ID   GGT1_ARATH              Reviewed;         481 AA.
AC   Q9LR30; B9DFR2; Q93Z05; Q94B22; Q9C5K2;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Glutamate--glyoxylate aminotransferase 1;
DE            Short=AtGGT2;
DE            EC=2.6.1.4 {ECO:0000269|PubMed:12529529};
DE   AltName: Full=Alanine aminotransferase GGT1;
DE            EC=2.6.1.2 {ECO:0000269|PubMed:12529529};
DE   AltName: Full=Alanine--glyoxylate aminotransferase GGT1;
DE            EC=2.6.1.44 {ECO:0000269|PubMed:12529529};
DE   AltName: Full=Alanine-2-oxoglutarate aminotransferase 1;
DE            EC=2.6.1.-;
GN   Name=GGAT1; Synonyms=AOAT1, GGT1; OrderedLocusNames=At1g23310;
GN   ORFNames=F26F24.16, F26F24_4;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   INDUCTION BY LIGHT.
RX   PubMed=12529529; DOI=10.1104/pp.011460;
RA   Liepman A.H., Olsen L.J.;
RT   "Alanine aminotransferase homologs catalyze the glutamate:glyoxylate
RT   aminotransferase reaction in peroxisomes of Arabidopsis.";
RL   Plant Physiol. 131:215-227(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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] (ISOFORM 1).
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
RN   [7]
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   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12631323; DOI=10.1046/j.1365-313x.2003.01688.x;
RA   Igarashi D., Miwa T., Seki M., Kobayashi M., Kato T., Tabata S.,
RA   Shinozaki K., Ohsumi C.;
RT   "Identification of photorespiratory glutamate:glyoxylate aminotransferase
RT   (GGAT) gene in Arabidopsis.";
RL   Plant J. 33:975-987(2003).
RN   [9]
RP   FUNCTION IN PHOTORESPIRATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=16950862; DOI=10.1104/pp.106.085514;
RA   Igarashi D., Tsuchida H., Miyao M., Ohsumi C.;
RT   "Glutamate:glyoxylate aminotransferase modulates amino acid content during
RT   photorespiration.";
RL   Plant Physiol. 142:901-910(2006).
RN   [10]
RP   TISSUE SPECIFICITY, AND INDUCTION BY HYPOXIC STRESS.
RX   PubMed=17319845; DOI=10.1111/j.1365-313x.2006.03023.x;
RA   Miyashita Y., Dolferus R., Ismond K.P., Good A.G.;
RT   "Alanine aminotransferase catalyses the breakdown of alanine after hypoxia
RT   in Arabidopsis thaliana.";
RL   Plant J. 49:1108-1121(2007).
RN   [11]
RP   FUNCTION, MUTAGENESIS OF LEU-109, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. C24, and cv. Columbia;
RX   PubMed=17318317; DOI=10.1007/s11103-007-9145-z;
RA   Verslues P.E., Kim Y.-S., Zhu J.-K.;
RT   "Altered ABA, proline and hydrogen peroxide in an Arabidopsis
RT   glutamate:glyoxylate aminotransferase mutant.";
RL   Plant Mol. Biol. 64:205-217(2007).
CC   -!- FUNCTION: Catalyzes the glutamate:glyoxylate (GGT or GGAT),
CC       alanine:glyoxylate (AGT), alanine:2-oxoglutarate (AKT) and
CC       glutamate:pyruvate (GPT) aminotransferase reactions in peroxisomes.
CC       Required for abscisic acid (ABA)- and stress-mediated responses in an
CC       H(2)O(2)-dependent manner. Functions as a photorespiratory
CC       aminotransferase that modulates amino acid content during
CC       photorespiration (GGAT activity); promotes serine, glycine and
CC       citrulline metabolism in response to light.
CC       {ECO:0000269|PubMed:12529529, ECO:0000269|PubMed:12631323,
CC       ECO:0000269|PubMed:16950862, ECO:0000269|PubMed:17318317}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC         Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC         Evidence={ECO:0000269|PubMed:12529529};
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:12529529};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + glycine = glyoxylate + L-glutamate;
CC         Xref=Rhea:RHEA:14089, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57305; EC=2.6.1.4;
CC         Evidence={ECO:0000269|PubMed:12529529};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3 mM for glutamate {ECO:0000269|PubMed:12529529};
CC         KM=7.16 mM for alanine {ECO:0000269|PubMed:12529529};
CC         KM=0.27 mM for glyoxylate {ECO:0000269|PubMed:12529529};
CC         KM=0.27 mM for 2-oxoglutarate {ECO:0000269|PubMed:12529529};
CC         KM=0.33 mM for pyruvate {ECO:0000269|PubMed:12529529};
CC   -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from
CC       glyoxylate: step 1/1.
CC   -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC       pathway; pyruvate from L-alanine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:12529529,
CC       ECO:0000269|PubMed:12631323}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9LR30-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9LR30-2; Sequence=VSP_042465, VSP_042466;
CC   -!- TISSUE SPECIFICITY: Mostly expressed in leaves, and, to a lower extent,
CC       in shoots, stems, flowers, seedlings and green siliques.
