6PGL3_ARATH
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 03-AUG-2022, entry version 120.
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 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 [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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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};
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DR EMBL; AB016884; BAB11233.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED93307.1; -; 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 STRING; 3702.AT5G24400.1; -.
DR iPTMnet; Q84WW2; -.
DR PaxDb; Q84WW2; -.
DR PRIDE; Q84WW2; -.
DR ProteomicsDB; 245161; -.
DR EnsemblPlants; AT5G24400.1; AT5G24400.1; AT5G24400.
DR GeneID; 832511; -.
DR Gramene; AT5G24400.1; AT5G24400.1; AT5G24400.
DR KEGG; ath:AT5G24400; -.
DR Araport; AT5G24400; -.
DR TAIR; locus:2152906; AT5G24400.
DR eggNOG; KOG3147; Eukaryota.
DR HOGENOM; CLU_053947_0_0_1; -.
DR InParanoid; Q84WW2; -.
DR OMA; IAMSQST; -.
DR OrthoDB; 1420529at2759; -.
DR PhylomeDB; Q84WW2; -.
DR BioCyc; ARA:AT5G24400-MON; -.
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 Genevisible; Q84WW2; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 InterPro; IPR005900; 6-phosphogluconolactonase_DevB.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR039104; PGLS.
DR PANTHER; PTHR11054; PTHR11054; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR01198; pgl; 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 COMPBIAS 59..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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. 4; AAM63366)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="Y -> H (in Ref. 4; AAM63366)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..94
FT /note="VI -> AV (in Ref. 4; 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
