ID SERC_ARATH Reviewed; 295 AA. AC O82796; Q9FZ85; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 2. DT 16-JAN-2019, entry version 132. DE RecName: Full=Phosphoserine phosphatase, chloroplastic; DE Short=PSP; DE Short=PSPase; DE EC=3.1.3.3; DE AltName: Full=O-phosphoserine phosphohydrolase; DE Flags: Precursor; GN Name=PSP; Synonyms=PSP1; OrderedLocusNames=At1g18640; GN ORFNames=F26I16.2; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, BIOPHYSICOCHEMICAL RP PROPERTIES, AND SUBCELLULAR LOCATION. RX PubMed=10196182; DOI=10.1074/jbc.274.16.11007; RA Ho C.-L., Noji M., Saito K.; RT "Plastidic pathway of serine biosynthesis. Molecular cloning and RT expression of 3-phosphoserine phosphatase from Arabidopsis thaliana."; RL J. Biol. Chem. 274:11007-11012(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). 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 RT reference genome."; RL Plant J. 89:789-804(2017). 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., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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, TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION, AND RP DISRUPTION PHENOTYPE. RC STRAIN=cv. Columbia; RX PubMed=23771893; DOI=10.1105/tpc.113.112359; RA Cascales-Minana B., Munoz-Bertomeu J., Flores-Tornero M., Anoman A.D., RA Pertusa J., Alaiz M., Osorio S., Fernie A.R., Segura J., Ros R.; RT "The phosphorylated pathway of serine biosynthesis is essential both RT for male gametophyte and embryo development and for root growth in RT Arabidopsis."; RL Plant Cell 25:2084-2101(2013). RN [7] RP DISRUPTION PHENOTYPE. RC STRAIN=cv. Columbia; RX PubMed=24368794; DOI=10.1105/tpc.113.118992; RA Benstein R.M., Ludewig K., Wulfert S., Wittek S., Gigolashvili T., RA Frerigmann H., Gierth M., Fluegge U.I., Krueger S.; RT "Arabidopsis phosphoglycerate dehydrogenase1 of the phosphoserine RT pathway is essential for development and required for ammonium RT assimilation and tryptophan biosynthesis."; RL Plant Cell 25:5011-5029(2013). CC -!- FUNCTION: Catalyzes the last step in the plastidial phosphorylated CC pathway of serine biosynthesis (PPSB). The reaction mechanism CC proceeds via the formation of a phosphoryl-enzyme intermediates. CC Required for embryo, pollen and root development. May be required CC preferentially for serine biosynthesis in non-photosynthetic CC tissues. {ECO:0000269|PubMed:10196182, CC ECO:0000269|PubMed:23771893}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-serine = L-serine + phosphate; CC Xref=Rhea:RHEA:21208, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=3.1.3.3; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-D-serine = D-serine + phosphate; CC Xref=Rhea:RHEA:24873, ChEBI:CHEBI:15377, ChEBI:CHEBI:35247, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58680; EC=3.1.3.3; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.5 mM for 3-phosphoserine (at 30 degrees Celsius and pH 7.5) CC {ECO:0000269|PubMed:10196182}; CC Note=Approximately 60% inhibition of PSP activity by 10 mM CC serine was observed.; CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine CC from 3-phospho-D-glycerate: step 3/3. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast CC {ECO:0000269|PubMed:10196182, ECO:0000269|PubMed:23771893}. CC -!- TISSUE SPECIFICITY: Ubiquitous. Mainly expressed in shoot and root CC meristems, vasculature, pollen, anthers, carpels and seeds. CC {ECO:0000269|PubMed:23771893}. CC -!