AAT5_ARATH
ID AAT5_ARATH Reviewed; 453 AA.
AC P46248; O49392; Q8LGE6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Aspartate aminotransferase, chloroplastic;
DE EC=2.6.1.1;
DE AltName: Full=Transaminase A;
DE Flags: Precursor;
GN Name=ASP5;
GN Synonyms=AAT1 {ECO:0000303|PubMed:7766905},
GN AAT3 {ECO:0000303|PubMed:9611168};
GN OrderedLocusNames=At4g31990 {ECO:0000312|Araport:AT4G31990};
GN ORFNames=F10N7.200;
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. C24; TISSUE=Leaf;
RX PubMed=7766905; DOI=10.1007/bf00020897;
RA Wilkie S.E., Roper J.M., Smith A.G., Warren M.J.;
RT "Isolation, characterisation and expression of a cDNA clone encoding
RT plastid aspartate aminotransferase from Arabidopsis thaliana.";
RL Plant Mol. Biol. 27:1227-1233(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND 3D-STRUCTURE MODELING.
RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX PubMed=8921007; DOI=10.1042/bj3190969;
RA Wilkie S.E., Lambert R., Warren M.J.;
RT "Chloroplastic aspartate aminotransferase from Arabidopsis thaliana: an
RT examination of the relationship between the structure of the gene and the
RT spatial structure of the protein.";
RL Biochem. J. 319:969-976(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
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 [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 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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9535706; DOI=10.1006/prep.1997.0845;
RA Wilkie S.E., Warren M.J.;
RT "Recombinant expression, purification, and characterization of three
RT isoenzymes of aspartate aminotransferase from Arabidopsis thaliana.";
RL Protein Expr. Purif. 12:381-389(1998).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF PRO-118; GLY-156 AND GLY-342.
RX PubMed=12068109; DOI=10.1104/pp.005090;
RA Miesak B.H., Coruzzi G.M.;
RT "Molecular and physiological analysis of Arabidopsis mutants defective in
RT cytosolic or chloroplastic aspartate aminotransferase.";
RL Plant Physiol. 129:650-660(2002).
RN [10]
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 [11]
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:7766905,
CC ECO:0000269|PubMed:9535706}.
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:9535706,
CC ECO:0000269|PubMed:9611168};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 mM for L-aspartate {ECO:0000269|PubMed:18318836};
CC KM=2.85 mM for L-aspartate {ECO:0000269|PubMed:9535706};
CC KM=0.09 mM for 2-oxoglutarate {ECO:0000269|PubMed:9535706};
CC KM=11.6 mM for L-glutamate {ECO:0000269|PubMed:9535706};
CC KM=0.020 mM for oxaloacetate {ECO:0000269|PubMed:9535706};
CC Note=kcat is 176 sec(-1) for the forward reaction. kcat is 279 sec(-
CC 1) for the reverse reaction. {ECO:0000269|PubMed:9535706};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast
CC {ECO:0000303|PubMed:9535706}.
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=P46248-1; Sequence=Displayed;
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; X81026; CAA56932.1; -; mRNA.
DR EMBL; X91865; CAA62972.1; -; Genomic_DNA.
DR EMBL; AL021636; CAA16590.1; -; Genomic_DNA.
DR EMBL; AL161580; CAB79917.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85987.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85988.1; -; Genomic_DNA.
DR EMBL; AY054660; AAK96851.1; -; mRNA.
DR EMBL; AY081506; AAM10068.1; -; mRNA.
DR EMBL; AY084314; AAM67272.1; -; mRNA.
DR PIR; T04646; T04646.
DR RefSeq; NP_194927.1; NM_119351.3. [P46248-1]
DR RefSeq; NP_849483.1; NM_179152.3. [P46248-1]
DR AlphaFoldDB; P46248; -.
DR SMR; P46248; -.
DR BioGRID; 14616; 12.
DR STRING; 3702.AT4G31990.3; -.
DR iPTMnet; P46248; -.
DR MetOSite; P46248; -.
DR PaxDb; P46248; -.
DR PRIDE; P46248; -.
DR ProteomicsDB; 245078; -. [P46248-1]
DR EnsemblPlants; AT4G31990.1; AT4G31990.1; AT4G31990. [P46248-1]
DR EnsemblPlants; AT4G31990.2; AT4G31990.2; AT4G31990. [P46248-1]
DR GeneID; 829330; -.
DR Gramene; AT4G31990.1; AT4G31990.1; AT4G31990. [P46248-1]
DR Gramene; AT4G31990.2; AT4G31990.2; AT4G31990. [P46248-1]
DR KEGG; ath:AT4G31990; -.
DR Araport; AT4G31990; -.
DR eggNOG; KOG1411; Eukaryota.
DR InParanoid; P46248; -.
DR OMA; VGACTIV; -.
DR PhylomeDB; P46248; -.
DR SABIO-RK; P46248; -.
DR PRO; PR:P46248; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P46248; baseline and differential.
DR Genevisible; P46248; AT.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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 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 Alternative splicing; Aminotransferase; Amyloplast; Chloroplast; Plastid;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 45..453
FT /note="Aspartate aminotransferase, chloroplastic"
FT /id="PRO_0000001211"
FT BINDING 85
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT BINDING 181
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250, ECO:0000250|UniProtKB:P23542"
FT BINDING 234
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT BINDING 427
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT MOD_RES 298
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT MUTAGEN 118
FT /note="P->S: In aat3-1; loss of function."
FT /evidence="ECO:0000269|PubMed:12068109"
FT MUTAGEN 156
FT /note="G->S: In aat3-4; loss of function."
FT /evidence="ECO:0000269|PubMed:12068109"
FT MUTAGEN 342
FT /note="G->E: In aat3-2; loss of function."
FT /evidence="ECO:0000269|PubMed:12068109"
FT CONFLICT 22..23
FT /note="KL -> NV (in Ref. 1; CAA56932 and 2; CAA62972)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="A -> S (in Ref. 6; AAM67272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 49831 MW; D3389C6FB0C4CADC CRC64;
MASLMLSLGS TSLLPREINK DKLKLGTSAS NPFLKAKSFS RVTMTVAVKP SRFEGITMAP
PDPILGVSEA FKADTNGMKL NLGVGAYRTE ELQPYVLNVV KKAENLMLER GDNKEYLPIE
GLAAFNKATA ELLFGAGHPV IKEQRVATIQ GLSGTGSLRL AAALIERYFP GAKVVISSPT
WGNHKNIFND AKVPWSEYRY YDPKTIGLDF EGMIADIKEA PEGSFILLHG CAHNPTGIDP
TPEQWVKIAD VIQEKNHIPF FDVAYQGFAS GSLDEDAASV RLFAERGMEF FVAQSYSKNL
GLYAERIGAI NVVCSSADAA TRVKSQLKRI ARPMYSNPPV HGARIVANVV GDVTMFSEWK
AEMEMMAGRI KTVRQELYDS LVSKDKSGKD WSFILKQIGM FSFTGLNKAQ SDNMTDKWHV
YMTKDGRISL AGLSLAKCEY LADAIIDSYH NVS
