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Glutamate--glyoxylate aminotransferase 1 (AtGGT2) (EC 2.6.1.4) (Alanine aminotransferase GGT1) (EC 2.6.1.2) (Alanine--glyoxylate aminotransferase GGT1) (EC 2.6.1.44) (Alanine-2-oxoglutarate aminotransferase 1) (EC 2.6.1.-)

 GGT1_ARATH              Reviewed;         481 AA.
Q9LR30; B9DFR2; Q93Z05; Q94B22; Q9C5K2;
21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-APR-2018, entry version 122.
RecName: Full=Glutamate--glyoxylate aminotransferase 1;
Short=AtGGT2;
EC=2.6.1.4 {ECO:0000269|PubMed:12529529};
AltName: Full=Alanine aminotransferase GGT1;
EC=2.6.1.2 {ECO:0000269|PubMed:12529529};
AltName: Full=Alanine--glyoxylate aminotransferase GGT1;
EC=2.6.1.44 {ECO:0000269|PubMed:12529529};
AltName: Full=Alanine-2-oxoglutarate aminotransferase 1;
EC=2.6.1.-;
Name=GGAT1; Synonyms=AOAT1, GGT1; OrderedLocusNames=At1g23310;
ORFNames=F26F24.16, F26F24_4;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND INDUCTION BY LIGHT.
PubMed=12529529; DOI=10.1104/pp.011460;
Liepman A.H., Olsen L.J.;
"Alanine aminotransferase homologs catalyze the glutamate:glyoxylate
aminotransferase reaction in peroxisomes of Arabidopsis.";
Plant Physiol. 131:215-227(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[7]
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).
[8]
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE
SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
PubMed=12631323; DOI=10.1046/j.1365-313X.2003.01688.x;
Igarashi D., Miwa T., Seki M., Kobayashi M., Kato T., Tabata S.,
Shinozaki K., Ohsumi C.;
"Identification of photorespiratory glutamate:glyoxylate
aminotransferase (GGAT) gene in Arabidopsis.";
Plant J. 33:975-987(2003).
[9]
FUNCTION IN PHOTORESPIRATION.
STRAIN=cv. Columbia;
PubMed=16950862; DOI=10.1104/pp.106.085514;
Igarashi D., Tsuchida H., Miyao M., Ohsumi C.;
"Glutamate:glyoxylate aminotransferase modulates amino acid content
during photorespiration.";
Plant Physiol. 142:901-910(2006).
[10]
TISSUE SPECIFICITY, AND INDUCTION BY HYPOXIC STRESS.
PubMed=17319845; DOI=10.1111/j.1365-313X.2006.03023.x;
Miyashita Y., Dolferus R., Ismond K.P., Good A.G.;
"Alanine aminotransferase catalyses the breakdown of alanine after
hypoxia in Arabidopsis thaliana.";
Plant J. 49:1108-1121(2007).
[11]
FUNCTION, MUTAGENESIS OF LEU-109, AND DISRUPTION PHENOTYPE.
STRAIN=cv. C24, and cv. Columbia;
PubMed=17318317; DOI=10.1007/s11103-007-9145-z;
Verslues P.E., Kim Y.-S., Zhu J.-K.;
"Altered ABA, proline and hydrogen peroxide in an Arabidopsis
glutamate:glyoxylate aminotransferase mutant.";
Plant Mol. Biol. 64:205-217(2007).
-!- FUNCTION: Catalyzes the glutamate:glyoxylate (GGT or GGAT),
alanine:glyoxylate (AGT), alanine:2-oxoglutarate (AKT) and
glutamate:pyruvate (GPT) aminotransferase reactions in
peroxisomes. Required for abscisic acid (ABA)- and stress-mediated
responses in an H(2)O(2)-dependent manner. Function as a
photorespiratory aminotransferase that modulates amino acid
content during photorespiration (GGAT activity); promotes serine,
glycine and citrulline metabolism in response to light.