- INDUCTION: Up-regulated in aerial parts by 8 hours exposure to CC darkness, whereas longer exposure down-regulate expression in both CC roots and aerial parts. {ECO:0000269|PubMed:23771893}. CC -!- DISRUPTION PHENOTYPE: Embryo lethal when homozygous. CC {ECO:0000269|PubMed:23771893, ECO:0000269|PubMed:24368794}. CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB CC family. {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; AB018408; BAA33806.1; -; mRNA. DR EMBL; AB018409; BAA33807.1; -; Genomic_DNA. DR EMBL; AC026238; AAF98410.1; -; Genomic_DNA. DR EMBL; CP002684; AEE29738.1; -; Genomic_DNA. DR EMBL; AY065351; AAL38792.1; -; mRNA. DR EMBL; AY096687; AAM20321.1; -; mRNA. DR EMBL; AY087385; AAM64935.1; -; mRNA. DR PIR; B86320; B86320. DR PIR; T51362; T51362. DR RefSeq; NP_973858.1; NM_202129.3. DR UniGene; At.356; -. DR UniGene; At.41785; -. DR ProteinModelPortal; O82796; -. DR SMR; O82796; -. DR BioGrid; 23684; 1. DR IntAct; O82796; 1. DR STRING; 3702.AT1G18640.2; -. DR PaxDb; O82796; -. DR PRIDE; O82796; -. DR EnsemblPlants; AT1G18640.2; AT1G18640.2; AT1G18640. DR GeneID; 838445; -. DR Gramene; AT1G18640.2; AT1G18640.2; AT1G18640. DR KEGG; ath:AT1G18640; -. DR Araport; AT1G18640; -. DR TAIR; locus:2027433; AT1G18640. DR eggNOG; KOG1615; Eukaryota. DR eggNOG; COG0560; LUCA. DR HOGENOM; HOG000231116; -. DR InParanoid; O82796; -. DR KO; K01079; -. DR OMA; NGSYAGF; -. DR OrthoDB; 1009123at2759; -. DR PhylomeDB; O82796; -. DR BioCyc; ARA:AT1G18640-MONOMER; -. DR BioCyc; MetaCyc:AT1G18640-MONOMER; -. DR BRENDA; 3.1.3.3; 399. DR Reactome; R-ATH-977347; Serine biosynthesis. DR UniPathway; UPA00135; UER00198. DR PRO; PR:O82796; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; O82796; baseline and differential. DR Genevisible; O82796; AT. DR GO; GO:0009507; C:chloroplast; IDA:TAIR. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central. DR GO; GO:0004647; F:phosphoserine phosphatase activity; IDA:TAIR. DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central. DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR. DR GO; GO:0006564; P:L-serine biosynthetic process; IBA:GO_Central. DR GO; GO:0006563; P:L-serine metabolic process; ISS:UniProtKB. DR GO; GO:0009555; P:pollen development; IMP:TAIR. DR GO; GO:0048364; P:root development; IMP:TAIR. DR Gene3D; 1.10.150.210; -; 1. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR023190; Pser_Pase_dom_2. DR SUPFAM; SSF56784; SSF56784; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Chloroplast; Complete proteome; Hydrolase; KW Magnesium; Metal-binding; Plastid; Reference proteome; KW Serine biosynthesis; Transit peptide. FT TRANSIT 1 62 Chloroplast. {ECO:0000255}. FT CHAIN 63 295 Phosphoserine phosphatase, chloroplastic. FT /FTId=PRO_0000032375. FT REGION 178 179 Substrate binding. {ECO:0000250}. FT ACT_SITE 89 89 Nucleophile. {ECO:0000250}. FT ACT_SITE 91 91 Proton donor. {ECO:0000250}. FT METAL 89 89 Magnesium. {ECO:0000250}. FT METAL 91 91 Magnesium; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 248 248 Magnesium. {ECO:0000250}. FT BINDING 98 98 Substrate. {ECO:0000250}. FT BINDING 134 134 Substrate. {ECO:0000250}. FT BINDING 227 227 Substrate. {ECO:0000250}. FT CONFLICT 266 266 C -> S (in Ref. 1; BAA33806/BAA33807). FT {ECO:0000305}. SQ SEQUENCE 295 AA; 32318 MW; F14C95E636F7745E CRC64; MEALTTSRVV PVQVPCRKLS SLFANFSCLE LRRYPCRGLV SIMNHPKLLR PVTASVQPHE LSTLGHEGNI VPSKEILDLW RSVEAVCFDV DSTVCVDEGI DELAEFCGAG KAVAEWTARA MGGSVPFEEA LAARLSLFKP SLSKVEEYLD KRPPRLSPGI EELVKKLRAN NIDVYLISGG FRQMINPVAS ILGIPRENIF ANNLLFGNSG EFLGFDENEP TSRSGGKAKA VQQIRKGRLY KTMAMIGDGA TDLEARKPGG ADLFICYAGV QLREAVAANA DWLIFKFESL INSLD //