ID SERB_ARATH Reviewed; 295 AA. AC O82796; Q9FZ85; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 2. DT 26-JUN-2013, entry version 92. 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; OrderedLocusNames=At1g18640; ORFNames=F26I16.2; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; 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 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; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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. CC -!- FUNCTION: Catalyzes the last step in the biosynthesis of serine CC from carbohydrates. The reaction mechanism proceeds via the CC formation of a phosphoryl-enzyme intermediates. May be required CC preferentially for serine biosynthesis in non-photosynthetic CC tissues. CC -!- CATALYTIC ACTIVITY: O-phospho-L(or D)-serine + H(2)O = L(or D)- CC serine + phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.5 mM for 3-phosphoserine (at 30 degrees Celsius and pH CC 7.5); 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 -!- TISSUE SPECIFICITY: Expressed in leaf and root. CC -!- SIMILARITY: Belongs to the SerB family. 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 IPI; IPI00526883; -. DR PIR; B86320; B86320. DR PIR; T51362; T51362. DR RefSeq; NP_973858.1; NM_202129.2. DR UniGene; At.356; -. DR UniGene; At.41785; -. DR ProteinModelPortal; O82796; -. DR SMR; O82796; 42-295. DR IntAct; O82796; 1. DR STRING; 3702.AT1G18640.2-P; -. DR PaxDb; O82796; -. DR PRIDE; O82796; -. DR EnsemblPlants; AT1G18640.2; AT1G18640.2; AT1G18640. DR GeneID; 838445; -. DR KEGG; ath:AT1G18640; -. DR GeneFarm; 4917; -. DR TAIR; AT1G18640; -. DR eggNOG; COG0560; -. DR HOGENOM; HOG000231116; -. DR KO; K01079; -. DR OMA; YAGFDES; -. DR PhylomeDB; O82796; -. DR ProtClustDB; PLN02954; -. DR BioCyc; MetaCyc:AT1G18640-MONOMER; -. DR UniPathway; UPA00135; UER00198. DR Genevestigator; O82796; -. DR GermOnline; AT1G18640; Arabidopsis thaliana. DR GO; GO:0009507; C:chloroplast; IDA:TAIR. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0004647; F:phosphoserine phosphatase activity; IDA:TAIR. DR GO; GO:0006564; P:L-serine biosynthetic process; IBA:RefGenome. DR Gene3D; 1.10.150.210; -; 1. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006383; HAD-SF_hydro_IB_PSP-like. DR InterPro; IPR023190; Pser_Pase_dom_2. DR InterPro; IPR004469; SerB. DR Pfam; PF00702; Hydrolase; 1. DR SUPFAM; SSF56784; HAD-like_dom; 1. DR TIGRFAMs; TIGR01488; HAD-SF-IB; 1. DR TIGRFAMs; TIGR00338; serB; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Chloroplast; Complete proteome; Hydrolase; KW Magnesium; Metal-binding; Phosphoprotein; Plastid; Reference proteome; KW Serine biosynthesis; Transit peptide. FT TRANSIT 1 62 Chloroplast (Potential). FT CHAIN 63 295 Phosphoserine phosphatase, chloroplastic. FT /FTId=PRO_0000032375. FT REGION 178 179 Substrate binding (By similarity). FT ACT_SITE 89 89 Nucleophile (By similarity). FT ACT_SITE 91 91 Proton donor (By similarity). FT METAL 89 89 Magnesium (By similarity). FT METAL 91 91 Magnesium; via carbonyl oxygen (By FT similarity). FT METAL 248 248 Magnesium (By similarity). FT BINDING 98 98 Substrate (By similarity). FT BINDING 134 134 Substrate (By similarity). FT BINDING 227 227 Substrate (By similarity). FT CONFLICT 266 266 C -> S (in Ref. 1; BAA33806/BAA33807). 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 //