{ECO:0000269|PubMed:12529529, ECO:0000269|PubMed:12631323,
ECO:0000269|PubMed:16950862, ECO:0000269|PubMed:17318317}.
-!- CATALYTIC ACTIVITY: L-alanine + 2-oxoglutarate = pyruvate + L-
glutamate. {ECO:0000269|PubMed:12529529}.
-!- CATALYTIC ACTIVITY: L-alanine + glyoxylate = pyruvate + glycine.
{ECO:0000269|PubMed:12529529}.
-!- CATALYTIC ACTIVITY: Glycine + 2-oxoglutarate = glyoxylate + L-
glutamate. {ECO:0000269|PubMed:12529529}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.00 mM for glutamate {ECO:0000269|PubMed:12529529};
KM=7.16 mM for alanine {ECO:0000269|PubMed:12529529};
KM=0.27 mM for glyoxylate {ECO:0000269|PubMed:12529529};
KM=0.27 mM for 2-oxoglutarate {ECO:0000269|PubMed:12529529};
KM=0.33 mM for pyruvate {ECO:0000269|PubMed:12529529};
-!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine
from glyoxylate: step 1/1.
-!- PATHWAY: Photosynthesis; C4 acid pathway.
-!- PATHWAY: Amino-acid degradation; L-alanine degradation via
transaminase pathway; pyruvate from L-alanine: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:12529529,
ECO:0000269|PubMed:12631323}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9LR30-1; Sequence=Displayed;
Name=2;
IsoId=Q9LR30-2; Sequence=VSP_042465, VSP_042466;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Mostly expressed in leaves, and, to a lower
extent, in shoots, stems, flowers, seedlings and green siliques.
{ECO:0000269|PubMed:12529529, ECO:0000269|PubMed:12631323,
ECO:0000269|PubMed:17319845}.
-!- INDUCTION: Down regulated in the dark. Slightly induced upon low-
oxygen stress in shoots. {ECO:0000269|PubMed:12529529,
ECO:0000269|PubMed:17319845}.
-!- PTM: The N-terminus is blocked. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Reduced growth. Loss of alanine
aminotransferase activity and increased light sensitivity
alleviated by addition of sucrose and rescued by high CO(2).
Higher H(2)O(2) levels in light conditions. Greater root growth in
low water potential and upon NaCl-stress.
{ECO:0000269|PubMed:12631323, ECO:0000269|PubMed:17318317}.
-!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
aminotransferase family. Alanine aminotransferase subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF479639; AAN62332.1; -; mRNA.
EMBL; AC005292; AAF87015.1; -; Genomic_DNA.
EMBL; CP002684; AEE30370.1; -; Genomic_DNA.
EMBL; CP002684; AEE30371.1; -; Genomic_DNA.
EMBL; AF360195; AAK25905.1; -; mRNA.
EMBL; AY042902; AAK68842.1; -; mRNA.
EMBL; AY056379; AAL08235.1; -; mRNA.
EMBL; AY058868; AAL24255.1; -; mRNA.
EMBL; AY150373; AAN12918.1; -; mRNA.
EMBL; BT002643; AAO11559.1; -; mRNA.
EMBL; AK316871; BAH19579.1; -; mRNA.
PIR; B86367; B86367.
RefSeq; NP_001031083.1; NM_001036006.1. [Q9LR30-2]
RefSeq; NP_564192.2; NM_102180.4. [Q9LR30-1]
UniGene; At.24749; -.
ProteinModelPortal; Q9LR30; -.
SMR; Q9LR30; -.
BioGrid; 24179; 2.
IntAct; Q9LR30; 2.
MINT; Q9LR30; -.
STRING; 3702.AT1G23310.1; -.
iPTMnet; Q9LR30; -.
PaxDb; Q9LR30; -.
PRIDE; Q9LR30; -.
ProMEX; Q9LR30; -.
EnsemblPlants; AT1G23310.1; AT1G23310.1; AT1G23310. [Q9LR30-1]
EnsemblPlants; AT1G23310.2; AT1G23310.2; AT1G23310. [Q9LR30-2]
GeneID; 838940; -.
