AGT23_ARATH
ID AGT23_ARATH Reviewed; 481 AA.
AC Q9SR86;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Alanine--glyoxylate aminotransferase 2 homolog 3, mitochondrial;
DE EC=2.6.1.44;
DE AltName: Full=Beta-alanine-pyruvate aminotransferase 3;
DE Flags: Precursor;
GN OrderedLocusNames=At3g08860; ORFNames=T16O11.21;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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 [4]
RP IDENTIFICATION.
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).
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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AC010871; AAF07846.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74688.1; -; Genomic_DNA.
DR EMBL; AY099816; AAM20667.1; -; mRNA.
DR RefSeq; NP_187498.1; NM_111720.4.
DR AlphaFoldDB; Q9SR86; -.
DR SMR; Q9SR86; -.
DR STRING; 3702.AT3G08860.1; -.
DR PaxDb; Q9SR86; -.
DR PRIDE; Q9SR86; -.
DR ProteomicsDB; 244835; -.
DR EnsemblPlants; AT3G08860.1; AT3G08860.1; AT3G08860.
DR GeneID; 820034; -.
DR Gramene; AT3G08860.1; AT3G08860.1; AT3G08860.
DR KEGG; ath:AT3G08860; -.
DR Araport; AT3G08860; -.
DR TAIR; locus:2097623; AT3G08860.
DR eggNOG; KOG1404; Eukaryota.
DR HOGENOM; CLU_016922_8_0_1; -.
DR InParanoid; Q9SR86; -.
DR OrthoDB; 145181at2759; -.
DR PhylomeDB; Q9SR86; -.
DR BioCyc; ARA:AT3G08860-MON; -.
DR BRENDA; 2.6.1.18; 399.
DR BRENDA; 2.6.1.44; 399.
DR PRO; PR:Q9SR86; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SR86; baseline and differential.
DR Genevisible; Q9SR86; 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:0043562; P:cellular response to nitrogen levels; IEP:TAIR.
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 2: Evidence at transcript level;
KW Aminotransferase; Mitochondrion; Photorespiration; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..481
FT /note="Alanine--glyoxylate aminotransferase 2 homolog 3,
FT mitochondrial"
FT /id="PRO_0000041947"
FT REGION 21..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 325
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 481 AA; 52461 MW; 31E78C568A84E60C CRC64;
MRKLTAVNSL LKRNNYLLPR HGSSQTAAQR TSSVRETETE TKLPKMPPFN YSPPPYDGPS
TAEIIAKRRE FLSPALFHFY NTPLNIVEAK MQYVFDENGR RYLDAFGGIA TVSCGHCHPE
VVNSVVKQLK LINHSTILYL NHTISDFAEA LVSTLPGDLK VVFFTNSGTE ANELAMMMAR
LYTGCNDIVS LRNSYHGNAA ATMGATAQSN WKFNVVQSGV HHAINPDPYR GIFGSDGEKY
ASDVHDLIQF GTSGQVAGFI GESIQGVGGI VELAPGYLPA AYDIVRKAGG VCIADEVQSG
FARTGTHFWG FQSHGVIPDI VTMAKGIGNG IPLGAVVTTP EIAGVLSRRS YFNTFGGNPM
CTAAGHAVLR VLHEEKLQEN ANLVGSHLKR RLTLLKNKYE LIGDVRGRGL MLGVEFVKDR
DLKTPAKAET LHLMDQMKEM GVLVGKGGFY GNVFRITPPL CFTLSDADFL VDVMDHAMSK
M
