SGAT_ARATH
ID SGAT_ARATH Reviewed; 401 AA.
AC Q56YA5; O81248;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Serine--glyoxylate aminotransferase {ECO:0000305|PubMed:18235971, ECO:0000305|PubMed:23098902};
DE EC=2.6.1.45 {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
DE AltName: Full=Alanine--glyoxylate aminotransferase {ECO:0000305|PubMed:18235971, ECO:0000305|PubMed:23098902};
DE Short=AGT {ECO:0000305|PubMed:18235971, ECO:0000305|PubMed:23098902};
DE EC=2.6.1.44 {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
DE AltName: Full=Asparagine aminotransferase {ECO:0000305|PubMed:18235971, ECO:0000305|PubMed:23098902};
DE EC=2.6.1.-;
DE AltName: Full=Serine--pyruvate aminotransferase {ECO:0000305|PubMed:18235971, ECO:0000305|PubMed:23098902};
DE EC=2.6.1.51 {ECO:0000269|PubMed:23098902};
GN Name=AGT1 {ECO:0000303|PubMed:11309139};
GN OrderedLocusNames=At2g13360 {ECO:0000312|Araport:AT2G13360};
GN ORFNames=F14O4.7 {ECO:0000312|EMBL:AAD28669.1};
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].
RC STRAIN=cv. Columbia;
RA Liepman A.H., Olsen L.J.;
RT "Sequence analysis of a cDNA encoding alanine:glyoxylate aminotransferase
RT from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR98-113(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Yamaguchi K., Takeuchi Y., Nishimura M.;
RT "Molecular characterization of serine:glyoxylate aminotransferase localized
RT in plant leaf peroxisomes.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 278-401.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP CHARACTERIZATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF PRO-251.
RX PubMed=11309139; DOI=10.1046/j.1365-313x.2001.00961.x;
RA Liepman A.H., Olsen L.J.;
RT "Peroxisomal alanine:glyoxylate aminotransferase (AGT1) is a
RT photorespiratory enzyme with multiple substrates in Arabidopsis thaliana.";
RL Plant J. 25:487-498(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP ACTIVITY REGULATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=18235971; DOI=10.1111/j.1745-7270.2008.00383.x;
RA Kendziorek M., Paszkowski A.;
RT "Properties of serine:glyoxylate aminotransferase purified from Arabidopsis
RT thaliana leaves.";
RL Acta Biochim. Biophys. Sin. 40:102-110(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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 [12]
RP FUNCTION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND INDUCTION BY ASPARAGINE.
RC STRAIN=cv. Columbia;
RX PubMed=23098902; DOI=10.1016/j.phytochem.2012.09.017;
RA Zhang Q., Lee J., Pandurangan S., Clarke M., Pajak A., Marsolais F.;
RT "Characterization of Arabidopsis serine:glyoxylate aminotransferase, AGT1,
RT as an asparagine aminotransferase.";
RL Phytochemistry 85:30-35(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RABGAP22, SUBCELLULAR
RP LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24505423; DOI=10.1371/journal.pone.0088187;
RA Roos J., Bejai S., Oide S., Dixelius C.;
RT "RabGAP22 is required for defense to the vascular pathogen Verticillium
RT longisporum and contributes to stomata immunity.";
RL PLoS ONE 9:E88187-E88187(2014).
RN [14]
RP FUNCTION, AND INDUCTION.
RX PubMed=31161264; DOI=10.1007/s00299-019-02435-9;
RA Wang R., Yang L., Han X., Zhao Y., Zhao L., Xiang B., Zhu Y., Bai Y.,
RA Wang Y.;
RT "Overexpression of AtAGT1 promoted root growth and development during
RT seedling establishment.";
RL Plant Cell Rep. 38:1165-1180(2019).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS)IN COMPLEX WITH 3-HYDROXYPYRUVATE AND
RP PYRIDOXAL 5'-PHOSPHATE, AND HOMODIMERIZATION.
RX PubMed=31681359; DOI=10.3389/fpls.2019.01229;
RA Liepman A.H., Vijayalakshmi J., Peisach D., Hulsebus B., Olsen L.J.,
RA Saper M.A.;
RT "Crystal structure of photorespiratory alanine:glyoxylate aminotransferase
RT 1 (AGT1) from Arabidopsis thaliana.";
RL Front. Plant Sci. 10:1229-1229(2019).
