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Q9LR30

- GGT1_ARATH

UniProt

Q9LR30 - GGT1_ARATH

Protein

Glutamate--glyoxylate aminotransferase 1

Gene

GGAT1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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 alanine1 Publication
    3. KM=0.27 mM for glyoxylate1 Publication
    4. KM=0.27 mM for 2-oxoglutarate1 Publication
    5. KM=0.33 mM for pyruvate1 Publication

    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

    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

    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)lysineBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti129 – 1291D → N in AAL24255. (PubMed:14593172)Curated
    Sequence conflicti129 – 1291D → N in AAO11559. (PubMed:14593172)Curated
    Sequence conflicti382 – 3821C → R in AAK25905. (PubMed:14593172)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei440 – 4412VF → RR in isoform 2. 1 PublicationVSP_042465
    Alternative sequencei442 – 48140Missing in isoform 2. 1 PublicationVSP_042466Add
    BLAST

    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

    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: October 1, 2014
    This is version 98 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