FRNQKFKHGV
VYAVATSDNP KKAMTVKTSM FERRKVDPQN VAAIILGGGN GAKLFPLTMR AATPAVPVGG
CYRLIDIPMS NCINSCINKI FVLTQFNSAS LNRHLARTYF GNGINFGGGF VEVLAATQTP
GEAGKKWFQG TADAVRKFLW VFEDAKNRNI ENILILSGDH LYRMNYMDFV QSHVDSNADI
TLSCAPVSES RASNFGLVKI DRGGRVIHFS EKPTGVDLKS MQTDTTMLGL SHQEATDSPY
IASMGVYCFK TEALLNLLTR QYPSSNDFGS EVIPAAIRDH DVQGYIFRDY WEDIGTIKTF
YEANLALVEE RPKFEFYDPE TPFYTSPRFL PPTKAEKCRM VDSIISHGCF LRECSVQRSI
IGERSRLDYG VELQDTLMLG ADYYQTESEI ASLLAEGKVP IGIGKDTKIR KCIIDKNAKI
GKNVIIMNKG DVQEADRPEE GFYIRSGITV IVEKATIQDG TVI
//
