GLGS_ARATH
ID GLGS_ARATH Reviewed; 520 AA.
AC P55228; O64400; Q96534;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic;
DE EC=2.7.7.27;
DE AltName: Full=ADP-glucose pyrophosphorylase;
DE AltName: Full=ADP-glucose synthase;
DE AltName: Full=AGPase B;
DE AltName: Full=Alpha-D-glucose-1-phosphate adenyl transferase;
DE Flags: Precursor;
GN Name=APS1; Synonyms=ADG1, APS; OrderedLocusNames=At5g48300;
GN ORFNames=K23F3.2;
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=9680965; DOI=10.1046/j.1365-313x.1998.00009.x;
RA Wang S.-M., Lue W.-L., Yu T.-S., Long J.-H., Wang C.-N., Eimert K.,
RA Chen J.;
RT "Characterization of ADG1, an Arabidopsis locus encoding for ADPG
RT pyrophosphorylase small subunit, demonstrates that the presence of the
RT small subunit is required for large subunit stability.";
RL Plant J. 13:63-70(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Choi S.B., Okita T.W.;
RT "cDNA cloning of ADP glucose pyrophosphorylase small subunit in Arabidopsis
RT thaliana.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Ito H., Kato C., Matsui H., Okita T.W.;
RT "Isolation of ADPglucose pyrophosphorylase small subunit gene from
RT Arabidopsis thaliana.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [MRNA] OF 293-478.
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 {ECO:0000250}.
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; U72351; AAC39441.1; -; mRNA.
DR EMBL; U70616; AAB09585.1; -; mRNA.
DR EMBL; AB039889; BAA92523.1; -; Genomic_DNA.
DR EMBL; AP000372; BAA98187.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95648.1; -; Genomic_DNA.
DR EMBL; AY049265; AAK83607.1; -; mRNA.
DR EMBL; AY065428; AAL38869.1; -; mRNA.
DR EMBL; AY090283; AAL90944.1; -; mRNA.
DR EMBL; AY096379; AAM20020.1; -; mRNA.
DR EMBL; X73365; CAA51777.1; -; mRNA.
DR RefSeq; NP_199641.1; NM_124205.4.
DR AlphaFoldDB; P55228; -.
DR SMR; P55228; -.
DR BioGRID; 20129; 9.
DR IntAct; P55228; 2.
DR STRING; 3702.AT5G48300.1; -.
DR iPTMnet; P55228; -.
DR PaxDb; P55228; -.
DR PRIDE; P55228; -.
DR ProteomicsDB; 220773; -.
DR EnsemblPlants; AT5G48300.1; AT5G48300.1; AT5G48300.
DR GeneID; 834883; -.
DR Gramene; AT5G48300.1; AT5G48300.1; AT5G48300.
DR KEGG; ath:AT5G48300; -.
DR Araport; AT5G48300; -.
DR TAIR; locus:2156263; AT5G48300.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_14_4_1; -.
DR InParanoid; P55228; -.
DR OMA; ISKDAMM; -.
DR OrthoDB; 806744at2759; -.
DR PhylomeDB; P55228; -.
DR BioCyc; ARA:AT5G48300-MON; -.
DR BioCyc; MetaCyc:MON-1822; -.
DR BRENDA; 2.7.7.27; 399.
DR SABIO-RK; P55228; -.
DR UniPathway; UPA00152; -.
DR PRO; PR:P55228; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P55228; baseline and differential.
DR Genevisible; P55228; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0030931; C:heterotetrameric ADPG pyrophosphorylase complex; IMP:TAIR.
DR GO; GO:0009536; C:plastid; 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:0048573; P:photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0019252; P:starch biosynthetic process; IMP: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..71
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 72..520
FT /note="Glucose-1-phosphate adenylyltransferase small
FT subunit, chloroplastic"
FT /id="PRO_0000011149"
FT CONFLICT 194..195
FT /note="RQ -> TD (in Ref. 2; AAB09585)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="A -> S (in Ref. 2; AAB09585)"
FT /evidence="ECO:0000305"
FT CONFLICT 293..298
FT /note="MPFIAS -> YPYIAG (in Ref. 7; CAA51777)"
FT /evidence="ECO:0000305"
FT CONFLICT 332..333
FT /note="TS -> PF (in Ref. 7; CAA51777)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="S -> A (in Ref. 2; AAB09585)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="K -> I (in Ref. 7; CAA51777)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="A -> S (in Ref. 2; AAB09585)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 56651 MW; 49E8F3141A3C5C0F CRC64;
MASVSAIGVL KVPPASTSNS TGKATEAVPT RTLSFSSSVT SSDDKISLKS TVSRLCKSVV
RRNPIIVSPK AVSDSQNSQT CLDPDASSSV LGIILGGGAG TRLYPLTKKR AKPAVPLGAN
YRLIDIPVSN CLNSNISKIY VLTQFNSASL NRHLSRAYAS NMGGYKNEGF VEVLAAQQSP
ENPNWFQGTA DAVRQYLWLF EEHNVLEYLI LAGDHLYRMD YEKFIQAHRE TDADITVAAL
PMDEQRATAF GLMKIDEEGR IIEFAEKPKG EHLKAMKVDT TILGLDDQRA KEMPFIASMG
IYVVSRDVML DLLRNQFPGA NDFGSEVIPG ATSLGLRVQA YLYDGYWEDI GTIEAFYNAN
LGITKKPVPD FSFYDRSAPI YTQPRYLPPS KMLDADVTDS VIGEGCVIKN CKIHHSVVGL
RSCISEGAII EDSLLMGADY YETATEKSLL SAKGSVPIGI GKNSHIKRAI IDKNARIGDN
VKIINSDNVQ EAARETDGYF IKSGIVTVIK DALIPTGTVI