CC -!- FUNCTION: Photorespiratory enzyme that catalyzes transamination
CC reactions with multiple substrates, including asparagine. Functions
CC exclusively as a catabolic enzyme in Asn metabolism (PubMed:18235971,
CC PubMed:23098902). Involved in root development during seedling
CC establishment after seed germination by regulating serine homeostasis
CC and acetate conversion (PubMed:31161264). {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902, ECO:0000269|PubMed:31161264}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-serine = 3-hydroxypyruvate + glycine;
CC Xref=Rhea:RHEA:19125, ChEBI:CHEBI:17180, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305; EC=2.6.1.45;
CC Evidence={ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19126;
CC Evidence={ECO:0000269|PubMed:23098902};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19127;
CC Evidence={ECO:0000269|PubMed:23098902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-alanine = glycine + pyruvate;
CC Xref=Rhea:RHEA:24248, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57972; EC=2.6.1.44;
CC Evidence={ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24249;
CC Evidence={ECO:0000269|PubMed:23098902};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24250;
CC Evidence={ECO:0000269|PubMed:23098902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine + pyruvate = 3-hydroxypyruvate + L-alanine;
CC Xref=Rhea:RHEA:22852, ChEBI:CHEBI:15361, ChEBI:CHEBI:17180,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57972; EC=2.6.1.51;
CC Evidence={ECO:0000269|PubMed:23098902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22853;
CC Evidence={ECO:0000269|PubMed:23098902};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22854;
CC Evidence={ECO:0000269|PubMed:23098902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxypyruvate + L-asparagine = 2-oxosuccinamate + L-
CC serine; Xref=Rhea:RHEA:68380, ChEBI:CHEBI:17180, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57735, ChEBI:CHEBI:58048;
CC Evidence={ECO:0000269|PubMed:23098902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68381;
CC Evidence={ECO:0000269|PubMed:23098902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-asparagine = 2-oxosuccinamate + glycine;
CC Xref=Rhea:RHEA:68376, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:57735, ChEBI:CHEBI:58048;
CC Evidence={ECO:0000269|PubMed:23098902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68377;
CC Evidence={ECO:0000269|PubMed:23098902};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-asparagine + pyruvate = 2-oxosuccinamate + L-alanine;
CC Xref=Rhea:RHEA:68372, ChEBI:CHEBI:15361, ChEBI:CHEBI:57735,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:58048;
CC Evidence={ECO:0000269|PubMed:23098902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68373;
CC Evidence={ECO:0000269|PubMed:23098902};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:31681359};
CC -!- ACTIVITY REGULATION: Inhibited by aminooxyacetate and beta-chloro-L-
CC alanine, but not by p-hydroxymercuribenzoate.
CC {ECO:0000269|PubMed:18235971}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.87 mM for alanine (with recombinant enzyme, in the presence of
CC 20 mM glyoxylate) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=1.08 mM for alanine (with recombinant enzyme, in the presence of
CC 20 mM hydroxypyruvate) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=2.47 mM for serine (with recombinant enzyme, in the presence of 20
CC mM glyoxylate) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=0.99 mM for serine (with recombinant enzyme, in the presence of 20
CC mM pyruvate) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=0.59 mM for glycine (with recombinant enzyme, in the presence of
CC 20 mM pyruvate) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=1.58 mM for glycine (with recombinant enzyme, in the presence of 1
CC mM hydroxypyruvate) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=2.82 mM for asparagine (with recombinant enzyme, in the presence
CC of 20 mM glyoxylate) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=3.79 mM for asparagine (with recombinant enzyme, in the presence
CC of 20 mM hydroxypyruvate) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=5.0 mM for L-serine (with native enzyme, in the presence of 10 mM
CC glyoxylate) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=1.53 mM for L-serine (with native enzyme, in the presence of 0.5
CC mM glyoxylate) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=0.91 mM for glyoxylate (with native enzyme, in the presence of 30
CC mM L-serine) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=2.83 mM for glycine (with native enzyme, in the presence of 0.5 mM
CC hydroxypyruvate) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=0.57 mM for hydroxypyruvate (with native enzyme, in the presence
CC of 15.4 mM glycine) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=1.25 mM for L-alanine (with native enzyme, in the presence of 10
CC mM glyoxylate) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=0.58 mM for L-alanine (with native enzyme, in the presence of 0.5
