Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9S7E9

- GGT2_ARATH

UniProt

Q9S7E9 - GGT2_ARATH

Protein

Glutamate--glyoxylate aminotransferase 2

Gene

GGAT2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Pyridoxal phosphate.By similarity

    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

    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. biosynthetic process Source: InterPro
    2. L-alanine catabolic process Source: UniProtKB-UniPathway

    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. 302.
    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: Chromosome 1

    Organism-specific databases

    TAIRiAT1G70580.

    Subcellular locationi

    Peroxisome 3 Publications

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. chloroplast stroma Source: TAIR
    3. peroxisome Source: TAIR

    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.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    GenevestigatoriQ9S7E9.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi3702.AT1G70580.3-P.

    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.
    OMAiLNEEKCW.
    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

    MSLKALDYES LNENVKNCQY AVRGELYLRA SELQKEGKKI IFTNVGNPHA    50
    LGQKPLTFPR QVVSLCQAPF LLDDPNVGMI FPADAIARAK HYLSLTSGGL 100
    GAYSDSRGLP GVRKEVAEFI ERRDGYPSDP ELIFLTDGAS KGVMQILNCV 150
    IRGQKDGILV PVPQYPLYSA TISLLGGTLV PYYLEESENW GLDVNNLRQS 200
    VAQARSQGIT VRAMVIINPG NPTGQCLSEA NIREILRFCC DERLVLLGDE 250
    VYQQNIYQDE RPFISSKKVL MDMGAPISKE VQLISFHTVS KGYWGECGQR 300
    GGYFEMTNIP PRTVEEIYKV ASIALSPNVS AQIFMGLMVS PPKPGDISYD 350
    QFVRESKGIL ESLRRRARMM TDGFNSCKNV VCNFTEGAMY SFPQIKLPSK 400
    AIQAAKQAGK VPDVFYCLKL LEATGISTVP GSGFGQKEGV FHLRTTILPA 450
    EEEMPEIMDS FKKFNDEFMS QYADNFGYSR M 481
    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. 1 PublicationCurated
    Sequence conflicti118 – 1181E → D in AAM61453. 1 PublicationCurated
    Sequence conflicti318 – 3181Y → H in BAH20108. (PubMed:19423640)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi H96729.
    RefSeqi NP_001031262.1. NM_001036185.1.
    NP_001031263.1. NM_001036186.1.
    NP_177215.1. NM_105726.2.
    NP_974122.1. NM_202393.1.
    UniGenei At.18115.

    3D structure databases

    ProteinModelPortali Q9S7E9.
    SMRi Q9S7E9. Positions 9-472.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT1G70580.3-P.

    Proteomic databases

    PRIDEi Q9S7E9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G70580.1 ; AT1G70580.1 ; AT1G70580 .
    AT1G70580.2 ; AT1G70580.2 ; AT1G70580 .
    AT1G70580.3 ; AT1G70580.3 ; AT1G70580 .
    AT1G70580.4 ; AT1G70580.4 ; AT1G70580 .
    GeneIDi 843395.
    KEGGi ath:AT1G70580.

    Organism-specific databases

    TAIRi AT1G70580.

    Phylogenomic databases

    HOGENOMi HOG000215020.
    InParanoidi Q9S7E9.
    KOi K14272.
    OMAi LNEEKCW.
    PhylomeDBi Q9S7E9.

    Enzyme and pathway databases

    UniPathwayi UPA00322 .
    UPA00528 ; UER00586 .
    BioCyci ARA:GQT-2823-MONOMER.
    ARA:GQT-2824-MONOMER.
    ARA:GQT-2825-MONOMER.
    MetaCyc:AT1G70580-MONOMER.
    BRENDAi 2.6.1.44. 302.
    SABIO-RK Q9S7E9.

    Gene expression databases

    Genevestigatori Q9S7E9.

    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], 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: October 1, 2014
    This is version 104 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