ID 6PGL3_ARATH Reviewed; 325 AA. AC Q84WW2; Q42135; Q8LD77; Q9FIN2; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 02-SEP-2026, entry version 135. DE RecName: Full=6-phosphogluconolactonase 3, chloroplastic {ECO:0000305}; DE Short=6PGL3 {ECO:0000305}; DE EC=3.1.1.31 {ECO:0000269|PubMed:19457984}; DE AltName: Full=Protein EMBRYO DEFECTIVE 2024 {ECO:0000303|PubMed:15266054}; DE Flags: Precursor; GN Name=PGL3 {ECO:0000303|PubMed:19457984}; GN Synonyms=EMB2024 {ECO:0000303|PubMed:15266054}; GN OrderedLocusNames=At5g24400 {ECO:0000312|Araport:AT5G24400}; GN ORFNames=K16H17.11 {ECO:0000312|EMBL:BAB11233.1}; 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=10048488; DOI=10.1093/dnares/5.6.379; RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence RT features of the regions of 1,081,958 bp covered by seventeen physically RT assigned P1 and TAC clones."; RL DNA Res. 5:379-391(1998). 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 GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RT "Community-consensus reference genome of Arabidopsis thaliana Col-0."; RL Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases. 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 [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 242-325. RC STRAIN=cv. Columbia; TISSUE=Seedling; RA Desprez T., Amselem J., Chiapello H., Caboche M., Hoefte H.; RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program."; RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases. RN [7] RP DISRUPTION PHENOTYPE. RX PubMed=15266054; DOI=10.1104/pp.104.045179; RA Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R., Hutchens S., RA Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.; RT "Identification of genes required for embryo development in Arabidopsis."; RL Plant Physiol. 135:1206-1220(2004). RN [8] RP SUBCELLULAR LOCATION. RX PubMed=17951448; DOI=10.1105/tpc.107.050989; RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E., RA Rasche N., Lueder F., Weckwerth W., Jahn O.; RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting RT peptides, metabolic pathways, and defense mechanisms."; RL Plant Cell 19:3170-3193(2007). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, GENE FAMILY, RP NOMENCLATURE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-150; ASP-231 AND RP HIS-233. RX PubMed=19457984; DOI=10.1093/pcp/pcp070; RA Xiong Y., DeFraia C., Williams D., Zhang X., Mou Z.; RT "Characterization of Arabidopsis 6-phosphogluconolactonase T-DNA insertion RT mutants reveals an essential role for the oxidative section of the RT plastidic pentose phosphate pathway in plant growth and development."; RL Plant Cell Physiol. 50:1277-1291(2009). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION RP PHENOTYPE. RX PubMed=23621281; DOI=10.1111/tpj.12222; RA Bussell J.D., Keech O., Fenske R., Smith S.M.; RT "Requirement for the plastidial oxidative pentose phosphate pathway for RT nitrate assimilation in Arabidopsis."; RL Plant J. 75:578-591(2013). RN [11] RP INTERACTION WITH TRXM2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-324. RX PubMed=24008768; DOI=10.1093/mp/sst126; RA Hoelscher C., Meyer T., von Schaewen A.; RT "Dual-targeting of Arabidopsis 6-phosphogluconolactonase 3 (PGL3) to RT chloroplasts and peroxisomes involves interaction with Trx m2 in the RT cytosol."; RL Mol. Plant 7:252-255(2014). CC -!- FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6- CC phosphogluconate (PubMed:19457984). Involved in the regulation of CC cellular redox state; enzymatic activity is required for this function CC (PubMed:19457984). Required for sugar-dependent expression of nitrate CC assimilation genes in the nucleus of root cells (PubMed:23621281). CC {ECO:0000269|PubMed:19457984, ECO:0000269|PubMed:23621281}. CC -!- CATALYTIC ACTIVITY: CC Reaction=6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate CC + H(+); Xref=Rhea:RHEA:12556, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57955, ChEBI:CHEBI:58759; EC=3.1.1.31; CC Evidence={ECO:0000269|PubMed:19457984}; CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step CC 2/3. {ECO:0000305}. CC -!- SUBUNIT: Interacts with TRXM2. {ECO:0000269|PubMed:24008768}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast CC {ECO:0000269|PubMed:19457984, ECO:0000269|PubMed:23621281, CC ECO:0000269|PubMed:24008768, ECO:0000305|PubMed:17951448}. Peroxisome CC {ECO:0000269|PubMed:17951448, ECO:0000269|PubMed:24008768}. CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and shoots. CC {ECO:0000269|PubMed:23621281}. CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous CC (PubMed:15266054, PubMed:19457984, PubMed:23621281). Embryo development CC arrest at cotyledon stage (PubMed:15266054). CC {ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:19457984, CC ECO:0000269|PubMed:23621281}. CC -!