Glutamate--glyoxylate aminotransferase 2 - Arabidopsis thaliana (Mouse-ear cress)

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Q9S7E9 (GGT2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Protein existence	Evidence 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: K_M=3.32 mM for glutamate Ref.1 K_M=3.56 mM for alanine K_M=0.14 mM for glyoxylate K_M=0.51 mM for 2-oxoglutarate K_M=0.36 mM for pyruvate

Ontologies

Keywords
Cellular component	Peroxisome
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	L-alanine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	chloroplast stroma Inferred from direct assay PubMed 18633119. Source: TAIR peroxisome Inferred from direct assay Ref.8 Ref.7. Source: TAIR
Molecular_function	L-alanine:2-oxoglutarate aminotransferase activity Inferred from direct assay Ref.1. Source: TAIR alanine-glyoxylate transaminase activity Inferred from direct assay Ref.1. Source: TAIR glycine:2-oxoglutarate aminotransferase activity Inferred from direct assay Ref.1. Source: TAIR pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 481

481

Glutamate--glyoxylate aminotransferase 2

PRO_0000416041

Regions

Motif

479 – 481

Peroxisomal targeting signal

Amino acid modifications

Modified residue

291

N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict

G → C in AAM61453. Ref.6

Sequence conflict

118

E → D in AAM61453. Ref.6

Sequence conflict

318

Y → H in BAH20108. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

Q9S7E9 [UniParc].

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

481

53,444

        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

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References

	« Hide 'large scale' referencesShow '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. 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. 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], IDENTIFICATION BY MASS SPECTROMETRY [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], IDENTIFICATION BY MASS SPECTROMETRY [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.
IPI	IPI00539634.
PIR	H96729.
RefSeq	NP_001031262.1. NM_001036185.1. NP_001031263.1. NM_001036186.1. NP_177215.1. NM_105726.2. NP_974122.1. NM_202393.1.
UniGene	At.18115.
3D structure databases
ProteinModelPortal	Q9S7E9.
SMR	Q9S7E9. Positions 9-472.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT1G70580.3-P.
Proteomic databases
PRIDE	Q9S7E9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G70580.1; AT1G70580.1; AT1G70580. AT1G70580.2; AT1G70580.2; AT1G70580. AT1G70580.3; AT1G70580.3; AT1G70580. AT1G70580.4; AT1G70580.4; AT1G70580.
GeneID	843395.
KEGG	ath:AT1G70580.
Organism-specific databases
TAIR	At1g70580.
Phylogenomic databases
HOGENOM	HOG000215020.
InParanoid	Q9S7E9.
KO	K14272.
OMA	IFPADAI.
PhylomeDB	Q9S7E9.
ProtClustDB	PLN02368.
Enzyme and pathway databases
BioCyc	MetaCyc:AT1G70580-MONOMER.
BRENDA	2.6.1.44. 302.
SABIO-RK	Q9S7E9.
UniPathway	UPA00322. UPA00528; UER00586.
Gene expression databases
ArrayExpress	Q9S7E9.
Genevestigator	Q9S7E9.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GGT2_ARATH

Accession

Primary (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:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents