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Serine--glyoxylate aminotransferase (EC 2.6.1.45) (Alanine--glyoxylate aminotransferase) (AGT) (EC 2.6.1.44) (Asparagine aminotransferase) (EC 2.6.1.-) (Serine--pyruvate aminotransferase) (EC 2.6.1.51)

 SGAT_ARATH              Reviewed;         401 AA.
Q56YA5; O81248;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
13-SEP-2005, sequence version 2.
28-FEB-2018, entry version 102.
RecName: Full=Serine--glyoxylate aminotransferase;
EC=2.6.1.45 {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
AltName: Full=Alanine--glyoxylate aminotransferase;
Short=AGT;
EC=2.6.1.44 {ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
AltName: Full=Asparagine aminotransferase;
EC=2.6.1.-;
AltName: Full=Serine--pyruvate aminotransferase;
EC=2.6.1.51 {ECO:0000269|PubMed:23098902};
Name=AGT1; OrderedLocusNames=At2g13360; ORFNames=F14O4.7;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Liepman A.H., Olsen L.J.;
"Sequence analysis of a cDNA encoding alanine:glyoxylate
aminotransferase from Arabidopsis thaliana.";
(er) Plant Gene Register PGR98-113(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Yamaguchi K., Takeuchi Y., Nishimura M.;
"Molecular characterization of serine:glyoxylate aminotransferase
localized in plant leaf peroxisomes.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 278-401.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
CHARACTERIZATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF PRO-251.
PubMed=11309139; DOI=10.1046/j.1365-313x.2001.00961.x;
Liepman A.H., Olsen L.J.;
"Peroxisomal alanine:glyoxylate aminotransferase (AGT1) is a
photorespiratory enzyme with multiple substrates in Arabidopsis
thaliana.";
Plant J. 25:487-498(2001).
[8]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17951448; DOI=10.1105/tpc.107.050989;
Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T.,
Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.;
"Proteome analysis of Arabidopsis leaf peroxisomes reveals novel
targeting peptides, metabolic pathways, and defense mechanisms.";
Plant Cell 19:3170-3193(2007).
[9]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
AND ENZYME REGULATION.
STRAIN=cv. Landsberg erecta;
PubMed=18235971; DOI=10.1111/j.1745-7270.2008.00383.x;
Kendziorek M., Paszkowski A.;
"Properties of serine:glyoxylate aminotransferase purified from
Arabidopsis thaliana leaves.";
Acta Biochim. Biophys. Sin. 40:102-110(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22092075; DOI=10.1021/pr200917t;
Aryal U.K., Krochko J.E., Ross A.R.;
"Identification of phosphoproteins in Arabidopsis thaliana leaves
using polyethylene glycol fractionation, immobilized metal-ion
affinity chromatography, two-dimensional gel electrophoresis and mass
spectrometry.";
J. Proteome Res. 11:425-437(2012).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[12]
FUNCTION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND INDUCTION BY ASPARAGINE.
STRAIN=cv. Columbia;
PubMed=23098902; DOI=10.1016/j.phytochem.2012.09.017;
Zhang Q., Lee J., Pandurangan S., Clarke M., Pajak A., Marsolais F.;
"Characterization of Arabidopsis serine:glyoxylate aminotransferase,
AGT1, as an asparagine aminotransferase.";
Phytochemistry 85:30-35(2013).
-!- FUNCTION: Photorespiratory enzyme that catalyzes transamination
reactions with multiple substrates, including asparagine. Function
exclusively as a catabolic enzyme in Asn metabolism.
{ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902}.
-!- CATALYTIC ACTIVITY: L-serine + glyoxylate = 3-hydroxypyruvate +
glycine. {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902}.
-!- CATALYTIC ACTIVITY: L-alanine + glyoxylate = pyruvate + glycine.
{ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902}.
-!- CATALYTIC ACTIVITY: L-serine + pyruvate = 3-hydroxypyruvate + L-
alanine. {ECO:0000269|PubMed:23098902}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- ENZYME REGULATION: Inhibited by aminooxyacetate and beta-chloro-L-
alanine, but not by p-hydroxymercuribenzoate.
