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Q9LR30

- GGT1_ARATH

UniProt

Q9LR30 - GGT1_ARATH

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Protein

Glutamate--glyoxylate aminotransferase 1

Gene
GGAT1, AOAT1, GGT1, At1g23310, F26F24.16, F26F24_4
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

L-alanine + 2-oxoglutarate = pyruvate + L-glutamate.1 Publication
L-alanine + glyoxylate = pyruvate + glycine.1 Publication
Glycine + 2-oxoglutarate = glyoxylate + L-glutamate.1 Publication

Cofactori

Pyridoxal phosphate By similarity.

Kineticsi

  1. KM=3.00 mM for glutamate1 Publication
  2. KM=7.16 mM for alanine
  3. KM=0.27 mM for glyoxylate
  4. KM=0.27 mM for 2-oxoglutarate
  5. KM=0.33 mM for pyruvate

Pathwayi

GO - Molecular functioni

  1. alanine-glyoxylate transaminase activity Source: TAIR
  2. glycine:2-oxoglutarate aminotransferase activity Source: TAIR
  3. L-alanine:2-oxoglutarate aminotransferase activity Source: TAIR
  4. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. glycine biosynthetic process Source: UniProtKB-UniPathway
  2. L-alanine catabolic process Source: UniProtKB-UniPathway
  3. photorespiration Source: TAIR
  4. response to hypoxia Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:AT1G23310-MONOMER.
SABIO-RKQ9LR30.
UniPathwayiUPA00288; UER00428.
UPA00322.
UPA00528; UER00586.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--glyoxylate aminotransferase 1 (EC:2.6.1.4)
Short name:
AtGGT2
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 namesi
Name:GGAT1
Synonyms:AOAT1, GGT1
Ordered Locus Names:At1g23310
ORF Names:F26F24.16, F26F24_4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G23310.

Subcellular locationi

Peroxisome 4 Publications

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. chloroplast Source: TAIR
  3. membrane Source: TAIR
  4. peroxisome Source: TAIR
  5. vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi109 – 1091L → 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. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 481481Glutamate--glyoxylate aminotransferase 1PRO_0000416040Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei291 – 2911N6-(pyridoxal phosphate)lysine By similarity

Post-translational modificationi

The N-terminus is blocked By similarity.

Proteomic databases

PRIDEiQ9LR30.

Expressioni

Tissue specificityi

Mostly expressed in leaves, and, to a lower extent, in shoots, stems, flowers, seedlings and green siliques.3 Publications

Inductioni

Down regulated in the dark. Slightly induced upon low-oxygen stress in shoots.2 Publications

Gene expression databases

GenevestigatoriQ9LR30.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

IntActiQ9LR30. 2 interactions.
STRINGi3702.AT1G23310.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9LR30.
SMRiQ9LR30. Positions 9-472.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi479 – 4813Peroxisomal targeting signal

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000215020.
InParanoidiQ9LR30.
KOiK14272.
OMAiQFARESK.
PhylomeDBiQ9LR30.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9LR30-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MALKALDYDT LNENVKKCQY AVRGELYLRA SELQKEGKKI IFTNVGNPHA    50
LGQKPLTFPR QVVALCQAPF LLDDPNVGML FPADAIARAK HYLSLTSGGL 100
GAYSDSRGLP GVRKEVAEFI QRRDGYPSDP ELIFLTDGAS KGVMQILNCV 150
IRGNGDGILV PVPQYPLYSA TISLLGGTLV PYYLDESENW GLDVANLRQS 200
VAQARSQGIT VRAMVIINPG NPTGQCLSEA NIREILKFCY NEKLVLLGDE 250
VYQQNIYQDE RPFISSKKVL MEMGSPFSKE VQLVSFHTVS KGYWGECGQR 300
GGYFEMTNLP PRVVEEIYKV ASIALSPNVS AQIFMGLMVN PPKPGDISYD 350
QFARESKGIL ESLRRRARLM TDGFNSCKNV VCNFTEGAMY SFPQIRLPTG 400
ALQAAKQAGK VPDVFYCLKL LEATGISTVP GSGFGQKEGV FHLRTTILPA 450
EDEMPEIMDS FKKFNDEFMT QYDNNFGYSK M 481
Length:481
Mass (Da):53,301
Last modified:October 1, 2000 - v1
Checksum:iC6EA2B3BD66FD44D
GO
Isoform 2 (identifier: Q9LR30-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:441
Mass (Da):48,550
Checksum:i337ACB390877F105
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei440 – 4412VF → RR in isoform 2. VSP_042465
Alternative sequencei442 – 48140Missing in isoform 2. VSP_042466Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291D → N in AAL24255. 1 Publication
Sequence conflicti129 – 1291D → N in AAO11559. 1 Publication
Sequence conflicti382 – 3821C → R in AAK25905. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiB86367.
RefSeqiNP_001031083.1. NM_001036006.1. [Q9LR30-2]
NP_564192.2. NM_102180.3. [Q9LR30-1]
UniGeneiAt.24749.

Genome annotation databases

EnsemblPlantsiAT1G23310.1; AT1G23310.1; AT1G23310. [Q9LR30-1]
GeneIDi838940.
KEGGiath:AT1G23310.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi B86367.
RefSeqi NP_001031083.1. NM_001036006.1. [Q9LR30-2 ]
NP_564192.2. NM_102180.3. [Q9LR30-1 ]
UniGenei At.24749.

3D structure databases

ProteinModelPortali Q9LR30.
SMRi Q9LR30. Positions 9-472.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9LR30. 2 interactions.
STRINGi 3702.AT1G23310.1-P.

Proteomic databases

PRIDEi Q9LR30.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G23310.1 ; AT1G23310.1 ; AT1G23310 . [Q9LR30-1 ]
GeneIDi 838940.
KEGGi ath:AT1G23310.

Organism-specific databases

TAIRi AT1G23310.

Phylogenomic databases

HOGENOMi HOG000215020.
InParanoidi Q9LR30.
KOi K14272.
OMAi QFARESK.
PhylomeDBi Q9LR30.

Enzyme and pathway databases

UniPathwayi UPA00288 ; UER00428 .
UPA00322 .
UPA00528 ; UER00586 .
BioCyci MetaCyc:AT1G23310-MONOMER.
SABIO-RK Q9LR30.

Gene expression databases

Genevestigatori Q9LR30.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
Pfami PF00155. Aminotran_1_2. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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].
  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.

Entry informationi

Entry nameiGGT1_ARATH
AccessioniPrimary (citable) accession number: Q9LR30
Secondary accession number(s): B9DFR2
, Q93Z05, Q94B22, Q9C5K2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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