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Glutamate--glyoxylate aminotransferase 2 (AtGGT2) (EC 2.6.1.4) (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.-)

 GGT2_ARATH              Reviewed;         481 AA.
Q9S7E9; B9DH91; Q8LFE9;
21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 123.
RecName: Full=Glutamate--glyoxylate aminotransferase 2;
Short=AtGGT2;
EC=2.6.1.4;
AltName: Full=Alanine aminotransferase GGT2;
EC=2.6.1.2;
AltName: Full=Alanine--glyoxylate aminotransferase GGT2;
EC=2.6.1.44;
AltName: Full=Alanine-2-oxoglutarate aminotransferase 2;
EC=2.6.1.-;
Name=GGAT2; Synonyms=AOAT2, GGT2; OrderedLocusNames=At1g70580;
ORFNames=F24J13.15, F5A18.24;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12529529; DOI=10.1104/pp.011460;
Liepman A.H., Olsen L.J.;
"Alanine aminotransferase homologs catalyze the glutamate:glyoxylate
aminotransferase reaction in peroxisomes of Arabidopsis.";
Plant Physiol. 131:215-227(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
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.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia; TISSUE=Root, and Rosette leaf;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17951448; DOI=10.1105/tpc.107.050989;
Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T.,
Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.;
"Proteome analysis of Arabidopsis leaf peroxisomes reveals novel
targeting peptides, metabolic pathways, and defense mechanisms.";
Plant Cell 19:3170-3193(2007).
[8]
TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
PubMed=12631323; DOI=10.1046/j.1365-313X.2003.01688.x;
Igarashi D., Miwa T., Seki M., Kobayashi M., Kato T., Tabata S.,
Shinozaki K., Ohsumi C.;
"Identification of photorespiratory glutamate:glyoxylate
aminotransferase (GGAT) gene in Arabidopsis.";
Plant J. 33:975-987(2003).
-!- FUNCTION: Catalyzes the Glu:glyoxylate aminotransferase (GGT),
Ala:glyoxylate aminotransferase (AGT), Ala:2-oxoglutarate
aminotransferase (AKT) and Glu:pyruvate aminotransferase (GPT)
reactions in peroxisomes. {ECO:0000269|PubMed:12529529}.
-!- CATALYTIC ACTIVITY: L-alanine + 2-oxoglutarate = pyruvate + L-
glutamate. {ECO:0000269|PubMed:12529529}.
-!- CATALYTIC ACTIVITY: L-alanine + glyoxylate = pyruvate + glycine.
{ECO:0000269|PubMed:12529529}.
-!- CATALYTIC ACTIVITY: Glycine + 2-oxoglutarate = glyoxylate + L-
glutamate. {ECO:0000269|PubMed:12529529}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.32 mM for glutamate {ECO:0000269|PubMed:12529529};
KM=3.56 mM for alanine {ECO:0000269|PubMed:12529529};
KM=0.14 mM for glyoxylate {ECO:0000269|PubMed:12529529};
KM=0.51 mM for 2-oxoglutarate {ECO:0000269|PubMed:12529529};
KM=0.36 mM for pyruvate {ECO:0000269|PubMed:12529529};
-!- PATHWAY: Photosynthesis; C4 acid pathway.
-!- PATHWAY: Amino-acid degradation; L-alanine degradation via
transaminase pathway; pyruvate from L-alanine: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:12529529}.
-!- TISSUE SPECIFICITY: Expressed at low levels in seedlings, leaves,
flowers, roots, and green siliques. {ECO:0000269|PubMed:12529529,
ECO:0000269|PubMed:12631323}.
-!- PTM: The N-terminus is blocked. {ECO:0000250}.
-!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
aminotransferase family. Alanine aminotransferase subfamily.
{ECO:0000305}.
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EMBL; AF479640; AAN62333.1; -; mRNA.
EMBL; AC010796; AAG52480.1; -; Genomic_DNA.
EMBL; AC011663; AAG52344.1; -; Genomic_DNA.
EMBL; CP002684; AEE35082.1; -; Genomic_DNA.
EMBL; CP002684; AEE35083.1; -; Genomic_DNA.
EMBL; CP002684; AEE35084.1; -; Genomic_DNA.
EMBL; CP002684; AEE35085.1; -; Genomic_DNA.
EMBL; AY035130; AAK59635.1; -; mRNA.
EMBL; AY062982; AAL34156.1; -; mRNA.
EMBL; AK316788; BAH19506.1; -; mRNA.
