SERC_ARATH
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 03-AUG-2022, entry version 147.
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}.
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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 PRIDE; 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; locus:2027433; AT1G18640.
DR eggNOG; KOG1615; Eukaryota.
DR HOGENOM; CLU_036368_2_1_1; -.
DR InParanoid; O82796; -.
DR OMA; RAQYYVT; -.
DR OrthoDB; 1009123at2759; -.
DR PhylomeDB; O82796; -.
DR BioCyc; ARA:AT1G18640-MON; -.
DR BioCyc; MetaCyc:AT1G18640-MON; -.
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 Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR004469; PSP.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR00338; serB; 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
