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 27-MAR-2024, entry version 147. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q8H103; -. DR iPTMnet; Q8H103; -. DR MetOSite; Q8H103; -. DR PaxDb; 3702-AT4G24620-1; -. 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; AT4G24620; PGI1. DR eggNOG; KOG2446; Eukaryota. DR HOGENOM; CLU_033288_0_0_1; -. DR InParanoid; Q8H103; -. DR OMA; WHRYVEW; -. DR OrthoDB; 370692at2759; -. DR PhylomeDB; Q8H103; -. DR BioCyc; ARA:AT4G24620-MONOMER; -. DR BioCyc; MetaCyc:AT4G24620-MONOMER; -. DR UniPathway; UPA00109; UER00181. DR UniPathway; UPA00138; -. DR PRO; PR:Q8H103; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q8H103; baseline and differential. 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:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. 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; GLUCOSE-6-PHOSPHATE ISOMERASE; 1. DR PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1. DR Pfam; PF00342; PGI; 2. DR PRINTS; PR00662; G6PISOMERASE. DR SUPFAM; SSF53697; SIS domain; 1. DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1. DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1. DR Genevisible; Q8H103; AT. 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 //