Q9LR30 (GGT1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--glyoxylate aminotransferase 1
Short name=AtGGT2
EC=2.6.1.4

Alternative name(s):
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.-

Gene names

Name:	GGAT1
Synonyms:	AOAT1, GGT1
Ordered Locus Names:	At1g23310
ORF Names:	F26F24.16, F26F24_4

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 H2O(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. Ref.1 Ref.8 Ref.9 Ref.11
Catalytic activity	L-alanine + 2-oxoglutarate = pyruvate + L-glutamate. Ref.1 L-alanine + glyoxylate = pyruvate + glycine. Ref.1 Glycine + 2-oxoglutarate = glyoxylate + L-glutamate. Ref.1
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid biosynthesis; glycine biosynthesis; glycine from glyoxylate: step 1/1. Photosynthesis; C4 acid pathway. Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.
Subunit structure	Homodimer By similarity.
Subcellular location	Peroxisome Ref.1 Ref.6 Ref.7 Ref.8.
Tissue specificity	Mostly expressed in leaves, and, to a lower extent, in shoots, stems, flowers, seedlings and green siliques. Ref.1 Ref.8 Ref.10
Induction	Down regulated in the dark. Slightly induced upon low-oxygen stress in shoots. Ref.1 Ref.10
Post-translational modification	The N-terminus is blocked By similarity.
Disruption phenotype	Reduced growth. Loss of alanine aminotransferase activity and increased light sensitivity alleviated by addition of sucrose and rescued by high CO2. Higher H2O2 levels in light conditions. Greater root growth in low water potential and upon NaCl-stress. Ref.8 Ref.11
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.
Biophysicochemical properties	Kinetic parameters: KM=3.00 mM for glutamate Ref.1 KM=7.16 mM for alanine KM=0.27 mM for glyoxylate KM=0.27 mM for 2-oxoglutarate KM=0.33 mM for pyruvate

Ontologies

Keywords
Cellular component	Peroxisome
Coding sequence diversity	Alternative splicing
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	L-alanine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway glycine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway photorespiration Traceable author statement Ref.1. Source: TAIR response to hypoxia Inferred from expression pattern Ref.10. Source: UniProtKB
Cellular_component	apoplast Inferred from direct assay PubMed 18538804. Source: TAIR chloroplast Inferred from direct assay PubMed 15028209PubMed 18431481. Source: TAIR membrane Inferred from direct assay PubMed 17432890. Source: TAIR peroxisome Inferred from direct assay Ref.7Ref.1Ref.8Ref.6. Source: TAIR vacuole Inferred from direct assay PubMed 15539469. Source: TAIR
Molecular_function	L-alanine:2-oxoglutarate aminotransferase activity Inferred from direct assay Ref.1. Source: TAIR alanine-glyoxylate transaminase activity Inferred from direct assay Ref.1. Source: TAIR glycine:2-oxoglutarate aminotransferase activity Inferred from direct assay Ref.1. Source: TAIR pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9LR30-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9LR30-2)