CC mM glyoxylate) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=0.50 mM for glyoxylate (with native enzyme, in the presence of 30
CC mM L-alanine) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC KM=1.25 mM for glycine (with native enzyme, in the presence of 0.5 mM
CC pyruvate) {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
CC KM=0.22 mM for pyruvate (with native enzyme, in the presence of 15.4
CC mM glycine) {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC Vmax=50.2 nmol/sec/mg enzyme with alanine as substrate (with
CC recombinant enzyme, in the presence of 20 mM glyoxylate)
CC {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
CC Vmax=73.8 nmol/sec/mg enzyme with alanine as substrate (with
CC recombinant enzyme, in the presence of 20 mM hydroxypyruvate)
CC {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
CC Vmax=33.2 nmol/sec/mg enzyme with serine as substrate (with
CC recombinant enzyme, in the presence of 20 mM glyoxylate)
CC {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
CC Vmax=37.0 nmol/sec/mg enzyme with serine as substrate (with
CC recombinant enzyme, in the presence of 20 mM pyruvate)
CC {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
CC Vmax=8.4 nmol/sec/mg enzyme with glycine as substrate (with
CC recombinant enzyme, in the presence of 20 mM pyruvate)
CC {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
CC Vmax=3.8 nmol/sec/mg enzyme with glycine as substrate (with
CC recombinant enzyme, in the presence of 1 mM hydroxypyruvate)
CC {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
CC Vmax=292 nmol/sec/mg enzyme with asparagine as substrate (with
CC recombinant enzyme, in the presence of 20 mM glyoxylate)
CC {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
CC Vmax=704 nmol/sec/mg enzyme with asparagine as substrate (with
CC recombinant enzyme, in the presence of 20 mM pyruvate)
CC {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
CC Vmax=358 nmol/sec/mg enzyme with asparagine as substrate (with
CC recombinant enzyme, in the presence of 20 mM hydroxypyruvate)
CC {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
CC Vmax=7.64 umol/min/mg enzyme with L-serine as substrate (with native
CC enzyme, in the presence of 10 mM glyoxylate)
CC {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
CC Vmax=3.42 umol/min/mg enzyme with L-alanine as substrate (with native
CC enzyme, in the presence of 10 mM glyoxylate)
CC {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
CC Note=kcat is 6.4 sec(-1) for L-serine. kcat is 2.86 sec(-1) for L-
CC alanine.;
CC pH dependence:
CC Optimum pH is 9.2. {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:23098902};
CC -!- SUBUNIT: Forms homodimers (PubMed:18235971, PubMed:31681359). Interacts
CC with RABGAP22 (PubMed:24505423). {ECO:0000269|PubMed:18235971,
CC ECO:0000269|PubMed:24505423, ECO:0000269|PubMed:31681359}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11309139,
CC ECO:0000269|PubMed:24505423}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Preferentially expressed in
CC green, leafy tissues, root cortex and epidermis, developing siliques
CC and dry seeds. {ECO:0000269|PubMed:11309139,
CC ECO:0000269|PubMed:23098902}.
CC -!- INDUCTION: Up-regulated in roots after treatment with asparagine
CC (PubMed:23098902). Induced in roots by infection with the soil-born
CC fungal pathogen Verticillium longisporum (PubMed:24505423). Induced in
CC roots by abscicic acid (ABA) and salt stress (PubMed:31161264).
CC {ECO:0000269|PubMed:23098902, ECO:0000269|PubMed:24505423,
CC ECO:0000269|PubMed:31161264}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:24505423}.
CC -!- MISCELLANEOUS: Preferentially acts as a serine--glyoxylate
CC aminotransferase in vitro (PubMed:18235971). Seedlings overexpressing
CC AGT1 exhibit increased length of primary roots, increased number of
CC lateral roots and increased tolerance to salt stress (PubMed:31161264).
CC {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:31161264}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AF063901; AAC26854.1; -; mRNA.
DR EMBL; AB048945; BAB20811.1; -; mRNA.
DR EMBL; AC007209; AAD28669.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06227.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06228.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62628.1; -; Genomic_DNA.
DR EMBL; AY096498; AAM20136.1; -; mRNA.
DR EMBL; AY114010; AAM45058.1; -; mRNA.
DR EMBL; AK221418; BAD94403.1; -; mRNA.
DR PIR; T52250; T52250.
DR RefSeq; NP_001318216.1; NM_001335388.1.
DR RefSeq; NP_178969.1; NM_126925.5.
DR RefSeq; NP_849951.1; NM_179620.2.
DR PDB; 6PK1; X-ray; 2.10 A; A/B=1-401.
DR PDB; 6PK3; X-ray; 2.18 A; A/B=1-401.
DR PDBsum; 6PK1; -.
DR PDBsum; 6PK3; -.
DR AlphaFoldDB; Q56YA5; -.
DR SMR; Q56YA5; -.
DR BioGRID; 1183; 4.
DR IntAct; Q56YA5; 4.
DR MINT; Q56YA5; -.
DR STRING; 3702.AT2G13360.1; -.
DR iPTMnet; Q56YA5; -.
DR PaxDb; Q56YA5; -.
DR PRIDE; Q56YA5; -.
DR ProteomicsDB; 234543; -.
DR EnsemblPlants; AT2G13360.1; AT2G13360.1; AT2G13360.
DR EnsemblPlants; AT2G13360.2; AT2G13360.2; AT2G13360.