Gramene; AT1G23310.1; AT1G23310.1; AT1G23310. [Q9LR30-1]
Gramene; AT1G23310.2; AT1G23310.2; AT1G23310. [Q9LR30-2]
KEGG; ath:AT1G23310; -.
Araport; AT1G23310; -.
TAIR; locus:2028000; AT1G23310.
eggNOG; KOG0258; Eukaryota.
eggNOG; COG0436; LUCA.
HOGENOM; HOG000215020; -.
InParanoid; Q9LR30; -.
KO; K14272; -.
OMA; ESYEQFI; -.
OrthoDB; EOG093607KI; -.
PhylomeDB; Q9LR30; -.
BioCyc; MetaCyc:AT1G23310-MONOMER; -.
BRENDA; 2.3.2.2; 399.
Reactome; R-ATH-70614; Amino acid synthesis and interconversion (transamination).
SABIO-RK; Q9LR30; -.
UniPathway; UPA00288; UER00428.
UniPathway; UPA00322; -.
UniPathway; UPA00528; UER00586.
PRO; PR:Q9LR30; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9LR30; baseline and differential.
Genevisible; Q9LR30; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:TAIR.
GO; GO:0047958; F:glycine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0006545; P:glycine biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0009853; P:photorespiration; TAS:TAIR.
GO; GO:0001666; P:response to hypoxia; IEP:UniProtKB.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
Pfam; PF00155; Aminotran_1_2; 1.
SUPFAM; SSF53383; SSF53383; 1.
1: Evidence at protein level;
Alternative splicing; Aminotransferase; Complete proteome; Peroxisome;
Pyridoxal phosphate; Reference proteome; Transferase.
CHAIN 1 481 Glutamate--glyoxylate aminotransferase 1.
/FTId=PRO_0000416040.
MOTIF 479 481 Peroxisomal targeting signal.
MOD_RES 291 291 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
VAR_SEQ 440 441 VF -> RR (in isoform 2).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_042465.
VAR_SEQ 442 481 Missing (in isoform 2).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_042466.
MUTAGEN 109 109 L->F: In ggt1-1; loss of alanine
aminotransferase activity. Pale green and
slow growth, with increased light
sensitivity. Impaired ABA and stress
responses, including gene expression,
proline and ABA metabolism stimulation.
{ECO:0000269|PubMed:17318317}.
CONFLICT 129 129 D -> N (in Ref. 4; AAL24255/AAO11559).
{ECO:0000305}.
CONFLICT 382 382 C -> R (in Ref. 4; AAK25905).
{ECO:0000305}.
SEQUENCE 481 AA; 53301 MW; C6EA2B3BD66FD44D CRC64;
MALKALDYDT LNENVKKCQY AVRGELYLRA SELQKEGKKI IFTNVGNPHA LGQKPLTFPR
QVVALCQAPF LLDDPNVGML FPADAIARAK HYLSLTSGGL GAYSDSRGLP GVRKEVAEFI
QRRDGYPSDP ELIFLTDGAS KGVMQILNCV IRGNGDGILV PVPQYPLYSA TISLLGGTLV
PYYLDESENW GLDVANLRQS VAQARSQGIT VRAMVIINPG NPTGQCLSEA NIREILKFCY
NEKLVLLGDE VYQQNIYQDE RPFISSKKVL MEMGSPFSKE VQLVSFHTVS KGYWGECGQR
GGYFEMTNLP PRVVEEIYKV ASIALSPNVS AQIFMGLMVN PPKPGDISYD QFARESKGIL
ESLRRRARLM TDGFNSCKNV VCNFTEGAMY SFPQIRLPTG ALQAAKQAGK VPDVFYCLKL
LEATGISTVP GSGFGQKEGV FHLRTTILPA EDEMPEIMDS FKKFNDEFMT QYDNNFGYSK
M


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