- MISCELLANEOUS: Plants silencing PGL3 exhibit reduced rosette size, CC constitutive expression of the pathogenesis-related genes PR1, PR2 and CC PR5, and enhanced resistance to Pseudomonas syringae pv. maculicola CC ES4326 and Hyaloperonospora arabidopsidis Noco2. CC {ECO:0000269|PubMed:19457984}. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. 6-phosphogluconolactonase subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB11233.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AB016884; BAB11233.1; ALT_INIT; Genomic_DNA. DR EMBL; CP002688; AED93307.1; -; Genomic_DNA. DR EMBL; OZ408687; CAO7053399.1; -; Genomic_DNA. DR EMBL; BT001923; AAN71922.1; -; mRNA. DR EMBL; AY086161; AAM63366.1; -; mRNA. DR EMBL; Z26557; CAA81328.1; -; mRNA. DR RefSeq; NP_568445.1; NM_122348.3. DR AlphaFoldDB; Q84WW2; -. DR SMR; Q84WW2; -. DR BioGRID; 17786; 1. DR FunCoup; Q84WW2; 4050. DR STRING; 3702.Q84WW2; -. DR iPTMnet; Q84WW2; -. DR PaxDb; 3702-Q84WW2; -. DR ProteomicsDB; 245161; -. DR GeneID; 832511; -. DR KEGG; ath:AT5G24400; -. DR Araport; AT5G24400; -. DR TAIR; AT5G24400; EMB2024. DR eggNOG; KOG3147; Eukaryota. DR HOGENOM; CLU_053947_0_0_1; -. DR InParanoid; Q84WW2; -. DR OMA; IAMSQST; -. DR PhylomeDB; Q84WW2; -. DR BioCyc; ARA:AT5G24400-MONOMER; -. DR BRENDA; 3.1.1.31; 399. DR UniPathway; UPA00115; UER00409. DR PRO; PR:Q84WW2; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q84WW2; baseline and differential. DR GO; GO:0009507; C:chloroplast; IDA:TAIR. DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR. DR GO; GO:0005777; C:peroxisome; IDA:TAIR. DR GO; GO:0009536; C:plastid; IDA:TAIR. DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IDA:TAIR. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0071461; P:cellular response to redox state; IMP:TAIR. DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR. DR GO; GO:0002229; P:defense response to oomycetes; IMP:TAIR. DR GO; GO:0042128; P:nitrate assimilation; IMP:TAIR. DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central. DR CDD; cd01400; 6PGL; 1. DR FunFam; 3.40.50.1360:FF:000009; Probable 6-phosphogluconolactonase; 1. DR Gene3D; 3.40.50.1360; -; 1. DR InterPro; IPR005900; 6-phosphogluconolactonase_DevB. DR InterPro; IPR039104; 6PGL. DR InterPro; IPR006148; Glc/Gal-6P_isomerase. DR InterPro; IPR037171; NagB/RpiA_transferase-like. DR NCBIfam; TIGR01198; pgl; 1. DR PANTHER; PTHR11054; 6-PHOSPHOGLUCONOLACTONASE; 1. DR PANTHER; PTHR11054:SF22; 6-PHOSPHOGLUCONOLACTONASE 3, CHLOROPLASTIC; 1. DR Pfam; PF01182; Glucosamine_iso; 1. DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1. PE 1: Evidence at protein level; KW Chloroplast; Hydrolase; Peroxisome; Plastid; Reference proteome; KW Transit peptide. FT TRANSIT 1..68 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 69..325 FT /note="6-phosphogluconolactonase 3, chloroplastic" FT /id="PRO_0000288672" FT REGION 51..73 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 323..325 FT /note="Microbody targeting signal" FT /evidence="ECO:0000269|PubMed:24008768" FT MUTAGEN 150 FT /note="D->A: Abolishes enzymatic activity." FT /evidence="ECO:0000269|PubMed:19457984" FT MUTAGEN 231 FT /note="D->A: Abolishes enzymatic activity; when associated FT with A-233." FT /evidence="ECO:0000269|PubMed:19457984" FT MUTAGEN 233 FT /note="H->A: Abolishes enzymatic activity; when associated FT with A-231." FT /evidence="ECO:0000269|PubMed:19457984" FT MUTAGEN 324 FT /note="K->L: Abolishes targeting to peroxisome." FT /evidence="ECO:0000269|PubMed:24008768" FT CONFLICT 30 FT /note="P -> L (in Ref. 5; AAM63366)" FT /evidence="ECO:0000305" FT CONFLICT 33 FT /note="Y -> H (in Ref. 5; AAM63366)" FT /evidence="ECO:0000305" FT CONFLICT 93..94 FT /note="VI -> AV (in Ref. 5; AAM63366)" FT /evidence="ECO:0000305" SQ SEQUENCE 325 AA; 35645 MW; 0FBC6E95F9C073DC CRC64; MASSSCFLRS ILFSSPTNLR SNHHLPTFFP KNYLICSHST SSRFESLSVS SIGTGSTKKS SDTRRKVKSM ATTNIGKEEK KRVEIYDLEE NLVIDLAKFT ADLSDKFCKE RGAFTVVVSG GSLIKSLRKL VESPYVDSID WARWHFFWVD ERVVPKNHDD SNYKLAYDSF LSKVPIPPGN VYAINEALSA EAAADDYETC LKHLVNTNIL RVSESTGFPK FDLMLLGMGP DGHVASLFPG HGLCNESKKW VVSISDSPKP PSERITFTFP VINSSAHVAL VVCGSGKAEA VEAALKKTGN VPPAGSVSAE DELVWFLDKP ASSKL //