GLGL2_ARATH
ID GLGL2_ARATH Reviewed; 518 AA.
AC P55230; Q9SFZ1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase large subunit 2, 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=APL2; OrderedLocusNames=At1g27680; ORFNames=T22C5.13;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 293-476.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
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; AC012375; AAF24945.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30862.1; -; Genomic_DNA.
DR EMBL; AY063927; AAL36283.1; -; mRNA.
DR EMBL; AY091251; AAM14190.1; -; mRNA.
DR EMBL; X73366; CAA51778.1; -; mRNA.
DR PIR; G86401; G86401.
DR RefSeq; NP_174089.1; NM_102533.5.
DR AlphaFoldDB; P55230; -.
DR SMR; P55230; -.
DR BioGRID; 24895; 1.
DR STRING; 3702.AT1G27680.1; -.
DR iPTMnet; P55230; -.
DR PaxDb; P55230; -.
DR PRIDE; P55230; -.
DR ProteomicsDB; 220662; -.
DR EnsemblPlants; AT1G27680.1; AT1G27680.1; AT1G27680.
DR GeneID; 839660; -.
DR Gramene; AT1G27680.1; AT1G27680.1; AT1G27680.
DR KEGG; ath:AT1G27680; -.
DR Araport; AT1G27680; -.
DR TAIR; locus:2199241; AT1G27680.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_14_4_1; -.
DR InParanoid; P55230; -.
DR OMA; RKWPLHT; -.
DR OrthoDB; 806744at2759; -.
DR PhylomeDB; P55230; -.
DR BRENDA; 2.7.7.27; 399.
DR SABIO-RK; P55230; -.
DR UniPathway; UPA00152; -.
DR PRO; PR:P55230; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P55230; baseline and differential.
DR Genevisible; P55230; 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; IDA: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 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..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..518
FT /note="Glucose-1-phosphate adenylyltransferase large
FT subunit 2, chloroplastic"
FT /id="PRO_0000011160"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55229"
FT CONFLICT 293
FT /note="S -> Y (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="S -> G (in Ref. 4; CAA51778)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="V -> G (in Ref. 4; CAA51778)"
FT /evidence="ECO:0000305"
FT CONFLICT 329..334
FT /note="PLAVGE -> RARRKL (in Ref. 4; CAA51778)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="K -> R (in Ref. 4; CAA51778)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="K -> I (in Ref. 4; CAA51778)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="K -> R (in Ref. 4; CAA51778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 57470 MW; BA781EC028D44EBC CRC64;
MESCFPAMKL NQCTFGLNNE IVSERVSAFW GTQVVKPNHL RTTKLRSAPQ KKIQTNLIRS
VLTPFVDQES HEPLLRTQNA DPKNVASIIL GGGAGTRLFP LTSKRAKPAV PIGGCYRLID
IPMSNCINSG IRKIFILTQF NSFSLNRHLS RTYNFGNGVN FGDGFVEVLA ATQTSGDAGK
KWFQGTADAV RQFIWVFEDA KTKNVEHVLI LSGDHLYRMD YMNFVQKHIE SNADITVSCL
PMDESRASDF GLLKIDQSGK IIQFSEKPKG DDLKAMQVDT SILGLPPKEA AESPYIASMG
VYVFRKEVLL KLLRSSYPTS NDFGSEIIPL AVGEHNVQAF LFNDYWEDIG TIGSFFDANL
ALTEQPPKFQ FYDQKTPFFT SPRFLPPTKV DKCRILDSIV SHGCFLRECS VQHSIVGIRS
RLESGVELQD TMMMGADFYQ TEAEIASLLA EGKVPVGVGQ NTKIKNCIID KNAKIGKNVV
IANADGVEEG DRPEEGFHIR SGITVVLKNA TIRDGLHI
