Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9LR30 (GGT1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Protein existenceEvidence 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

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 481481Glutamate--glyoxylate aminotransferase 1
PRO_0000416040

Regions

Motif479 – 4813Peroxisomal targeting signal

Amino acid modifications

Modified residue2911N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Alternative sequence440 – 4412VF → RR in isoform 2.
VSP_042465
Alternative sequence442 – 48140Missing in isoform 2.
VSP_042466

Experimental info

Mutagenesis1091L → 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 conflict1291D → N in AAL24255. Ref.4
Sequence conflict1291D → N in AAO11559. Ref.4
Sequence conflict3821C → R in AAK25905. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C6EA2B3BD66FD44D

FASTA48153,301
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 337ACB390877F105
Show »

FASTA44148,550

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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].
[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].
[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.
PIRB86367.
RefSeqNP_001031083.1. NM_001036006.1.
NP_564192.2. NM_102180.3.
UniGeneAt.24749.

3D structure databases

ProteinModelPortalQ9LR30.
SMRQ9LR30. Positions 9-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9LR30. 1 interaction.
STRING3702.AT1G23310.1-P.

Proteomic databases

PRIDEQ9LR30.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G23310.1; AT1G23310.1; AT1G23310. [Q9LR30-1]
GeneID838940.
KEGGath:AT1G23310.

Organism-specific databases

TAIRAT1G23310.

Phylogenomic databases

HOGENOMHOG000215020.
InParanoidQ9LR30.
KOK14272.
OMAQFARESK.
PhylomeDBQ9LR30.
ProtClustDBPLN02368.

Enzyme and pathway databases

BioCycMetaCyc:AT1G23310-MONOMER.
SABIO-RKQ9LR30.
UniPathwayUPA00288; UER00428.
UPA00322.
UPA00528; UER00586.

Gene expression databases

GenevestigatorQ9LR30.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGGT1_ARATH
AccessionPrimary (citable) accession number: Q9LR30
Secondary accession number(s): B9DFR2 expand/collapse secondary AC list , Q93Z05, Q94B22, Q9C5K2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names