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Q9S7E9 (GGT2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate--glyoxylate aminotransferase 2

Short name=AtGGT2
EC=2.6.1.4
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 names
Name:GGAT2
Synonyms:AOAT2, GGT2
Ordered Locus Names:At1g70580
ORF Names:F24J13.15, F5A18.24
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 Glu:glyoxylate aminotransferase (GGT), Ala:glyoxylate aminotransferase (AGT), Ala:2-oxoglutarate aminotransferase (AKT) and Glu:pyruvate aminotransferase (GPT) reactions in peroxisomes. Ref.1

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

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.7 Ref.8.

Tissue specificity

Expressed at low levels in seedlings, leaves, flowers, roots, and green siliques. Ref.1 Ref.9

Post-translational modification

The N-terminus is blocked By similarity.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=3.32 mM for glutamate Ref.1

KM=3.56 mM for alanine

KM=0.14 mM for glyoxylate

KM=0.51 mM for 2-oxoglutarate

KM=0.36 mM for pyruvate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 481481Glutamate--glyoxylate aminotransferase 2
PRO_0000416041

Regions

Motif479 – 4813Peroxisomal targeting signal

Amino acid modifications

Modified residue2911N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict371G → C in AAM61453. Ref.6
Sequence conflict1181E → D in AAM61453. Ref.6
Sequence conflict3181Y → H in BAH20108. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9S7E9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: A00D1D49157021FA

FASTA48153,444
        10         20         30         40         50         60 
MSLKALDYES LNENVKNCQY AVRGELYLRA SELQKEGKKI IFTNVGNPHA LGQKPLTFPR 

        70         80         90        100        110        120 
QVVSLCQAPF LLDDPNVGMI FPADAIARAK HYLSLTSGGL GAYSDSRGLP GVRKEVAEFI 

       130        140        150        160        170        180 
ERRDGYPSDP ELIFLTDGAS KGVMQILNCV IRGQKDGILV PVPQYPLYSA TISLLGGTLV 

       190        200        210        220        230        240 
PYYLEESENW GLDVNNLRQS VAQARSQGIT VRAMVIINPG NPTGQCLSEA NIREILRFCC 

       250        260        270        280        290        300 
DERLVLLGDE VYQQNIYQDE RPFISSKKVL MDMGAPISKE VQLISFHTVS KGYWGECGQR 

       310        320        330        340        350        360 
GGYFEMTNIP PRTVEEIYKV ASIALSPNVS AQIFMGLMVS PPKPGDISYD QFVRESKGIL 

       370        380        390        400        410        420 
ESLRRRARMM TDGFNSCKNV VCNFTEGAMY SFPQIKLPSK AIQAAKQAGK VPDVFYCLKL 

       430        440        450        460        470        480 
LEATGISTVP GSGFGQKEGV FHLRTTILPA EEEMPEIMDS FKKFNDEFMS QYADNFGYSR 


M 

« Hide

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], 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. 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].
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRH96729.
RefSeqNP_001031262.1. NM_001036185.1.
NP_001031263.1. NM_001036186.1.
NP_177215.1. NM_105726.2.
NP_974122.1. NM_202393.1.
UniGeneAt.18115.

3D structure databases

ProteinModelPortalQ9S7E9.
SMRQ9S7E9. Positions 9-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G70580.3-P.

Proteomic databases

PRIDEQ9S7E9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G70580.1; AT1G70580.1; AT1G70580.
AT1G70580.2; AT1G70580.2; AT1G70580.
AT1G70580.3; AT1G70580.3; AT1G70580.
AT1G70580.4; AT1G70580.4; AT1G70580.
GeneID843395.
KEGGath:AT1G70580.

Organism-specific databases

TAIRAT1G70580.

Phylogenomic databases

HOGENOMHOG000215020.
InParanoidQ9S7E9.
KOK14272.
OMAEDMPAIM.
PhylomeDBQ9S7E9.
ProtClustDBPLN02368.

Enzyme and pathway databases

BioCycARA:GQT-2823-MONOMER.
ARA:GQT-2824-MONOMER.
ARA:GQT-2825-MONOMER.
MetaCyc:AT1G70580-MONOMER.
BRENDA2.6.1.44. 302.
SABIO-RKQ9S7E9.
UniPathwayUPA00322.
UPA00528; UER00586.

Gene expression databases

GenevestigatorQ9S7E9.

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 nameGGT2_ARATH
AccessionPrimary (citable) accession number: Q9S7E9
Secondary accession number(s): B9DH91, Q8LFE9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 102 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