CC       {ECO:0000269|PubMed:12529529, ECO:0000269|PubMed:12631323,
CC       ECO:0000269|PubMed:17319845}.
CC   -!- INDUCTION: Down regulated in the dark. Slightly induced upon low-oxygen
CC       stress in shoots. {ECO:0000269|PubMed:12529529,
CC       ECO:0000269|PubMed:17319845}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Reduced growth. Loss of alanine aminotransferase
CC       activity and increased light sensitivity alleviated by addition of
CC       sucrose and rescued by high CO(2). Higher H(2)O(2) levels in light
CC       conditions. Greater root growth in low water potential and upon NaCl-
CC       stress. {ECO:0000269|PubMed:12631323, ECO:0000269|PubMed:17318317}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF479639; AAN62332.1; -; mRNA.
DR   EMBL; AC005292; AAF87015.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30370.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30371.1; -; Genomic_DNA.
DR   EMBL; AF360195; AAK25905.1; -; mRNA.
DR   EMBL; AY042902; AAK68842.1; -; mRNA.
DR   EMBL; AY056379; AAL08235.1; -; mRNA.
DR   EMBL; AY058868; AAL24255.1; -; mRNA.
DR   EMBL; AY150373; AAN12918.1; -; mRNA.
DR   EMBL; BT002643; AAO11559.1; -; mRNA.
DR   EMBL; AK316871; BAH19579.1; -; mRNA.
DR   PIR; B86367; B86367.
DR   RefSeq; NP_001031083.1; NM_001036006.1. [Q9LR30-2]
DR   RefSeq; NP_564192.2; NM_102180.4. [Q9LR30-1]
DR   AlphaFoldDB; Q9LR30; -.
DR   SMR; Q9LR30; -.
DR   BioGRID; 24179; 2.
DR   IntAct; Q9LR30; 2.
DR   MINT; Q9LR30; -.
DR   STRING; 3702.Q9LR30; -.
DR   iPTMnet; Q9LR30; -.
DR   PaxDb; 3702-AT1G23310-1; -.
DR   ProMEX; Q9LR30; -.
DR   ProteomicsDB; 221846; -. [Q9LR30-1]
DR   EnsemblPlants; AT1G23310.1; AT1G23310.1; AT1G23310. [Q9LR30-1]
DR   EnsemblPlants; AT1G23310.2; AT1G23310.2; AT1G23310. [Q9LR30-2]
DR   GeneID; 838940; -.
DR   Gramene; AT1G23310.1; AT1G23310.1; AT1G23310. [Q9LR30-1]
DR   Gramene; AT1G23310.2; AT1G23310.2; AT1G23310. [Q9LR30-2]
DR   KEGG; ath:AT1G23310; -.
DR   Araport; AT1G23310; -.
DR   TAIR; AT1G23310; GGT1.
DR   eggNOG; KOG0258; Eukaryota.
DR   InParanoid; Q9LR30; -.
DR   OMA; AYPIPYY; -.
DR   OrthoDB; 5472891at2759; -.
DR   PhylomeDB; Q9LR30; -.
DR   BioCyc; ARA:AT1G23310-MONOMER; -.
DR   BioCyc; MetaCyc:AT1G23310-MONOMER; -.
DR   BRENDA; 2.3.2.2; 399.
DR   SABIO-RK; Q9LR30; -.
DR   UniPathway; UPA00288; UER00428.
DR   UniPathway; UPA00322; -.
DR   UniPathway; UPA00528; UER00586.
DR   PRO; PR:Q9LR30; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LR30; baseline and differential.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:TAIR.
DR   GO; GO:0047958; F:glycine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006545; P:glycine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009853; P:photorespiration; TAS:TAIR.
DR   GO; GO:0001666; P:response to hypoxia; IEP:UniProtKB.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 1.10.287.1970; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR045088; ALAT1/2-like.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11751; ALANINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11751:SF472; GLUTAMATE--GLYOXYLATE AMINOTRANSFERASE 1; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   Genevisible; Q9LR30; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Aminotransferase; Peroxisome; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..481
FT                   /note="Glutamate--glyoxylate aminotransferase 1"
FT                   /id="PRO_0000416040"
FT   MOTIF           479..481
FT                   /note="Peroxisomal targeting signal"
FT   MOD_RES         291
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         440..441
FT                   /note="VF -> RR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19423640"
FT                   /id="VSP_042465"
FT   VAR_SEQ         442..481
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19423640"
FT                   /id="VSP_042466"
FT   MUTAGEN         109
FT                   /note="L->F: In ggt1-1; loss of alanine aminotransferase
FT                   activity. Pale green and slow growth, with increased light
FT                   sensitivity. Impaired ABA and stress responses, including
FT                   gene expression, proline and ABA metabolism stimulation."
FT                   /evidence="ECO:0000269|PubMed:17318317"
FT   CONFLICT        129
FT                   /note="D -> N (in Ref. 4; AAL24255/AAO11559)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        382
FT                   /note="C -> R (in Ref. 4; AAK25905)"
FT                   /evidence="ECO:0000305"
SQ   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
//