AAT3_ARATH
ID AAT3_ARATH Reviewed; 449 AA.
AC P46644; Q9CAZ5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Aspartate aminotransferase 3, chloroplastic;
DE EC=2.6.1.1;
DE AltName: Full=Protein YELLOW-LEAF-SPECIFIC GENE 4;
DE AltName: Full=Transaminase A;
DE Flags: Precursor;
GN Name=ASP3; Synonyms=YLS4; OrderedLocusNames=At5g11520; ORFNames=F15N18.110;
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], AND FUNCTION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7894512; DOI=10.1046/j.1365-313x.1995.07010061.x;
RA Schultz C.J., Coruzzi G.M.;
RT "The aspartate aminotransferase gene family of Arabidopsis encodes
RT isoenzymes localized to three distinct subcellular compartments.";
RL Plant J. 7:61-75(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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 [MRNA] OF 177-282, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RX PubMed=11230571; DOI=10.1093/pcp/pce021;
RA Yoshida S., Ito M., Nishida I., Watanabe A.;
RT "Isolation and RNA gel blot analysis of genes that could serve as potential
RT molecular markers for leaf senescence in Arabidopsis thaliana.";
RL Plant Cell Physiol. 42:170-178(2001).
RN [6]
RP FUNCTION.
RX PubMed=9611168; DOI=10.1093/genetics/149.2.491;
RA Schultz C.J., Hsu M., Miesak B., Coruzzi G.M.;
RT "Arabidopsis mutants define an in vivo role for isoenzymes of aspartate
RT aminotransferase in plant nitrogen assimilation.";
RL Genetics 149:491-499(1998).
RN [7]
RP TISSUE SPECIFICITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=14754918; DOI=10.1093/jxb/erh062;
RA Kwok E.Y., Hanson M.R.;
RT "GFP-labelled Rubisco and aspartate aminotransferase are present in plastid
RT stromules and traffic between plastids.";
RL J. Exp. Bot. 55:595-604(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [9]
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., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18318836; DOI=10.1111/j.1742-4658.2008.06279.x;
RA Funakoshi M., Sekine M., Katane M., Furuchi T., Yohda M., Yoshikawa T.,
RA Homma H.;
RT "Cloning and functional characterization of Arabidopsis thaliana D-amino
RT acid aminotransferase--D-aspartate behavior during germination.";
RL FEBS J. 275:1188-1200(2008).
CC -!- FUNCTION: Amino acid aminotransferase important for the metabolism of
CC amino acids and Krebs-cycle related organic acids. No activity with D-
CC Asp or D-Ala as amino donors. In plants, it is involved in nitrogen
CC metabolism and in aspects of carbon and energy metabolism.
CC {ECO:0000269|PubMed:18318836, ECO:0000269|PubMed:7894512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC Evidence={ECO:0000269|PubMed:18318836, ECO:0000269|PubMed:9611168};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 mM for L-aspartate {ECO:0000269|PubMed:18318836};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14754918}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:14754918}. Note=accumulates in stromules, which are
CC membrane-bound protrusions of the plastid envelope containing soluble
CC stroma. Stromules are often found connecting plastids within a cell.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cauline leaves, flowers,
CC hypocotyl epidermis and root hair cells. {ECO:0000269|PubMed:11230571,
CC ECO:0000269|PubMed:14754918}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in leaves during natural senescence.
CC {ECO:0000269|PubMed:11230571}.
CC -!- INDUCTION: By ethylene and dark. {ECO:0000269|PubMed:11230571}.
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC chloroplastic isozymes.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; U15034; AAA79371.1; -; mRNA.
DR EMBL; AL163815; CAB87712.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91691.1; -; Genomic_DNA.
DR EMBL; AY050765; AAK92700.1; -; mRNA.
DR EMBL; AY079310; AAL85041.1; -; mRNA.
DR EMBL; AB047807; BAB32884.1; -; mRNA.
DR PIR; T48511; T48511.
DR RefSeq; NP_196713.1; NM_121190.3.
DR AlphaFoldDB; P46644; -.
DR SMR; P46644; -.
DR BioGRID; 16302; 10.
DR IntAct; P46644; 1.
DR STRING; 3702.AT5G11520.1; -.
DR PaxDb; P46644; -.
DR PRIDE; P46644; -.
DR ProteomicsDB; 244522; -.
DR EnsemblPlants; AT5G11520.1; AT5G11520.1; AT5G11520.
DR GeneID; 831024; -.
DR Gramene; AT5G11520.1; AT5G11520.1; AT5G11520.
DR KEGG; ath:AT5G11520; -.
DR Araport; AT5G11520; -.
DR TAIR; locus:2144226; AT5G11520.
DR eggNOG; KOG1411; Eukaryota.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; P46644; -.
DR OMA; ITQPTWG; -.
DR OrthoDB; 1104596at2759; -.
DR PhylomeDB; P46644; -.
DR SABIO-RK; P46644; -.
DR PRO; PR:P46644; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P46644; baseline and differential.
DR Genevisible; P46644; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0010150; P:leaf senescence; IEP:TAIR.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IMP:TAIR.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11879; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Chloroplast; Plastid; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 44..449
FT /note="Aspartate aminotransferase 3, chloroplastic"
FT /id="PRO_0000001210"
FT BINDING 81
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT BINDING 178
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT BINDING 231
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT BINDING 423
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT MOD_RES 295
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P23542"
SQ SEQUENCE 449 AA; 48954 MW; 8668EA40367C6A58 CRC64;
MKTTHFSSSS SSDRRIGALL RHLNSGSDSD NLSSLYASPT SGGTGGSVFS HLVQAPEDPI
LGVTVAYNKD PSPVKLNLGV GAYRTEEGKP LVLNVVRKAE QQLINDRTRI KEYLPIVGLV
EFNKLSAKLI LGADSPAIRE NRITTVECLS GTGSLRVGGE FLAKHYHQKT IYITQPTWGN
HPKIFTLAGL TVKTYRYYDP ATRGLNFQGL LEDLGAAAPG SIVLLHACAH NPTGVDPTIQ
QWEQIRKLMR SKGLMPFFDS AYQGFASGSL DTDAKPIRMF VADGGECLVA QSYAKNMGLY
GERVGALSIV CKSADVAGRV ESQLKLVIRP MYSSPPIHGA SIVAVILRDK NLFNEWTLEL
KAMADRIISM RKQLFEALRT RGTPGDWSHI IKQIGMFTFT GLNPAQVSFM TKEYHIYMTS
DGRISMAGLS SKTVPHLADA IHAVVTKAV
