Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutamate--glyoxylate aminotransferase 2

Gene

GGAT2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the Glu:glyoxylate aminotransferase (GGT), Ala:glyoxylate aminotransferase (AGT), Ala:2-oxoglutarate aminotransferase (AKT) and Glu:pyruvate aminotransferase (GPT) reactions in peroxisomes.1 Publication

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

Kineticsi

  1. KM=3.32 mM for glutamate1 Publication
  2. KM=3.56 mM for alanine1 Publication
  3. KM=0.14 mM for glyoxylate1 Publication
  4. KM=0.51 mM for 2-oxoglutarate1 Publication
  5. KM=0.36 mM for pyruvate1 Publication

    Pathway:iC4 acid pathway

    This protein is involved in the pathway C4 acid pathway, which is part of Photosynthesis.
    View all proteins of this organism that are known to be involved in the pathway C4 acid pathway and in Photosynthesis.

    Pathway:iL-alanine degradation via transaminase pathway

    This protein is involved in step 1 of the subpathway that synthesizes pyruvate from L-alanine.
    Proteins known to be involved in this subpathway in this organism are:
    1. Alanine aminotransferase 1, mitochondrial (ALAAT1), Alanine aminotransferase 2, mitochondrial (ALAAT2), Glutamate--glyoxylate aminotransferase 2 (GGAT2), Glutamate--glyoxylate aminotransferase 1 (GGAT1)
    This subpathway is part of the pathway L-alanine degradation via transaminase pathway, which is itself part of Amino-acid degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from L-alanine, the pathway L-alanine degradation via transaminase pathway and in Amino-acid degradation.

    GO - Molecular functioni

    • alanine-glyoxylate transaminase activity Source: TAIR
    • glycine:2-oxoglutarate aminotransferase activity Source: TAIR
    • L-alanine:2-oxoglutarate aminotransferase activity Source: TAIR
    • pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciARA:GQT-2823-MONOMER.
    ARA:GQT-2824-MONOMER.
    ARA:GQT-2825-MONOMER.
    MetaCyc:AT1G70580-MONOMER.
    BRENDAi2.6.1.44. 399.
    ReactomeiREACT_276185. Amino acid synthesis and interconversion (transamination).
    SABIO-RKQ9S7E9.
    UniPathwayiUPA00322.
    UPA00528; UER00586.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate--glyoxylate aminotransferase 2 (EC:2.6.1.4)
    Short name:
    AtGGT2
    Alternative name(s):
    Alanine aminotransferase GGT2 (EC:2.6.1.2)
    Alanine--glyoxylate aminotransferase GGT2 (EC:2.6.1.44)
    Alanine-2-oxoglutarate aminotransferase 2 (EC:2.6.1.-)
    Gene namesi
    Name:GGAT2
    Synonyms:AOAT2, GGT2
    Ordered Locus Names:At1g70580
    ORF Names:F24J13.15, F5A18.24
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 1

    Organism-specific databases

    TAIRiAT1G70580.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: TAIR
    • chloroplast stroma Source: TAIR
    • peroxisome Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 481481Glutamate--glyoxylate aminotransferase 2PRO_0000416041Add
    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

    PRIDEiQ9S7E9.
    ProMEXiQ9S7E9.

    Expressioni

    Tissue specificityi

    Expressed at low levels in seedlings, leaves, flowers, roots, and green siliques.2 Publications

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi28615. 1 interaction.
    STRINGi3702.AT1G70580.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9S7E9.
    SMRiQ9S7E9. Positions 9-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

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

    Sequence similaritiesi

    Phylogenomic databases

    HOGENOMiHOG000215020.
    InParanoidiQ9S7E9.
    KOiK14272.
    OMAiEESENWG.
    PhylomeDBiQ9S7E9.

    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.

    Sequencei

    Sequence statusi: Complete.

