ID   AGT22_ARATH             Reviewed;         477 AA.
AC   Q94AL9; O80911;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Alanine--glyoxylate aminotransferase 2 homolog 2, mitochondrial;
DE            EC=2.6.1.44;
DE   AltName: Full=Beta-alanine-pyruvate aminotransferase 2;
DE   Flags: Precursor;
GN   Name=AGT3; OrderedLocusNames=At2g38400; ORFNames=T19C21.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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 reference
RT   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., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   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].
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   [6]
RP   INTERACTION WITH GRF3.
RX   PubMed=21094157; DOI=10.1016/j.febslet.2010.11.025;
RA   Shin R., Jez J.M., Basra A., Zhang B., Schachtman D.P.;
RT   "14-3-3 proteins fine-tune plant nutrient metabolism.";
RL   FEBS Lett. 585:143-147(2011).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP   ILE-22.
RX   PubMed=25732537; DOI=10.1093/jxb/erv064;
RA   Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT   "Identification of cleavage sites and substrate proteins for two
RT   mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL   J. Exp. Bot. 66:2691-2708(2015).
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q9APM5};
CC   -!- SUBUNIT: Homotetramer (By similarity). Interacts with GRF3.
CC       {ECO:0000250|UniProtKB:Q9APM5, ECO:0000269|PubMed:21094157}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:25732537}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q94AL9-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AF166352; AAD48838.1; -; mRNA.
DR   EMBL; AC004683; AAC28764.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09532.1; -; Genomic_DNA.
DR   EMBL; AY045941; AAK76615.1; -; mRNA.
DR   EMBL; BT001918; AAN71917.1; -; mRNA.
DR   EMBL; AY085348; AAM62579.1; -; mRNA.
DR   PIR; T02505; T02505.
DR   RefSeq; NP_181374.1; NM_129396.4. [Q94AL9-1]
DR   AlphaFoldDB; Q94AL9; -.
DR   SMR; Q94AL9; -.
DR   BioGRID; 3763; 3.
DR   STRING; 3702.AT2G38400.2; -.
DR   PaxDb; Q94AL9; -.
DR   PRIDE; Q94AL9; -.
DR   ProteomicsDB; 245032; -. [Q94AL9-1]
DR   EnsemblPlants; AT2G38400.1; AT2G38400.1; AT2G38400. [Q94AL9-1]
DR   GeneID; 818421; -.
DR   Gramene; AT2G38400.1; AT2G38400.1; AT2G38400. [Q94AL9-1]
DR   KEGG; ath:AT2G38400; -.
DR   Araport; AT2G38400; -.
DR   eggNOG; KOG1404; Eukaryota.
DR   HOGENOM; CLU_016922_8_0_1; -.
DR   InParanoid; Q94AL9; -.
DR   OMA; PSVGHCH; -.
DR   PhylomeDB; Q94AL9; -.
DR   BioCyc; ARA:AT2G38400-MON; -.
DR   PRO; PR:Q94AL9; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q94AL9; baseline and differential.
DR   Genevisible; Q94AL9; AT.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Aminotransferase; Mitochondrion; Photorespiration;
KW   Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..22
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:25732537"
FT   CHAIN           23..477
FT                   /note="Alanine--glyoxylate aminotransferase 2 homolog 2,
FT                   mitochondrial"
FT                   /id="PRO_0000041946"
FT   BINDING         165..166
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P22256"
FT   BINDING         192
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P22256"
FT   BINDING         292..295
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P22256"
FT   BINDING         350
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P22256"
FT   MOD_RES         321
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P22256"
FT   CONFLICT        461
FT                   /note="D -> G (in Ref. 4; AAK76615)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   477 AA;  51912 MW;  FE52ACFAAAA25FCC CRC64;
     MQRFAAKRSV QNISVSLWRR CISSTSQAAT ASVKDSDEFQ ARLPPFAYTP PPYTGPSADV
     ILSKRKEFLS PSMFCLYRKP LNIVDGKMQY LFDESGRRYL DAFAGIAVVN CGHCHPDVVE
     PVINQIKRLQ HPTVLYLNHA IADFSEALAS KLPGDLKVVF FTNSGTEANE LALMMAKLYT
     GCQDIVAVRN GYHGNAAATM GATGQSMWKF NVVQNSVHHA LNPDPYRGVF GSDGEKYAKD
     LQDLIQYGTT GHIAGFICEA IQGVGGIVEL APGYLSAAYD TVKKAGGLFI ADEVQSGFAR
     TGNFWGFEAH NVVPDIVTMA KGIGNGFPLG AVVTTPEIAG VLTRRSYFNT FGGNSVSTTA
     GLAVLNVIEK EKLQENAAMV GSYLKEKLTQ LKEKHEIIGD VRGRGLMLGV ELVSDRKLKT
     PATAETLHIM DQMKELGVLI GKGGYFGNVF RITPPLCFTK DDADFLVEAM DYSMSKM