GLGL1_ARATH
ID GLGL1_ARATH Reviewed; 522 AA.
AC P55229; O04929; Q9SXS1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase large subunit 1, 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 Name=ADG2; Synonyms=APL1; OrderedLocusNames=At5g19220; ORFNames=T24G5.120;
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=9193079; DOI=10.1046/j.1365-313x.1997.11051121.x;
RA Wang S.-M., Chu B., Lue W.-L., Yu T.-S., Eimert K., Chen J.;
RT "adg2-1 represents a missense mutation in the ADPG pyrophosphorylase large
RT subunit gene of Arabidopsis thaliana.";
RL Plant J. 11:1121-1126(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Ito H., Sokolov L.N., Kleczkowski L.A., Okita T.W.;
RT "The Arabidopsis thaliana ADP glucose pyrophosphorylase large subunit gene,
RT adg2.";
RL (er) Plant Gene Register PGR99-051(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=10431387; DOI=10.1515/znc-1999-5-610;
RA Kleczkowski L.A., Sokolov L.N., Luo C., Villand P.;
RT "Molecular cloning and spatial expression of an osmotic-responsive cDNA for
RT the large subunit of ADP-glucose pyrophosphorylase from Arabidopsis
RT thaliana.";
RL Z. Naturforsch. C 54:353-358(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [5]
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 [6]
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).
RN [7]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 297-480.
RC STRAIN=cv. Columbia;
RX PubMed=8292792; DOI=10.1007/bf00042361;
RA Villand P., Olsen O.-A., Kleczkowski L.A.;
RT "Molecular characterization of multiple cDNA clones for ADP-glucose
RT pyrophosphorylase from Arabidopsis thaliana.";
RL Plant Mol. Biol. 23:1279-1284(1993).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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.
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.
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC -!- SUBUNIT: Heterotetramer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- TISSUE SPECIFICITY: Leaves.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; U72290; AAB58475.1; -; mRNA.
DR EMBL; AB022891; BAA76362.1; -; Genomic_DNA.
DR EMBL; X73367; CAA51779.2; -; mRNA.
DR EMBL; AC069326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92672.1; -; Genomic_DNA.
DR EMBL; BT008884; AAP68323.1; -; mRNA.
DR EMBL; AF370503; AAK43880.1; -; mRNA.
DR PIR; S42548; S42548.
DR PIR; T52629; T52629.
DR RefSeq; NP_197423.1; NM_121927.3.
DR AlphaFoldDB; P55229; -.
DR SMR; P55229; -.
DR BioGRID; 17318; 3.
DR STRING; 3702.AT5G19220.1; -.
DR iPTMnet; P55229; -.
DR PaxDb; P55229; -.
DR PRIDE; P55229; -.
DR ProteomicsDB; 221896; -.
DR EnsemblPlants; AT5G19220.1; AT5G19220.1; AT5G19220.
DR GeneID; 832042; -.
DR Gramene; AT5G19220.1; AT5G19220.1; AT5G19220.
DR KEGG; ath:AT5G19220; -.
DR Araport; AT5G19220; -.
DR TAIR; locus:2182132; AT5G19220.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_14_4_1; -.
DR InParanoid; P55229; -.
DR OMA; YRMDFSQ; -.
DR OrthoDB; 806744at2759; -.
DR PhylomeDB; P55229; -.
DR BioCyc; ARA:AT5G19220-MON; -.
DR BioCyc; MetaCyc:MON-1823; -.
DR BRENDA; 2.7.7.27; 399.
DR SABIO-RK; P55229; -.
DR UniPathway; UPA00152; -.
DR PRO; PR:P55229; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P55229; baseline and differential.
DR Genevisible; P55229; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA: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; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 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 PANTHER; PTHR43523; PTHR43523; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR02091; glgC; 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 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Chloroplast; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Plastid; Reference proteome;
KW Starch biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 55..522
FT /note="Glucose-1-phosphate adenylyltransferase large
FT subunit 1, chloroplastic"
FT /id="PRO_0000011159"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 196
FT /note="Q -> R (in Ref. 2; BAA76362)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 57674 MW; F66CCF1A877A52C4 CRC64;
MVVSADCRIS LSAPSCIRSS STGLTRHIKL GSFCNGELMG KKLNLSQLPN IRLRSSTNFS
QKRILMSLNS VAGESKVQEL ETEKRDPRTV ASIILGGGAG TRLFPLTKRR AKPAVPIGGA
YRLIDVPMSN CINSGINKVY ILTQYNSASL NRHLARAYNS NGLGFGDGYV EVLAATQTPG
ESGKRWFQGT ADAVRQFHWL FEDARSKDIE DVLILSGDHL YRMDYMDFIQ DHRQSGADIS
ISCIPIDDRR ASDFGLMKID DKGRVISFSE KPKGDDLKAM AVDTTILGLS KEEAEKKPYI
ASMGVYVFKK EILLNLLRWR FPTANDFGSE IIPFSAKEFY VNAYLFNDYW EDIGTIRSFF
EANLALTEHP GAFSFYDAAK PIYTSRRNLP PSKIDNSKLI DSIISHGSFL TNCLIEHSIV
GIRSRVGSNV QLKDTVMLGA DYYETEAEVA ALLAEGNVPI GIGENTKIQE CIIDKNARVG
KNVIIANSEG IQEADRSSDG FYIRSGITVI LKNSVIKDGV VI