The sequence of this isoform differs from the canonical sequence as follows:
     440-441: VF → RR
     442-481: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 481	481	Glutamate--glyoxylate aminotransferase 1		PRO_0000416040
Regions
	Motif	479 – 481	3	Peroxisomal targeting signal
Amino acid modifications
	Modified residue	291	1	N6-(pyridoxal phosphate)lysine By similarity
Natural variations
	Alternative sequence	440 – 441	2	VF → RR in isoform 2.		VSP_042465
	Alternative sequence	442 – 481	40	Missing in isoform 2.		VSP_042466
Experimental info
	Mutagenesis	109	1	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. Ref.11
	Sequence conflict	129	1	D → N in AAL24255. Ref.4
	Sequence conflict	129	1	D → N in AAO11559. Ref.4
	Sequence conflict	382	1	C → R in AAK25905. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: C6EA2B3BD66FD44D	FASTA	481	53,301
	10 20 30 40 50 60 MALKALDYDT LNENVKKCQY AVRGELYLRA SELQKEGKKI IFTNVGNPHA LGQKPLTFPR 70 80 90 100 110 120 QVVALCQAPF LLDDPNVGML FPADAIARAK HYLSLTSGGL GAYSDSRGLP GVRKEVAEFI 130 140 150 160 170 180 QRRDGYPSDP ELIFLTDGAS KGVMQILNCV IRGNGDGILV PVPQYPLYSA TISLLGGTLV 190 200 210 220 230 240 PYYLDESENW GLDVANLRQS VAQARSQGIT VRAMVIINPG NPTGQCLSEA NIREILKFCY 250 260 270 280 290 300 NEKLVLLGDE VYQQNIYQDE RPFISSKKVL MEMGSPFSKE VQLVSFHTVS KGYWGECGQR 310 320 330 340 350 360 GGYFEMTNLP PRVVEEIYKV ASIALSPNVS AQIFMGLMVN PPKPGDISYD QFARESKGIL 370 380 390 400 410 420 ESLRRRARLM TDGFNSCKNV VCNFTEGAMY SFPQIRLPTG ALQAAKQAGK VPDVFYCLKL 430 440 450 460 470 480 LEATGISTVP GSGFGQKEGV FHLRTTILPA EDEMPEIMDS FKKFNDEFMT QYDNNFGYSK M
	Isoform 2 [UniParc]. Checksum: 337ACB390877F105	FASTA	441	48,550
	10 20 30 40 50 60 MALKALDYDT LNENVKKCQY AVRGELYLRA SELQKEGKKI IFTNVGNPHA LGQKPLTFPR 70 80 90 100 110 120 QVVALCQAPF LLDDPNVGML FPADAIARAK HYLSLTSGGL GAYSDSRGLP GVRKEVAEFI 130 140 150 160 170 180 QRRDGYPSDP ELIFLTDGAS KGVMQILNCV IRGNGDGILV PVPQYPLYSA TISLLGGTLV 190 200 210 220 230 240 PYYLDESENW GLDVANLRQS VAQARSQGIT VRAMVIINPG NPTGQCLSEA NIREILKFCY 250 260 270 280 290 300 NEKLVLLGDE VYQQNIYQDE RPFISSKKVL MEMGSPFSKE VQLVSFHTVS KGYWGECGQR 310 320 330 340 350 360 GGYFEMTNLP PRVVEEIYKV ASIALSPNVS AQIFMGLMVN PPKPGDISYD QFARESKGIL 370 380 390 400 410 420 ESLRRRARLM TDGFNSCKNV VCNFTEGAMY SFPQIRLPTG ALQAAKQAGK VPDVFYCLKL 430 440 LEATGISTVP GSGFGQKEGR R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Alanine aminotransferase homologs catalyze the glutamate:glyoxylate aminotransferase reaction in peroxisomes of Arabidopsis." Liepman A.H., Olsen L.J. Plant Physiol. 131:215-227(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY LIGHT.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." 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. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: cv. Columbia.
[5]	"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs." Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K. DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: cv. Columbia.
[6]	"Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting peptides, metabolic pathways, and defense mechanisms." Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O. Plant Cell 19:3170-3193(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 91-107 AND 213-233, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"Proteomic analysis of leaf peroxisomal proteins in greening cotyledons of Arabidopsis thaliana." Fukao Y., Hayashi M., Nishimura M. Plant Cell Physiol. 43:689-696(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"Identification of photorespiratory glutamate:glyoxylate aminotransferase (GGAT) gene in Arabidopsis." Igarashi D., Miwa T., Seki M., Kobayashi M., Kato T., Tabata S., Shinozaki K., Ohsumi C. Plant J. 33:975-987(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
[9]	"Glutamate:glyoxylate aminotransferase modulates amino acid content during photorespiration." Igarashi D., Tsuchida H., Miyao M., Ohsumi C. Plant Physiol. 142:901-910(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOTORESPIRATION. Strain: cv. Columbia.
[10]	"Alanine aminotransferase catalyses the breakdown of alanine after hypoxia in Arabidopsis thaliana." Miyashita Y., Dolferus R., Ismond K.P., Good A.G. Plant J. 49:1108-1121(2007) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION BY HYPOXIC STRESS.
[11]	"Altered ABA, proline and hydrogen peroxide in an Arabidopsis glutamate:glyoxylate aminotransferase mutant." Verslues P.E., Kim Y.-S., Zhu J.-K. Plant Mol. Biol. 64:205-217(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LEU-109, DISRUPTION PHENOTYPE. Strain: cv. C24 and cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF479639 mRNA. Translation: AAN62332.1. AC005292 Genomic DNA. Translation: AAF87015.1. CP002684 Genomic DNA. Translation: AEE30370.1. CP002684 Genomic DNA. Translation: AEE30371.1. AF360195 mRNA. Translation: AAK25905.1. AY042902 mRNA. Translation: AAK68842.1. AY056379 mRNA. Translation: AAL08235.1. AY058868 mRNA. Translation: AAL24255.1. AY150373 mRNA. Translation: AAN12918.1. BT002643 mRNA. Translation: AAO11559.1. AK316871 mRNA. Translation: BAH19579.1.
IPI	IPI00524653. IPI00657435.
PIR	B86367.
RefSeq	NP_001031083.1. NM_001036006.1. NP_564192.2. NM_102180.3.
UniGene	At.24749.
3D structure databases
ProteinModelPortal	Q9LR30.
SMR	Q9LR30. Positions 9-472.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9LR30. 1 interaction.
STRING	3702.AT1G23310.1-P.
Proteomic databases
PRIDE	Q9LR30.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G23310.1; AT1G23310.1; AT1G23310.
GeneID	838940.
KEGG	ath:AT1G23310.
Organism-specific databases
TAIR	At1g23310.
Phylogenomic databases
HOGENOM	HOG000215020.
InParanoid	Q9LR30.
KO	K14272.
OMA	CISAQLC.
PhylomeDB	Q9LR30.
ProtClustDB	PLN02368.
Enzyme and pathway databases
BioCyc	MetaCyc:AT1G23310-MONOMER.
SABIO-RK	Q9LR30.
UniPathway	UPA00288; UER00428. UPA00322. UPA00528; UER00586.
Gene expression databases
ArrayExpress	Q9LR30.
Genevestigator	Q9LR30.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GGT1_ARATH

Accession

Primary (citable) accession number: Q9LR30
Secondary accession number(s): B9DFR2 , Q93Z05, Q94B22, Q9C5K2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2012
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program