Reviewed, UniProtKB/Swiss-Prot P46248 (AAT5_ARATH)

Names and origin

Protein names

Recommended name:
    Aspartate aminotransferase, chloroplastic
    EC=2.6.1.1
Alternative name(s):
    Transaminase A

Gene names

Name:	ASP5
Synonyms:	AAT1
Ordered Locus Names:	At4g31990
ORF Names:	F10N7.200

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	453 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Important for the metabolism of amino acids and Krebs-cycle related organic acids. In plants, it is involved in nitrogen metabolism and in aspects of carbon and energy metabolism.
Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
Cofactor	Pyridoxal phosphate.
Subunit structure	Homodimer By similarity.
Subcellular location	Plastid › chloroplast.
Miscellaneous	In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	2-oxoglutarate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB aspartate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB biosynthetic process Inferred from electronic annotation. Source: InterPro glutamate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB response to cadmium ion Inferred from expression pattern. Source: TAIR response to cold Inferred from expression pattern. Source: TAIR
Cellular component	apoplast Inferred from direct assay. Source: TAIR chloroplast envelope Inferred from direct assay. Source: TAIR chloroplast stroma Inferred from direct assay. Source: TAIR stromule Inferred from direct assay. Source: TAIR
Molecular function	L-aspartate:2-oxoglutarate aminotransferase activity Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P46248-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 52	52	Chloroplast Potential
	Chain	53 – 453	401	Aspartate aminotransferase, chloroplastic		PRO_0000001211
Sites
	Binding site	85	1	Aspartate; via amide nitrogen By similarity
	Binding site	181	1	Aspartate By similarity
	Binding site	234	1	Aspartate By similarity
	Binding site	427	1	Aspartate By similarity
Amino acid modifications
	Modified residue	298	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	22 – 23	2	KL → NV Ref.1
	Sequence conflict	22 – 23	2	KL → NV Ref.2
	Sequence conflict	409	1	A → S in AAM67272. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 10, 2002. Version 2. Checksum: D3389C6FB0C4CADC	FASTA	453	49,831
	10 20 30 40 50 60 MASLMLSLGS TSLLPREINK DKLKLGTSAS NPFLKAKSFS RVTMTVAVKP SRFEGITMAP 70 80 90 100 110 120 PDPILGVSEA FKADTNGMKL NLGVGAYRTE ELQPYVLNVV KKAENLMLER GDNKEYLPIE 130 140 150 160 170 180 GLAAFNKATA ELLFGAGHPV IKEQRVATIQ GLSGTGSLRL AAALIERYFP GAKVVISSPT 190 200 210 220 230 240 WGNHKNIFND AKVPWSEYRY YDPKTIGLDF EGMIADIKEA PEGSFILLHG CAHNPTGIDP 250 260 270 280 290 300 TPEQWVKIAD VIQEKNHIPF FDVAYQGFAS GSLDEDAASV RLFAERGMEF FVAQSYSKNL 310 320 330 340 350 360 GLYAERIGAI NVVCSSADAA TRVKSQLKRI ARPMYSNPPV HGARIVANVV GDVTMFSEWK 370 380 390 400 410 420 AEMEMMAGRI KTVRQELYDS LVSKDKSGKD WSFILKQIGM FSFTGLNKAQ SDNMTDKWHV 430 440 450 YMTKDGRISL AGLSLAKCEY LADAIIDSYH NVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation, characterisation and expression of a cDNA clone encoding plastid aspartate aminotransferase from Arabidopsis thaliana." Wilkie S.E., Roper J.M., Smith A.G., Warren M.J. Plant Mol. Biol. 27:1227-1233(1995) [PubMed: 7766905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. C24. Tissue: Leaf.
[2]	"Chloroplastic aspartate aminotransferase from Arabidopsis thaliana: an examination of the relationship between the structure of the gene and the spatial structure of the protein." Wilkie S.E., Lambert R., Warren M.J. Biochem. J. 319:969-976(1996) [PubMed: 8921007] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Landsberg erecta. Tissue: Leaf.
[3]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X81026 mRNA. Translation: CAA56932.1. X91865 Genomic DNA. Translation: CAA62972.1. AL021636 Genomic DNA. Translation: CAA16590.1. AL161580 Genomic DNA. Translation: CAB79917.1. AY054660 mRNA. Translation: AAK96851.1. AY081506 mRNA. Translation: AAM10068.1. AY084314 mRNA. Translation: AAM67272.1.
IPI	IPI00523179.
PIR	T04646.
RefSeq	NP_194927.1. NP_849483.1.
UniGene	At.20417 Rra.5937
3D structure databases
SMR	P46248. Positions 50-447.
ModBase	Search...
Protein-protein interaction databases
STRING	P46248.
Proteomic databases
PRIDE	P46248.
ProMEX	P46248.
Genome annotation databases
GeneID	829330.
GenomeReviews	Gene locus AT4G31990 in contig CT486007_GR.
NMPDR	fig|3702.1.peg.21215.
Organism-specific databases
TAIR	At4g31990.
Phylogenomic databases
eggNOG	KOG1411.
HOGENOM	HBG446828.
InParanoid	P46248.
PhylomeDB	P46248.
Enzyme and pathway databases
BRENDA	2.6.1.1. 302.
Gene expression databases
ArrayExpress	P46248.
Genevestigator	P46248.
Family and domain databases
InterPro	IPR004839. Aminotransferase_I/II. IPR000796. Asp_trans. IPR004838. NHTrfase_class1_PyrdxlP-BS. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11879. Asp_trans. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00799. TRANSAMINASE.
PROSITE	PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AAT5_ARATH

Accession

Primary (citable) accession number: P46248
Secondary accession number(s): O49392, Q8LGE6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	May 10, 2002
Last modified:	February 9, 2010
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)