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 13-SEP-2023, entry version 150. 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; ORFNames=F26I16.2; 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 [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 expression RT 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., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., 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., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis 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 reference RT 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., 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, 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 for RT 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 pathway RT is essential for development and required for ammonium assimilation and RT 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 proceeds CC via the formation of a phosphoryl-enzyme intermediates. Required for CC embryo, pollen and root development. May be required preferentially for CC serine biosynthesis in non-photosynthetic tissues. CC {ECO:0000269|PubMed:10196182, 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 serine was CC observed.; CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from CC 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 family. CC {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 AlphaFoldDB; O82796; -. DR SMR; O82796; -. DR BioGRID; 23684; 1. DR IntAct; O82796; 1. DR STRING; 3702.AT1G18640.2; -. DR PaxDb; O82796; -. DR ProteomicsDB; 232675; -. 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; AT1G18640; PSP. DR eggNOG; KOG1615; Eukaryota. DR HOGENOM; CLU_036368_2_1_1; -. DR InParanoid; O82796; -. DR OMA; RAQYYVT; -. DR OrthoDB; 275980at2759; -. DR PhylomeDB; O82796; -. DR BioCyc; ARA:AT1G18640-MONOMER; -. DR BioCyc; MetaCyc:AT1G18640-MONOMER; -. DR BRENDA; 3.1.3.3; 399. 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:0009536; C:plastid; IDA:TAIR. DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IDA:TAIR. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. 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 GO; GO:0000096; P:sulfur amino acid metabolic process; IMP:TAIR. DR CDD; cd04309; HAD_PSP_eu; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR004469; PSP. DR NCBIfam; TIGR01488; HAD-SF-IB; 1. DR NCBIfam; TIGR00338; serB; 1. DR PANTHER; PTHR43344; PHOSPHOSERINE PHOSPHATASE; 1. DR PANTHER; PTHR43344:SF2; PHOSPHOSERINE PHOSPHATASE; 1. DR Pfam; PF00702; Hydrolase; 1. DR SUPFAM; SSF56784; HAD-like; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Chloroplast; Hydrolase; Magnesium; Metal-binding; KW Plastid; Reference proteome; Serine biosynthesis; Transit peptide. FT TRANSIT 1..62 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 63..295 FT /note="Phosphoserine phosphatase, chloroplastic" FT /id="PRO_0000032375" FT ACT_SITE 89 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 91 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 89 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 91 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 98 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 134 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 178..179 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 227 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 248 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT CONFLICT 266 FT /note="C -> S (in Ref. 1; BAA33806/BAA33807)" FT /evidence="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 //