GenomeNet

Database: UniProt/SWISS-PROT
Entry: GGT2_ARATH
LinkDB: GGT2_ARATH
Original site: GGT2_ARATH 
ID   GGT2_ARATH              Reviewed;         481 AA.
AC   Q9S7E9; B9DH91; Q8LFE9;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   05-DEC-2018, entry version 128.
DE   RecName: Full=Glutamate--glyoxylate aminotransferase 2;
DE            Short=AtGGT2;
DE            EC=2.6.1.4;
DE   AltName: Full=Alanine aminotransferase GGT2;
DE            EC=2.6.1.2;
DE   AltName: Full=Alanine--glyoxylate aminotransferase GGT2;
DE            EC=2.6.1.44;
DE   AltName: Full=Alanine-2-oxoglutarate aminotransferase 2;
DE            EC=2.6.1.-;
GN   Name=GGAT2; Synonyms=AOAT2, GGT2; OrderedLocusNames=At1g70580;
GN   ORFNames=F24J13.15, F5A18.24;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=12529529; DOI=10.1104/pp.011460;
RA   Liepman A.H., Olsen L.J.;
RT   "Alanine aminotransferase homologs catalyze the glutamate:glyoxylate
RT   aminotransferase reaction in peroxisomes of Arabidopsis.";
RL   Plant Physiol. 131:215-227(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Root, and Rosette leaf;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
RA   Seki M., Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA   Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T.,
RA   Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT   "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel
RT   targeting peptides, metabolic pathways, and defense mechanisms.";
RL   Plant Cell 19:3170-3193(2007).
RN   [8]
RP   TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12631323; DOI=10.1046/j.1365-313X.2003.01688.x;
RA   Igarashi D., Miwa T., Seki M., Kobayashi M., Kato T., Tabata S.,
RA   Shinozaki K., Ohsumi C.;
RT   "Identification of photorespiratory glutamate:glyoxylate
RT   aminotransferase (GGAT) gene in Arabidopsis.";
RL   Plant J. 33:975-987(2003).
CC   -!- FUNCTION: Catalyzes the Glu:glyoxylate aminotransferase (GGT),
CC       Ala:glyoxylate aminotransferase (AGT), Ala:2-oxoglutarate
CC       aminotransferase (AKT) and Glu:pyruvate aminotransferase (GPT)
CC       reactions in peroxisomes. {ECO:0000269|PubMed:12529529}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC         Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC         Evidence={ECO:0000269|PubMed:12529529};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glyoxylate + L-alanine = glycine + pyruvate;
CC         Xref=Rhea:RHEA:24248, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:57972; EC=2.6.1.44;
CC         Evidence={ECO:0000269|PubMed:12529529};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + glycine = glyoxylate + L-glutamate;
CC         Xref=Rhea:RHEA:14089, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57305; EC=2.6.1.4;
CC         Evidence={ECO:0000269|PubMed:12529529};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.32 mM for glutamate {ECO:0000269|PubMed:12529529};
CC         KM=3.56 mM for alanine {ECO:0000269|PubMed:12529529};
CC         KM=0.14 mM for glyoxylate {ECO:0000269|PubMed:12529529};
CC         KM=0.51 mM for 2-oxoglutarate {ECO:0000269|PubMed:12529529};
CC         KM=0.36 mM for pyruvate {ECO:0000269|PubMed:12529529};
CC   -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via
CC       transaminase pathway; pyruvate from L-alanine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:12529529}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in seedlings, leaves,
CC       flowers, roots, and green siliques. {ECO:0000269|PubMed:12529529,
CC       ECO:0000269|PubMed:12631323}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000305}.
DR   EMBL; AF479640; AAN62333.1; -; mRNA.
DR   EMBL; AC010796; AAG52480.1; -; Genomic_DNA.
DR   EMBL; AC011663; AAG52344.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35082.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35083.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35084.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35085.1; -; Genomic_DNA.
DR   EMBL; AY035130; AAK59635.1; -; mRNA.
DR   EMBL; AY062982; AAL34156.1; -; mRNA.
DR   EMBL; AK316788; BAH19506.1; -; mRNA.
DR   EMBL; AK317441; BAH20108.1; -; mRNA.
DR   EMBL; AY084890; AAM61453.1; -; mRNA.
DR   PIR; H96729; H96729.
DR   RefSeq; NP_001031262.1; NM_001036185.1.
DR   RefSeq; NP_001031263.1; NM_001036186.2.
DR   RefSeq; NP_177215.1; NM_105726.3.
DR   RefSeq; NP_974122.1; NM_202393.2.
DR   UniGene; At.18115; -.
DR   ProteinModelPortal; Q9S7E9; -.
DR   SMR; Q9S7E9; -.
DR   BioGrid; 28615; 1.
DR   STRING; 3702.AT1G70580.1; -.
DR   iPTMnet; Q9S7E9; -.
DR   PaxDb; Q9S7E9; -.
DR   PRIDE; Q9S7E9; -.
DR   ProMEX; Q9S7E9; -.
DR   EnsemblPlants; AT1G70580.1; AT1G70580.1; AT1G70580.
DR   EnsemblPlants; AT1G70580.2; AT1G70580.2; AT1G70580.
DR   EnsemblPlants; AT1G70580.3; AT1G70580.3; AT1G70580.
DR   EnsemblPlants; AT1G70580.4; AT1G70580.4; AT1G70580.
DR   GeneID; 843395; -.
DR   Gramene; AT1G70580.1; AT1G70580.1; AT1G70580.
DR   Gramene; AT1G70580.2; AT1G70580.2; AT1G70580.
DR   Gramene; AT1G70580.3; AT1G70580.3; AT1G70580.
DR   Gramene; AT1G70580.4; AT1G70580.4; AT1G70580.
DR   KEGG; ath:AT1G70580; -.
DR   Araport; AT1G70580; -.
DR   TAIR; locus:2026841; AT1G70580.
DR   eggNOG; KOG0258; Eukaryota.
DR   eggNOG; COG0436; LUCA.
DR   HOGENOM; HOG000215020; -.
DR   InParanoid; Q9S7E9; -.
DR   KO; K14272; -.
DR   OMA; FHAKFTL; -.
DR   OrthoDB; EOG093607KI; -.
DR   PhylomeDB; Q9S7E9; -.
DR   BioCyc; MetaCyc:AT1G70580-MONOMER; -.
DR   BRENDA; 2.6.1.44; 399.
DR   Reactome; R-ATH-70614; Amino acid synthesis and interconversion (transamination).
DR   SABIO-RK; Q9S7E9; -.
DR   UniPathway; UPA00322; -.
DR   UniPathway; UPA00528; UER00586.
DR   PRO; PR:Q9S7E9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9S7E9; baseline and differential.
DR   Genevisible; Q9S7E9; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:TAIR.
DR   GO; GO:0047958; F:glycine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Complete proteome; Peroxisome; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN         1    481       Glutamate--glyoxylate aminotransferase 2.
FT                                /FTId=PRO_0000416041.
FT   MOTIF       479    481       Peroxisomal targeting signal.
FT   MOD_RES     291    291       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
FT   CONFLICT     37     37       G -> C (in Ref. 6; AAM61453).
FT                                {ECO:0000305}.
FT   CONFLICT    118    118       E -> D (in Ref. 6; AAM61453).
FT                                {ECO:0000305}.
FT   CONFLICT    318    318       Y -> H (in Ref. 5; BAH20108).
FT                                {ECO:0000305}.
SQ   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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