{ECO:0000269|PubMed:18235971}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.87 mM for alanine (with recombinant enzyme, in the presence
of 20 mM glyoxylate) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=1.08 mM for alanine (with recombinant enzyme, in the presence
of 20 mM hydroxypyruvate) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=2.47 mM for serine (with recombinant enzyme, in the presence
of 20 mM glyoxylate) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=0.99 mM for serine (with recombinant enzyme, in the presence
of 20 mM pyruvate) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=0.59 mM for glycine (with recombinant enzyme, in the presence
of 20 mM pyruvate) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=1.58 mM for glycine (with recombinant enzyme, in the presence
of 1 mM hydroxypyruvate) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=2.82 mM for asparagine (with recombinant enzyme, in the
presence of 20 mM glyoxylate) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=3.79 mM for asparagine (with recombinant enzyme, in the
presence of 20 mM hydroxypyruvate) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=5.0 mM for L-serine (with native enzyme, in the presence of
10 mM glyoxylate) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=1.53 mM for L-serine (with native enzyme, in the presence of
0.5 mM glyoxylate) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=0.91 mM for glyoxylate (with native enzyme, in the presence
of 30 mM L-serine) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=2.83 mM for glycine (with native enzyme, in the presence of
0.5 mM hydroxypyruvate) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=0.57 mM for hydroxypyruvate (with native enzyme, in the
presence of 15.4 mM glycine) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=1.25 mM for L-alanine (with native enzyme, in the presence of
10 mM glyoxylate) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=0.58 mM for L-alanine (with native enzyme, in the presence of
0.5 mM glyoxylate) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=0.50 mM for glyoxylate (with native enzyme, in the presence
of 30 mM L-alanine) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=1.25 mM for glycine (with native enzyme, in the presence of
0.5 mM pyruvate) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
KM=0.22 mM for pyruvate (with native enzyme, in the presence of
15.4 mM glycine) {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
Vmax=50.2 nmol/sec/mg enzyme with alanine as substrate (with
recombinant enzyme, in the presence of 20 mM glyoxylate)
{ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
Vmax=73.8 nmol/sec/mg enzyme with alanine as substrate (with
recombinant enzyme, in the presence of 20 mM hydroxypyruvate)
{ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
Vmax=33.2 nmol/sec/mg enzyme with serine as substrate (with
recombinant enzyme, in the presence of 20 mM glyoxylate)
{ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
Vmax=37.0 nmol/sec/mg enzyme with serine as substrate (with
recombinant enzyme, in the presence of 20 mM pyruvate)
{ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
Vmax=8.4 nmol/sec/mg enzyme with glycine as substrate (with
recombinant enzyme, in the presence of 20 mM pyruvate)
{ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
Vmax=3.8 nmol/sec/mg enzyme with glycine as substrate (with
recombinant enzyme, in the presence of 1 mM hydroxypyruvate)
{ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
Vmax=292 nmol/sec/mg enzyme with asparagine as substrate (with
recombinant enzyme, in the presence of 20 mM glyoxylate)
{ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
Vmax=704 nmol/sec/mg enzyme with asparagine as substrate (with
recombinant enzyme, in the presence of 20 mM pyruvate)
{ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
Vmax=358 nmol/sec/mg enzyme with asparagine as substrate (with
recombinant enzyme, in the presence of 20 mM hydroxypyruvate)
{ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
Vmax=7.64 umol/min/mg enzyme with L-serine as substrate (with
native enzyme, in the presence of 10 mM glyoxylate)
{ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
Vmax=3.42 umol/min/mg enzyme with L-alanine as substrate (with
native enzyme, in the presence of 10 mM glyoxylate)
{ECO:0000269|PubMed:18235971, ECO:0000269|PubMed:23098902};
Note=kcat is 6.4 sec(-1) for L-serine. kcat is 2.86 sec(-1) for
L-alanine.;
pH dependence:
Optimum pH is 9.2. {ECO:0000269|PubMed:18235971,
ECO:0000269|PubMed:23098902};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18235971}.
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11309139}.
