SERCL_ARATH
ID SERCL_ARATH Reviewed; 238 AA.
AC F4KI56; Q8GYJ6; Q9FYE8;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Metal-independent phosphoserine phosphatase;
DE Short=iPSP;
DE EC=3.1.3.3 {ECO:0000269|PubMed:22337887};
DE AltName: Full=Phosphoglycerate mutase-like protein 3 {ECO:0000305};
GN Name=IPSP; OrderedLocusNames=At5g04120; ORFNames=F21E1.40;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22337887; DOI=10.1074/jbc.m111.330621;
RA Chiba Y., Oshima K., Arai H., Ishii M., Igarashi Y.;
RT "Discovery and analysis of cofactor-dependent phosphoglycerate mutase
RT homologs as novel phosphoserine phosphatases in Hydrogenobacter
RT thermophilus.";
RL J. Biol. Chem. 287:11934-11941(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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] OF 70-238.
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).
CC -!- FUNCTION: Phosphoglycerate mutase-like protein lacking PGM activity,
CC but having a low metal-independent phosphoserine phosphatase activity
CC in vitro. May be involved in serine biosynthesis.
CC {ECO:0000269|PubMed:22337887}.
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 Evidence={ECO:0000269|PubMed:22337887};
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 Evidence={ECO:0000269|PubMed:22337887};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=0.087 umol/min/mg enzyme toward L-phosphoserine
CC {ECO:0000269|PubMed:22337887};
CC Vmax=0.079 umol/min/mg enzyme toward D-phosphoserine
CC {ECO:0000269|PubMed:22337887};
CC Note=Measured in a reaction mixture containing 1 mM EDTA and no
CC magnesium.;
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC {ECO:0000305}.
CC -!- CAUTION: The full-length coding region has been amplified by RT-PCR and
CC sequenced, but not submitted to the EMBL/GenBank/DDBJ databases.
CC {ECO:0000305|PubMed:22337887}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC42237.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC05494.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391716; CAC05494.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90700.1; -; Genomic_DNA.
DR EMBL; AK117579; BAC42237.1; ALT_INIT; mRNA.
DR RefSeq; NP_196032.1; NM_120494.4.
DR AlphaFoldDB; F4KI56; -.
DR SMR; F4KI56; -.
DR BioGRID; 15570; 1.
DR STRING; 3702.AT5G04120.1; -.
DR PaxDb; F4KI56; -.
DR PRIDE; F4KI56; -.
DR ProteomicsDB; 232576; -.
DR EnsemblPlants; AT5G04120.1; AT5G04120.1; AT5G04120.
DR GeneID; 830290; -.
DR Gramene; AT5G04120.1; AT5G04120.1; AT5G04120.
DR KEGG; ath:AT5G04120; -.
DR Araport; AT5G04120; -.
DR TAIR; locus:2146678; AT5G04120.
DR eggNOG; KOG0235; Eukaryota.
DR HOGENOM; CLU_033323_14_0_1; -.
DR InParanoid; F4KI56; -.
DR OMA; NTQKRVQ; -.
DR OrthoDB; 1112626at2759; -.
DR PRO; PR:F4KI56; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KI56; baseline and differential.
DR Genevisible; F4KI56; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036424; F:L-phosphoserine phosphatase activity; IDA:TAIR.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0070179; P:D-serine biosynthetic process; IDA:TAIR.
DR GO; GO:0006564; P:L-serine biosynthetic process; IDA:TAIR.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..238
FT /note="Metal-independent phosphoserine phosphatase"
FT /id="PRO_0000430239"
FT ACT_SITE 32
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P62707"
FT ACT_SITE 107
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P62707"
FT SITE 176
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P62707"
SQ SEQUENCE 238 AA; 26474 MW; 8986F50F7BC24F1B CRC64;
MGHEWIDAER EFKWSEDVKV ESEVTEIVLV RHGETTWNAA GRIQGQIESD LNEVGLKQAV
AIAERLGKEE RPVAVYSSDL KRAKDTALMI AKTCFCPEVI EVPDLKERHV GSLQGLYWKE
GAEKEPEAYS AFFSSQNDLE IPGGGESFDQ LADRSMDALE QIAKKHKGER VIVVTHGGVL
RAIYLRITQA SSAGKLLNAS VNVVHLRDQK WIIDSWSDVS HLSSVGFLQR GFDGDAKP