DR EnsemblPlants; AT2G13360.3; AT2G13360.3; AT2G13360.
DR GeneID; 815822; -.
DR Gramene; AT2G13360.1; AT2G13360.1; AT2G13360.
DR Gramene; AT2G13360.2; AT2G13360.2; AT2G13360.
DR Gramene; AT2G13360.3; AT2G13360.3; AT2G13360.
DR KEGG; ath:AT2G13360; -.
DR Araport; AT2G13360; -.
DR TAIR; locus:2041649; AT2G13360.
DR eggNOG; KOG2862; Eukaryota.
DR HOGENOM; CLU_027686_1_0_1; -.
DR InParanoid; Q56YA5; -.
DR OMA; KNWLPIM; -.
DR OrthoDB; 984738at2759; -.
DR PhylomeDB; Q56YA5; -.
DR BioCyc; ARA:AT2G13360-MON; -.
DR BioCyc; MetaCyc:AT2G13360-MON; -.
DR BRENDA; 2.6.1.14; 399.
DR BRENDA; 2.6.1.44; 399.
DR BRENDA; 2.6.1.45; 399.
DR SABIO-RK; Q56YA5; -.
DR PRO; PR:Q56YA5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q56YA5; baseline and differential.
DR Genevisible; Q56YA5; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0050281; F:serine-glyoxylate transaminase activity; IDA:TAIR.
DR GO; GO:0004760; F:serine-pyruvate transaminase activity; IDA:TAIR.
DR GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IBA:GO_Central.
DR GO; GO:0009853; P:photorespiration; NAS:TAIR.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminotransferase; Peroxisome; Phosphoprotein;
KW Photorespiration; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..401
FT /note="Serine--glyoxylate aminotransferase"
FT /id="PRO_0000150234"
FT MOTIF 399..401
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 68..70
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:31681359,
FT ECO:0007744|PDB:6PK1, ECO:0007744|PDB:6PK3"
FT BINDING 148
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:31681359,
FT ECO:0007744|PDB:6PK1, ECO:0007744|PDB:6PK3"
FT BINDING 200..201
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:31681359,
FT ECO:0007744|PDB:6PK1, ECO:0007744|PDB:6PK3"
FT BINDING 201
FT /ligand="3-hydroxypyruvate"
FT /ligand_id="ChEBI:CHEBI:17180"
FT /evidence="ECO:0000269|PubMed:31681359,
FT ECO:0007744|PDB:6PK1"
FT BINDING 347
FT /ligand="3-hydroxypyruvate"
FT /ligand_id="ChEBI:CHEBI:17180"
FT /evidence="ECO:0000269|PubMed:31681359,
FT ECO:0007744|PDB:6PK1"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 201
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MUTAGEN 251
FT /note="P->L: Abolishes aminotransferase activity."
FT /evidence="ECO:0000269|PubMed:11309139"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 39..55
FT /evidence="ECO:0007829|PDB:6PK1"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 69..80
FT /evidence="ECO:0007829|PDB:6PK1"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:6PK1"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:6PK1"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:6PK1"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 156..165
FT /evidence="ECO:0007829|PDB:6PK1"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:6PK1"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:6PK1"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:6PK1"
FT TURN 199..203
FT /evidence="ECO:0007829|PDB:6PK3"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 216..222
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 234..242
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 253..269
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 271..292
FT /evidence="ECO:0007829|PDB:6PK1"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:6PK1"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 319..330
FT /evidence="ECO:0007829|PDB:6PK1"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:6PK1"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:6PK1"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 356..372
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 381..393
FT /evidence="ECO:0007829|PDB:6PK1"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:6PK1"
SQ SEQUENCE 401 AA; 44208 MW; 608E7EFD840C84D3 CRC64;
MDYMYGPGRH HLFVPGPVNI PEPVIRAMNR NNEDYRSPAI PALTKTLLED VKKIFKTTSG
TPFLFPTTGT GAWESALTNT LSPGDRIVSF LIGQFSLLWI DQQKRLNFNV DVVESDWGQG
ANLQVLASKL SQDENHTIKA ICIVHNETAT GVTNDISAVR TLLDHYKHPA LLLVDGVSSI
CALDFRMDEW GVDVALTGSQ KALSLPTGLG IVCASPKALE ATKTSKSLKV FFDWNDYLKF
YKLGTYWPYT PSIQLLYGLR AALDLIFEEG LENIIARHAR LGKATRLAVE AWGLKNCTQK
EEWISNTVTA VMVPPHIDGS EIVRRAWQRY NLSLGLGLNK VAGKVFRIGH LGNVNELQLL
GCLAGVEMIL KDVGYPVVMG SGVAAASTYL QHHIPLIPSR I
