ID   PGP2_ARATH              Reviewed;         301 AA.
AC   Q8GWU0; Q8LAU0; Q9FIK4;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Phosphoglycolate phosphatase 2;
DE            EC=3.1.3.18;
GN   Name=PGLP2; OrderedLocusNames=At5g47760; ORFNames=MCA23.8;
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=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   [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   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION 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).
CC   -!- FUNCTION: Dephosphorylates 2-phosphoglycolate, but does not contribute
CC       to photorespiratory metabolism. {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   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {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=BAB11323.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB016886; BAB11323.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED95569.1; -; Genomic_DNA.
DR   EMBL; AK118640; BAC43237.1; -; mRNA.
DR   EMBL; BT005294; AAO63358.1; -; mRNA.
DR   EMBL; AY087611; AAM65152.1; -; mRNA.
DR   RefSeq; NP_199587.1; NM_124150.5.
DR   AlphaFoldDB; Q8GWU0; -.
DR   SMR; Q8GWU0; -.
DR   BioGRID; 20075; 1.
DR   STRING; 3702.AT5G47760.1; -.
DR   PaxDb; Q8GWU0; -.
DR   PRIDE; Q8GWU0; -.
DR   ProteomicsDB; 236345; -.
DR   EnsemblPlants; AT5G47760.1; AT5G47760.1; AT5G47760.
DR   GeneID; 834827; -.
DR   Gramene; AT5G47760.1; AT5G47760.1; AT5G47760.
DR   KEGG; ath:AT5G47760; -.
DR   Araport; AT5G47760; -.
DR   TAIR; locus:2160937; AT5G47760.
DR   eggNOG; KOG2882; Eukaryota.
DR   HOGENOM; CLU_043473_0_0_1; -.
DR   InParanoid; Q8GWU0; -.
DR   OMA; MDGVLIH; -.
DR   OrthoDB; 982374at2759; -.
DR   BioCyc; MetaCyc:AT5G47760-MON; -.
DR   PRO; PR:Q8GWU0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8GWU0; baseline and differential.
DR   Genevisible; Q8GWU0; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:TAIR.
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   Hydrolase; Reference proteome.
FT   CHAIN           1..301
FT                   /note="Phosphoglycolate phosphatase 2"
FT                   /id="PRO_0000422099"
FT   ACT_SITE        19
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        79
FT                   /note="I -> V (in Ref. 5; AAM65152)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="V -> I (in Ref. 5; AAM65152)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   301 AA;  33012 MW;  08AF5EE746B14E56 CRC64;
     MAPQLLSSSN FKSLFDSVDT FLFDCDGVIW KGETLIDGVS QTLDLIRSKG KNVVFVTNNS
     VKSRRQYAEK FRSLGVTSIT QDEIFSSSFA AAMYLKVNNF PKDKKVYVIG GEGVLEELQI
     AGFTGLGGPE DGEKKAQWKS NSLFEHDKSV GAVVVGLDPN INYYKLQYGT LCVRENPGCL
     FIATNRDAVG HMTDLQEWPG AGCMVAAMCG STEREPIVVG KPSTFMMDFL LQKFGTETSR
     MCMVGDRLDT DILFGQNAGC KTLLVLTGVT SESNLLDKGN KIEPDYYTST VSDIIKLMES
     P