PGP1A_ARATH
ID PGP1A_ARATH Reviewed; 362 AA.
AC P0DKC3; F4K4H2; Q8GY27; Q8L3U4; Q9LHT3;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Phosphoglycolate phosphatase 1A, chloroplastic;
DE EC=3.1.3.18;
DE Flags: Precursor;
GN Name=PGLP1A; OrderedLocusNames=At5g36700; ORFNames=F24C7;
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;
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 (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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] (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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-362 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-260, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17478634; DOI=10.1104/pp.107.099192;
RA Schwarte S., Bauwe H.;
RT "Identification of the photorespiratory 2-phosphoglycolate phosphatase,
RT PGLP1, in Arabidopsis.";
RL Plant Physiol. 144:1580-1586(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, 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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-55, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER MET-54, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Photorespiratory enzyme that dephosphorylates the 2-
CC phosphoglycolate produced by the RuBisCO oxygenation reaction.
CC {ECO:0000269|PubMed:17478634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phosphoglycolate + H2O = glycolate + phosphate;
CC Xref=Rhea:RHEA:14369, ChEBI:CHEBI:15377, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58033; EC=3.1.3.18;
CC Evidence={ECO:0000269|PubMed:17478634};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0DKC3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0DKC3-2; Sequence=VSP_046408, VSP_046409;
CC -!- DISRUPTION PHENOTYPE: Chlorotic primary leaves soon after germination
CC and plants not viable when grown under ambient air, but normal growth
CC under CO(2)-enriched air. {ECO:0000269|PubMed:17478634}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97552.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC42546.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP002029; BAA97552.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94099.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94100.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94101.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94102.1; -; Genomic_DNA.
DR EMBL; AY094446; AAM19818.1; -; mRNA.
DR EMBL; AY122899; AAM67432.1; -; mRNA.
DR EMBL; AK117908; BAC42546.1; ALT_INIT; mRNA.
DR RefSeq; NP_001119316.1; NM_001125844.1. [P0DKC3-1]
DR RefSeq; NP_001119317.1; NM_001125845.1. [P0DKC3-2]
DR RefSeq; NP_001119318.1; NM_001125846.2. [P0DKC3-1]
DR RefSeq; NP_001190427.1; NM_001203498.2. [P0DKC3-1]
DR RefSeq; NP_001190428.1; NM_001203499.1. [P0DKC3-1]
DR RefSeq; NP_198485.2; NM_123027.4. [P0DKC3-1]
DR RefSeq; NP_198495.1; NM_123037.5. [P0DKC3-1]
DR AlphaFoldDB; P0DKC3; -.
DR SMR; P0DKC3; -.
DR BioGRID; 18897; 1.
DR STRING; 3702.AT5G36700.1; -.
DR iPTMnet; P0DKC3; -.
DR MetOSite; P0DKC3; -.
DR PaxDb; P0DKC3; -.
DR PRIDE; P0DKC3; -.
DR ProMEX; P0DKC3; -.
DR DNASU; 833635; -.
DR EnsemblPlants; AT5G36700.1; AT5G36700.1; AT5G36700. [P0DKC3-1]
DR EnsemblPlants; AT5G36700.2; AT5G36700.2; AT5G36700. [P0DKC3-1]
DR EnsemblPlants; AT5G36700.3; AT5G36700.3; AT5G36700. [P0DKC3-2]
DR EnsemblPlants; AT5G36700.4; AT5G36700.4; AT5G36700. [P0DKC3-1]
DR EnsemblPlants; AT5G36790.1; AT5G36790.1; AT5G36790. [P0DKC3-1]
DR EnsemblPlants; AT5G36790.2; AT5G36790.2; AT5G36790. [P0DKC3-1]
DR EnsemblPlants; AT5G36790.3; AT5G36790.3; AT5G36790. [P0DKC3-1]
DR GeneID; 833635; -.
DR GeneID; 833646; -.
DR Gramene; AT5G36700.1; AT5G36700.1; AT5G36700. [P0DKC3-1]
DR Gramene; AT5G36700.2; AT5G36700.2; AT5G36700. [P0DKC3-1]
DR Gramene; AT5G36700.3; AT5G36700.3; AT5G36700. [P0DKC3-2]
DR Gramene; AT5G36700.4; AT5G36700.4; AT5G36700. [P0DKC3-1]
DR Gramene; AT5G36790.1; AT5G36790.1; AT5G36790. [P0DKC3-1]
DR Gramene; AT5G36790.2; AT5G36790.2; AT5G36790. [P0DKC3-1]
DR Gramene; AT5G36790.3; AT5G36790.3; AT5G36790. [P0DKC3-1]
DR KEGG; ath:AT5G36700; -.
DR KEGG; ath:AT5G36790; -.
DR Araport; AT5G36700; -.
DR eggNOG; KOG2882; Eukaryota.
DR HOGENOM; CLU_043473_0_0_1; -.
DR InParanoid; P0DKC3; -.
DR OMA; PPMHRET; -.
DR PhylomeDB; P0DKC3; -.
DR BioCyc; MetaCyc:AT5G36700-MON; -.
DR PRO; PR:P0DKC3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P0DKC3; baseline and differential.
DR Genevisible; P0DKC3; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006349; PGP_euk.
DR Pfam; PF13344; Hydrolase_6; 1.
DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR TIGRFAMs; TIGR01452; PGP_euk; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chloroplast; Hydrolase; Phosphoprotein;
KW Photorespiration; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 55..362
FT /note="Phosphoglycolate phosphatase 1A, chloroplastic"
FT /id="PRO_0000422097"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 329..332
FT /note="VTSI -> ITNL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046408"
FT VAR_SEQ 333..362
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046409"
FT MUTAGEN 260
FT /note="G->S: 60% decreased catalytic activity."
FT /evidence="ECO:0000269|PubMed:17478634"
FT CONFLICT 84
FT /note="F -> L (in Ref. 4; BAC42546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 39762 MW; E95B32C0D232DC29 CRC64;
MLSRSVASAV TPVSSSSLLP NSKPIFCLKT LSGYRSSSFC GGCIRKINHK PLRMTSSNIT
PRAMATQQLE NADQLIDSVE TFIFDCDGVI WKGDKLIEGV PETLDMLRAK GKRLVFVTNN
STKSRKQYGK KFETLGLNVN EEEIFASSFA AAAYLQSINF PKDKKVYVIG EEGILKELEL
AGFQYLGGPD DGKRQIELKP GFLMEHDHDV GAVVVGFDRY FNYYKIQYGT LCIRENPGCL
FIATNRDAVT HLTDAQEWAG GGSMVGALVG STQREPLVVG KPSTFMMDYL ADKFGIQKSQ
ICMVGDRLDT DILFGQNGGC KTLLVLSGVT SISMLESPEN KIQPDFYTSK ISDFLSPKAA
TV
