G6PIP_ARATH
ID G6PIP_ARATH Reviewed; 613 AA.
AC Q8H103; A8MR16; Q9SB57; Q9SEJ5;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Glucose-6-phosphate isomerase 1, chloroplastic;
DE Short=GPI 1;
DE EC=5.3.1.9;
DE AltName: Full=Phosphoglucose isomerase 1;
DE Short=PGI 1;
DE AltName: Full=Phosphohexose isomerase;
DE Short=PHI;
DE Flags: Precursor;
GN Name=PGI1; Synonyms=pgi2, pgi3; OrderedLocusNames=At4g24620;
GN ORFNames=F22K18.180;
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], FUNCTION, AND MUTAGENESIS OF SER-166.
RX PubMed=10806248; DOI=10.1104/pp.123.1.319;
RA Yu T.-S., Lue W.-L., Wang S.-M., Chen J.;
RT "Mutation of Arabidopsis plastid phosphoglucose isomerase affects leaf
RT starch synthesis and floral initiation.";
RL Plant Physiol. 123:319-326(2000).
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] (ISOFORM 1).
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS], PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-595, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=18599644; DOI=10.1104/pp.108.123703;
RA Quettier A.-L., Shaw E., Eastmond P.J.;
RT "SUGAR-DEPENDENT6 encodes a mitochondrial flavin adenine dinucleotide-
RT dependent glycerol-3-p dehydrogenase, which is required for glycerol
RT catabolism and post germinative seedling growth in Arabidopsis.";
RL Plant Physiol. 148:519-528(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-595, 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: Promotes the synthesis of starch in leaves.
CC {ECO:0000269|PubMed:10806248}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC EC=5.3.1.9;
CC -!- ACTIVITY REGULATION: Inhibited by glycerol-3-P (G3P).
CC {ECO:0000269|PubMed:18599644}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18431481}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8H103-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H103-2; Sequence=VSP_044431, VSP_044432;
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA23001.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79372.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF120494; AAF24124.1; -; Genomic_DNA.
DR EMBL; AL035356; CAA23001.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161561; CAB79372.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84933.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84934.1; -; Genomic_DNA.
DR EMBL; BT000953; AAN41353.1; -; mRNA.
DR EMBL; AK227111; BAE99162.1; -; mRNA.
DR PIR; T05572; T05572.
DR RefSeq; NP_001078444.1; NM_001084975.1. [Q8H103-2]
DR RefSeq; NP_194193.2; NM_118595.5. [Q8H103-1]
DR AlphaFoldDB; Q8H103; -.
DR SMR; Q8H103; -.
DR BioGRID; 13853; 13.
DR STRING; 3702.AT4G24620.1; -.
DR iPTMnet; Q8H103; -.
DR MetOSite; Q8H103; -.
DR PaxDb; Q8H103; -.
DR PRIDE; Q8H103; -.
DR ProteomicsDB; 230022; -. [Q8H103-1]
DR EnsemblPlants; AT4G24620.1; AT4G24620.1; AT4G24620. [Q8H103-1]
DR EnsemblPlants; AT4G24620.2; AT4G24620.2; AT4G24620. [Q8H103-2]
DR GeneID; 828564; -.
DR Gramene; AT4G24620.1; AT4G24620.1; AT4G24620. [Q8H103-1]
DR Gramene; AT4G24620.2; AT4G24620.2; AT4G24620. [Q8H103-2]
DR KEGG; ath:AT4G24620; -.
DR Araport; AT4G24620; -.
DR TAIR; locus:2121929; AT4G24620.
DR eggNOG; KOG2446; Eukaryota.
DR HOGENOM; CLU_033288_0_0_1; -.
DR InParanoid; Q8H103; -.
DR OMA; WHRYVEW; -.
DR PhylomeDB; Q8H103; -.
DR BioCyc; ARA:AT4G24620-MON; -.
DR BioCyc; MetaCyc:AT4G24620-MON; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00138; -.
DR PRO; PR:Q8H103; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8H103; baseline and differential.
DR Genevisible; Q8H103; 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:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; ISS:TAIR.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; ISS:TAIR.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0009911; P:positive regulation of flower development; IMP:TAIR.
DR GO; GO:0005982; P:starch metabolic process; IMP:TAIR.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 1.
DR HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035476; SIS_PGI_1.
DR InterPro; IPR035482; SIS_PGI_2.
DR PANTHER; PTHR11469; PTHR11469; 1.
DR Pfam; PF00342; PGI; 2.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 1.
DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Gluconeogenesis; Glycolysis; Isomerase;
KW Phosphoprotein; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..613
FT /note="Glucose-6-phosphate isomerase 1, chloroplastic"
FT /id="PRO_0000420249"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 392
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 421
FT /evidence="ECO:0000250"
FT ACT_SITE 526
FT /evidence="ECO:0000250"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT VAR_SEQ 570
FT /note="I -> K (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044431"
FT VAR_SEQ 571..613
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044432"
FT MUTAGEN 166
FT /note="S->F: In pgi1-1; decreased plastid phospho-glucose
FT (Glc) isomerase activity leading to a deficiency in leaf
FT starch synthesis, but an accumulation of starch in root cap
FT cells. Delayed flowering time under short-day conditions."
FT /evidence="ECO:0000269|PubMed:10806248"
FT CONFLICT 24..45
FT /note="ALPAQSRDSFSFPHTSKPTNLP -> GIAGAISRFLLFPTYLQTHQST (in
FT Ref. 1; AAF24124)"
FT /evidence="ECO:0000305"
FT CONFLICT 201..207
FT /note="FVAEALA -> LSLRLG (in Ref. 1; AAF24124)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="A -> H (in Ref. 1; AAF24124)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="A -> P (in Ref. 1; AAF24124)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="D -> Y (in Ref. 1; AAF24124)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 67048 MW; 95792BA6A173991B CRC64;
MASLSGLYSS SPSLKPAKNH SFKALPAQSR DSFSFPHTSK PTNLPLTLSS ARSVARDISH
ADSKKELLKD PDALWKRYLD WFYQQKELGL YLDISRVGFT DEFVAEMEPR FQAAFKAMED
LEKGSIANPD EGRMVGHYWL RNSKLAPKPT LKTLIENTLD SICAFSDDII SGKIKPPSSP
EGRFTQILSV GIGGSALGPQ FVAEALAPDN PPLKIRFIDN TDPAGIDHQI AQLGPELAST
LVVVISKSGG TPETRNGLLE VQKAFREAGL NFAKQGVAIT QENSLLDNTA RIEGWLARFP
MYDWVGGRTS IMSAVGLLPA ALQGINVREM LTGAALMDEA TRTTSIKNNP AALLAMCWYW
ASNGVGSKDM VVLPYKDSLL LFSRYLQQLV MESLGKEFDL DGNTVNQGLT VYGNKGSTDQ
HAYIQQLRDG VHNFFATFIE VLRDRPPGHD WELEPGVTCG DYLFGMLQGT RSALYANGRE
SISVTIQEVT PTSVGAIIAL YERAVGLYAS IVNINAYHQP GVEAGKKAAA EVLALQKRVL
SVLNEATCKD PVEPLTLEEI ADRCHAPEEI EMIYKIIAHM SANDRVLIAE GNCGSPRSIK
VYLGECNVDD LYA
