SERB2_ARATH
ID SERB2_ARATH Reviewed; 422 AA.
AC Q9SHP0; Q0WPU8;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Phosphoserine aminotransferase 2, chloroplastic;
DE Short=AtPSAT2;
DE EC=2.6.1.52;
DE Flags: Precursor;
GN Name=PSAT2; OrderedLocusNames=At2g17630; ORFNames=T19E12.3;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-51, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER CYS-50, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP FUNCTION.
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: Involved in the plastidial phosphorylated pathway of serine
CC biosynthesis (PPSB). Catalyzes the reversible conversion of 3-
CC phosphohydroxypyruvate to phosphoserine. {ECO:0000269|PubMed:24368794}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate +
CC L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-
CC oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452,
CC ChEBI:CHEBI:58538; EC=2.6.1.52;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 2/3.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily. {ECO:0000305}.
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DR EMBL; AC007509; AAD32948.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06659.1; -; Genomic_DNA.
DR EMBL; BT023418; AAY56409.1; -; mRNA.
DR EMBL; BT025981; ABG25070.1; -; mRNA.
DR EMBL; AK228962; BAF00851.1; -; mRNA.
DR PIR; E84554; E84554.
DR RefSeq; NP_179354.1; NM_127317.5.
DR AlphaFoldDB; Q9SHP0; -.
DR SMR; Q9SHP0; -.
DR BioGRID; 1627; 13.
DR STRING; 3702.AT2G17630.1; -.
DR iPTMnet; Q9SHP0; -.
DR PaxDb; Q9SHP0; -.
DR PRIDE; Q9SHP0; -.
DR ProteomicsDB; 232785; -.
DR EnsemblPlants; AT2G17630.1; AT2G17630.1; AT2G17630.
DR GeneID; 816270; -.
DR Gramene; AT2G17630.1; AT2G17630.1; AT2G17630.
DR KEGG; ath:AT2G17630; -.
DR Araport; AT2G17630; -.
DR TAIR; locus:2057259; AT2G17630.
DR eggNOG; KOG2790; Eukaryota.
DR HOGENOM; CLU_034866_0_2_1; -.
DR InParanoid; Q9SHP0; -.
DR OMA; MDAPRHV; -.
DR OrthoDB; 1357311at2759; -.
DR PhylomeDB; Q9SHP0; -.
DR BioCyc; ARA:AT2G17630-MON; -.
DR BRENDA; 2.6.1.52; 399.
DR UniPathway; UPA00135; UER00197.
DR PRO; PR:Q9SHP0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SHP0; baseline and differential.
DR Genevisible; Q9SHP0; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0006564; P:L-serine biosynthetic process; IBA:GO_Central.
DR CDD; cd00611; PSAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR022278; Pser_aminoTfrase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43247; PTHR43247; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01364; serC_1; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Aminotransferase; Chloroplast;
KW Plastid; Pyridoxal phosphate; Reference proteome; Serine biosynthesis;
KW Transferase; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 51..422
FT /note="Phosphoserine aminotransferase 2, chloroplastic"
FT /id="PRO_0000430238"
FT BINDING 101
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 135..136
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 298..299
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 51
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 257
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 350
FT /note="V -> I (in Ref. 5; BAF00851)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="E -> K (in Ref. 5; BAF00851)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 46634 MW; B12A60B66299F00E CRC64;
MAASTNSFLI GNQTQIPSLK PKSISQSFIH FTKPNTINLT TRTKSVSIRC ASASTTVGSE
QRVINFAAGP AALPENVLLK AQSDLYNWRG SGMSVMEMSH RGKEFLSIIQ KAESDLRQLL
EIPSEYSVLF LQGGATTQFA ALPLNLCKSD DSVDYIVTGS WGDKAFKEAK KYCNPKVIWS
GKSEKYTKVP TFDGLEQSSD AKYLHICANE TIHGVEFKDY PLVENPDGVL IADMSSNFCS
KPVDVSKFGV IYAGAQKNVG PSGVTIVIIR KDLIGNARDI TPVMLDYKIH DENSSLYNTP
PCFGIYMCGL VFDDLLEQGG LKEVEKKNQR KAELLYNAID ESRGFFRCPV EKSVRSLMNV
PFTLEKSELE AEFIKEAAKE KMVQLKGHRS VGGMRASIYN AMPLAGVEKL VAFMKDFQAR
HA
