GLGL3_ARATH
ID GLGL3_ARATH Reviewed; 521 AA.
AC P55231; Q9ZR38;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase large subunit 3, 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=APL3; OrderedLocusNames=At4g39210; ORFNames=T22F8.110;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11439129; DOI=10.1046/j.1365-313x.2001.2641043.x;
RA Rook F., Corke F., Card R., Munz G., Smith C., Bevan M.W.;
RT "Impaired sucrose-induction mutants reveal the modulation of sugar-induced
RT starch biosynthetic gene expression by abscisic acid signalling.";
RL Plant J. 26:421-433(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 296-479.
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).
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: Probably are expressed in roots, flowers and/or
CC seeds.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; Y18432; CAA77173.1; -; Genomic_DNA.
DR EMBL; AL050351; CAB43636.1; -; Genomic_DNA.
DR EMBL; AL161594; CAB80584.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87038.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66846.1; -; Genomic_DNA.
DR EMBL; AY059862; AAL24344.1; -; mRNA.
DR EMBL; BT010378; AAQ56821.1; -; mRNA.
DR EMBL; X73364; CAA51776.1; -; mRNA.
DR PIR; T08569; T08569.
DR RefSeq; NP_001328715.1; NM_001342527.1.
DR RefSeq; NP_195632.1; NM_120081.2.
DR AlphaFoldDB; P55231; -.
DR SMR; P55231; -.
DR STRING; 3702.AT4G39210.1; -.
DR iPTMnet; P55231; -.
DR PaxDb; P55231; -.
DR PRIDE; P55231; -.
DR ProteomicsDB; 220663; -.
DR EnsemblPlants; AT4G39210.1; AT4G39210.1; AT4G39210.
DR EnsemblPlants; AT4G39210.2; AT4G39210.2; AT4G39210.
DR GeneID; 830076; -.
DR Gramene; AT4G39210.1; AT4G39210.1; AT4G39210.
DR Gramene; AT4G39210.2; AT4G39210.2; AT4G39210.
DR KEGG; ath:AT4G39210; -.
DR Araport; AT4G39210; -.
DR TAIR; locus:2136358; AT4G39210.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_14_4_1; -.
DR InParanoid; P55231; -.
DR OMA; HEAKKSP; -.
DR OrthoDB; 806744at2759; -.
DR PhylomeDB; P55231; -.
DR BRENDA; 2.7.7.27; 399.
DR SABIO-RK; P55231; -.
DR UniPathway; UPA00152; -.
DR PRO; PR:P55231; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P55231; baseline and differential.
DR Genevisible; P55231; AT.
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; ISS:TAIR.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0019252; P:starch biosynthetic process; TAS:TAIR.
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 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..61
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 62..521
FT /note="Glucose-1-phosphate adenylyltransferase large
FT subunit 3, chloroplastic"
FT /id="PRO_0000011161"
FT CONFLICT 296
FT /note="S -> Y (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="S -> G (in Ref. 5; CAA51776)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="N -> S (in Ref. 5; CAA51776)"
FT /evidence="ECO:0000305"
FT CONFLICT 448..450
FT /note="IAS -> SR (in Ref. 5; CAA51776)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="K -> R (in Ref. 5; CAA51776)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 58029 MW; 2E6AAE91F9E6E367 CRC64;
MDSCCNFSLG TKTVLAKDSF KNVENKFLGE KIKGSVLKPF SSDLSSKKFR NRKLRPGVAY
AIATSKNAKE ALKNQPSMFE RRRADPKNVA AIILGGGDGA KLFPLTKRAA TPAVPVGGCY
RMIDIPMSNC INSCINKIFV LTQFNSASLN RHLARTYFGN GINFGDGFVE VLAATQTPGE
AGKKWFQGTA DAVRKFLWVF EDAKNRNIEN IIILSGDHLY RMNYMDFVQH HVDSKADITL
SCAPVDESRA SEYGLVNIDR SGRVVHFSEK PTGIDLKSMQ TDTTMHGLSH QEAAKSPYIA
SMGVYCFKTE ALLKLLTWRY PSSNDFGSEI IPAAIKDHNV QGYIYRDYWE DIGTIKSFYE
ANIALVEEHP KFEFYDQNTP FYTSPRFLPP TKTEKCRIVN SVISHGCFLG ECSIQRSIIG
ERSRLDYGVE LQDTLMLGAD SYQTESEIAS LLAEGNVPIG IGRDTKIRKC IIDKNAKIGK
NVVIMNKDDV KEADRPEEGF YIRSGITVVV EKATIKDGTV I