EMBL; AK317441; BAH20108.1; -; mRNA.
EMBL; AY084890; AAM61453.1; -; mRNA.
PIR; H96729; H96729.
RefSeq; NP_001031262.1; NM_001036185.1.
RefSeq; NP_001031263.1; NM_001036186.2.
RefSeq; NP_177215.1; NM_105726.3.
RefSeq; NP_974122.1; NM_202393.2.
UniGene; At.18115; -.
ProteinModelPortal; Q9S7E9; -.
SMR; Q9S7E9; -.
BioGrid; 28615; 1.
STRING; 3702.AT1G70580.1; -.
iPTMnet; Q9S7E9; -.
PaxDb; Q9S7E9; -.
PRIDE; Q9S7E9; -.
ProMEX; Q9S7E9; -.
EnsemblPlants; AT1G70580.1; AT1G70580.1; AT1G70580.
EnsemblPlants; AT1G70580.2; AT1G70580.2; AT1G70580.
EnsemblPlants; AT1G70580.3; AT1G70580.3; AT1G70580.
EnsemblPlants; AT1G70580.4; AT1G70580.4; AT1G70580.
GeneID; 843395; -.
Gramene; AT1G70580.1; AT1G70580.1; AT1G70580.
Gramene; AT1G70580.2; AT1G70580.2; AT1G70580.
Gramene; AT1G70580.3; AT1G70580.3; AT1G70580.
Gramene; AT1G70580.4; AT1G70580.4; AT1G70580.
KEGG; ath:AT1G70580; -.
Araport; AT1G70580; -.
TAIR; locus:2026841; AT1G70580.
eggNOG; KOG0258; Eukaryota.
eggNOG; COG0436; LUCA.
HOGENOM; HOG000215020; -.
InParanoid; Q9S7E9; -.
KO; K14272; -.
OMA; LNEEKCW; -.
OrthoDB; EOG093607KI; -.
PhylomeDB; Q9S7E9; -.
BioCyc; MetaCyc:AT1G70580-MONOMER; -.
BRENDA; 2.6.1.44; 399.
Reactome; R-ATH-70614; Amino acid synthesis and interconversion (transamination).
SABIO-RK; Q9S7E9; -.
UniPathway; UPA00322; -.
UniPathway; UPA00528; UER00586.
PRO; PR:Q9S7E9; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9S7E9; baseline and differential.
Genevisible; Q9S7E9; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:TAIR.
GO; GO:0047958; F:glycine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
Pfam; PF00155; Aminotran_1_2; 1.
SUPFAM; SSF53383; SSF53383; 1.
1: Evidence at protein level;
Aminotransferase; Complete proteome; Peroxisome; Pyridoxal phosphate;
Reference proteome; Transferase.
CHAIN 1 481 Glutamate--glyoxylate aminotransferase 2.
/FTId=PRO_0000416041.
MOTIF 479 481 Peroxisomal targeting signal.
MOD_RES 291 291 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
CONFLICT 37 37 G -> C (in Ref. 6; AAM61453).
{ECO:0000305}.
CONFLICT 118 118 E -> D (in Ref. 6; AAM61453).
{ECO:0000305}.
CONFLICT 318 318 Y -> H (in Ref. 5; BAH20108).
{ECO:0000305}.
SEQUENCE 481 AA; 53444 MW; A00D1D49157021FA CRC64;
MSLKALDYES LNENVKNCQY AVRGELYLRA SELQKEGKKI IFTNVGNPHA LGQKPLTFPR
QVVSLCQAPF LLDDPNVGMI FPADAIARAK HYLSLTSGGL GAYSDSRGLP GVRKEVAEFI
ERRDGYPSDP ELIFLTDGAS KGVMQILNCV IRGQKDGILV PVPQYPLYSA TISLLGGTLV
PYYLEESENW GLDVNNLRQS VAQARSQGIT VRAMVIINPG NPTGQCLSEA NIREILRFCC
DERLVLLGDE VYQQNIYQDE RPFISSKKVL MDMGAPISKE VQLISFHTVS KGYWGECGQR
GGYFEMTNIP PRTVEEIYKV ASIALSPNVS AQIFMGLMVS PPKPGDISYD QFVRESKGIL
ESLRRRARMM TDGFNSCKNV VCNFTEGAMY SFPQIKLPSK AIQAAKQAGK VPDVFYCLKL
LEATGISTVP GSGFGQKEGV FHLRTTILPA EEEMPEIMDS FKKFNDEFMS QYADNFGYSR
M


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