    Q9S7E9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSLKALDYES LNENVKNCQY AVRGELYLRA SELQKEGKKI IFTNVGNPHA
    60 70 80 90 100
    LGQKPLTFPR QVVSLCQAPF LLDDPNVGMI FPADAIARAK HYLSLTSGGL
    110 120 130 140 150
    GAYSDSRGLP GVRKEVAEFI ERRDGYPSDP ELIFLTDGAS KGVMQILNCV
    160 170 180 190 200
    IRGQKDGILV PVPQYPLYSA TISLLGGTLV PYYLEESENW GLDVNNLRQS
    210 220 230 240 250
    VAQARSQGIT VRAMVIINPG NPTGQCLSEA NIREILRFCC DERLVLLGDE
    260 270 280 290 300
    VYQQNIYQDE RPFISSKKVL MDMGAPISKE VQLISFHTVS KGYWGECGQR
    310 320 330 340 350
    GGYFEMTNIP PRTVEEIYKV ASIALSPNVS AQIFMGLMVS PPKPGDISYD
    360 370 380 390 400
    QFVRESKGIL ESLRRRARMM TDGFNSCKNV VCNFTEGAMY SFPQIKLPSK
    410 420 430 440 450
    AIQAAKQAGK VPDVFYCLKL LEATGISTVP GSGFGQKEGV FHLRTTILPA
    460 470 480
    EEEMPEIMDS FKKFNDEFMS QYADNFGYSR M
    Length:481
    Mass (Da):53,444
    Last modified:May 1, 2000 - v1
    Checksum:iA00D1D49157021FA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371G → C in AAM61453 (Ref. 6) Curated
    Sequence conflicti118 – 1181E → D in AAM61453 (Ref. 6) Curated
    Sequence conflicti318 – 3181Y → H in BAH20108 (PubMed:19423640).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF479640 mRNA. Translation: AAN62333.1.
    AC010796 Genomic DNA. Translation: AAG52480.1.
    AC011663 Genomic DNA. Translation: AAG52344.1.
    CP002684 Genomic DNA. Translation: AEE35082.1.
    CP002684 Genomic DNA. Translation: AEE35083.1.
    CP002684 Genomic DNA. Translation: AEE35084.1.
    CP002684 Genomic DNA. Translation: AEE35085.1.
    AY035130 mRNA. Translation: AAK59635.1.
    AY062982 mRNA. Translation: AAL34156.1.
    AK316788 mRNA. Translation: BAH19506.1.
    AK317441 mRNA. Translation: BAH20108.1.
    AY084890 mRNA. Translation: AAM61453.1.
    PIRiH96729.
    RefSeqiNP_001031262.1. NM_001036185.1.
    NP_001031263.1. NM_001036186.1.
    NP_177215.1. NM_105726.2.
    NP_974122.1. NM_202393.1.
    UniGeneiAt.18115.

    Genome annotation databases

    EnsemblPlantsiAT1G70580.1; AT1G70580.1; AT1G70580.
    AT1G70580.2; AT1G70580.2; AT1G70580.
    AT1G70580.3; AT1G70580.3; AT1G70580.
    AT1G70580.4; AT1G70580.4; AT1G70580.
    GeneIDi843395.
    KEGGiath:AT1G70580.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF479640 mRNA. Translation: AAN62333.1.
    AC010796 Genomic DNA. Translation: AAG52480.1.
    AC011663 Genomic DNA. Translation: AAG52344.1.
    CP002684 Genomic DNA. Translation: AEE35082.1.
    CP002684 Genomic DNA. Translation: AEE35083.1.
    CP002684 Genomic DNA. Translation: AEE35084.1.
    CP002684 Genomic DNA. Translation: AEE35085.1.
    AY035130 mRNA. Translation: AAK59635.1.
    AY062982 mRNA. Translation: AAL34156.1.
    AK316788 mRNA. Translation: BAH19506.1.
    AK317441 mRNA. Translation: BAH20108.1.
    AY084890 mRNA. Translation: AAM61453.1.
    PIRiH96729.
    RefSeqiNP_001031262.1. NM_001036185.1.
    NP_001031263.1. NM_001036186.1.
    NP_177215.1. NM_105726.2.
    NP_974122.1. NM_202393.1.
    UniGeneiAt.18115.

    3D structure databases

    ProteinModelPortaliQ9S7E9.
    SMRiQ9S7E9. Positions 9-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi28615. 1 interaction.
    STRINGi3702.AT1G70580.1.

    Proteomic databases

    PRIDEiQ9S7E9.
    ProMEXiQ9S7E9.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT1G70580.1; AT1G70580.1; AT1G70580.
    AT1G70580.2; AT1G70580.2; AT1G70580.
    AT1G70580.3; AT1G70580.3; AT1G70580.
    AT1G70580.4; AT1G70580.4; AT1G70580.
    GeneIDi843395.
    KEGGiath:AT1G70580.

    Organism-specific databases

    TAIRiAT1G70580.

    Phylogenomic databases

    HOGENOMiHOG000215020.
    InParanoidiQ9S7E9.
    KOiK14272.
    OMAiEESENWG.
    PhylomeDBiQ9S7E9.

    Enzyme and pathway databases

    UniPathwayiUPA00322.
    UPA00528; UER00586.
    BioCyciARA:GQT-2823-MONOMER.
    ARA:GQT-2824-MONOMER.
    ARA:GQT-2825-MONOMER.
    MetaCyc:AT1G70580-MONOMER.
    BRENDAi2.6.1.44. 399.
    ReactomeiREACT_276185. Amino acid synthesis and interconversion (transamination).
    SABIO-RKQ9S7E9.

    Miscellaneous databases

    PROiQ9S7E9.

    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.
    ProtoNetiSearch...

    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], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    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].
      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].
      Strain: cv. Columbia.
      Tissue: Root and Rosette leaf.
    6. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "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].
    8. "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].
    9. "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: TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.

    Entry informationi

    Entry nameiGGT2_ARATH
    AccessioniPrimary (citable) accession number: Q9S7E9
    Secondary accession number(s): B9DH91, Q8LFE9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2012
    Last sequence update: May 1, 2000
    Last modified: July 22, 2015
    This is version 110 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.