GGT1_ARATH
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 03-AUG-2022, entry version 141.
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=3.00 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.AT1G23310.1; -.
DR iPTMnet; Q9LR30; -.
DR PaxDb; Q9LR30; -.
DR PRIDE; Q9LR30; -.
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; locus:2028000; AT1G23310.
DR eggNOG; KOG0258; Eukaryota.
DR InParanoid; Q9LR30; -.
DR OMA; HNIYAPD; -.
DR PhylomeDB; Q9LR30; -.
DR BioCyc; ARA:AT1G23310-MON; -.
DR BioCyc; MetaCyc:AT1G23310-MON; -.
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 Genevisible; Q9LR30; AT.
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; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; IEP:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR11751; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
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