-!- TISSUE SPECIFICITY: Ubiquitous. Preferentially expressed in green,
leafy tissues, root cortex and epidermis, developing siliques and
dry seeds. {ECO:0000269|PubMed:11309139,
ECO:0000269|PubMed:23098902}.
-!- INDUCTION: Up-regulated in roots after treatment with asparagine.
{ECO:0000269|PubMed:23098902}.
-!- MISCELLANEOUS: Preferentially acts as a serine--glyoxylate
aminotransferase in vitro.
-!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF063901; AAC26854.1; -; mRNA.
EMBL; AB048945; BAB20811.1; -; mRNA.
EMBL; AC007209; AAD28669.1; -; Genomic_DNA.
EMBL; CP002685; AEC06227.1; -; Genomic_DNA.
EMBL; CP002685; AEC06228.1; -; Genomic_DNA.
EMBL; CP002685; ANM62628.1; -; Genomic_DNA.
EMBL; AY096498; AAM20136.1; -; mRNA.
EMBL; AY114010; AAM45058.1; -; mRNA.
EMBL; AK221418; BAD94403.1; -; mRNA.
PIR; T52250; T52250.
RefSeq; NP_001318216.1; NM_001335388.1.
RefSeq; NP_178969.1; NM_126925.5.
RefSeq; NP_849951.1; NM_179620.2.
UniGene; At.24853; -.
ProteinModelPortal; Q56YA5; -.
SMR; Q56YA5; -.
BioGrid; 1183; 4.
IntAct; Q56YA5; 4.
MINT; Q56YA5; -.
STRING; 3702.AT2G13360.1; -.
iPTMnet; Q56YA5; -.
PaxDb; Q56YA5; -.
PRIDE; Q56YA5; -.
EnsemblPlants; AT2G13360.1; AT2G13360.1; AT2G13360.
EnsemblPlants; AT2G13360.2; AT2G13360.2; AT2G13360.
EnsemblPlants; AT2G13360.3; AT2G13360.3; AT2G13360.
GeneID; 815822; -.
Gramene; AT2G13360.1; AT2G13360.1; AT2G13360.
Gramene; AT2G13360.2; AT2G13360.2; AT2G13360.
Gramene; AT2G13360.3; AT2G13360.3; AT2G13360.
KEGG; ath:AT2G13360; -.
Araport; AT2G13360; -.
TAIR; locus:2041649; AT2G13360.
eggNOG; KOG2862; Eukaryota.
eggNOG; COG0075; LUCA.
HOGENOM; HOG000171814; -.
InParanoid; Q56YA5; -.
KO; K00830; -.
OMA; WGCDDKP; -.
OrthoDB; EOG09360C7Z; -.
PhylomeDB; Q56YA5; -.
BioCyc; MetaCyc:AT2G13360-MONOMER; -.
BRENDA; 2.6.1.44; 399.
BRENDA; 2.6.1.45; 399.
Reactome; R-ATH-389661; Glyoxylate metabolism and glycine degradation.
SABIO-RK; Q56YA5; -.
PRO; PR:Q56YA5; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q56YA5; baseline and differential.
Genevisible; Q56YA5; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:TAIR.
GO; GO:0050281; F:serine-glyoxylate transaminase activity; IDA:TAIR.
GO; GO:0004760; F:serine-pyruvate transaminase activity; IDA:TAIR.
GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IBA:GO_Central.
GO; GO:0009853; P:photorespiration; NAS:TAIR.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
InterPro; IPR000192; Aminotrans_V_dom.
InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
Pfam; PF00266; Aminotran_5; 1.
PIRSF; PIRSF000524; SPT; 1.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
1: Evidence at protein level;
Acetylation; Aminotransferase; Complete proteome; Peroxisome;
Phosphoprotein; Photorespiration; Pyridoxal phosphate;
Reference proteome; Transferase.
CHAIN 1 401 Serine--glyoxylate aminotransferase.
/FTId=PRO_0000150234.
MOTIF 399 401 Microbody targeting signal.
{ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 201 201 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000244|PubMed:22092075}.
MUTAGEN 251 251 P->L: Abolishes aminotransferase
activity. {ECO:0000269|PubMed:11309139}.
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


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