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 27-MAR-2024, entry version 140.
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.Q94AL9; -.
DR PaxDb; 3702-AT2G38400-2; -.
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 TAIR; AT2G38400; AGT3.
DR eggNOG; KOG1404; Eukaryota.
DR HOGENOM; CLU_016922_8_0_1; -.
DR InParanoid; Q94AL9; -.
DR OMA; FWGWQAH; -.
DR PhylomeDB; Q94AL9; -.
DR BioCyc; ARA:AT2G38400-MONOMER; -.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45688:SF13; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2 HOMOLOG 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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
//
