P26563 (AATM_LUPAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Aspartate aminotransferase P2, mitochondrial EC=2.6.1.1 Alternative name(s): Transaminase A
Organism	Lupinus angustifolius (Narrow-leaved blue lupin)
Taxonomic identifier	3871 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Genisteae › Lupinus

Protein attributes

Sequence length	454 AA.
Sequence status	Fragment.
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	Mitochondrion matrix.
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	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
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
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity Inferred from sequence or structural similarity. Source: UniProtKB L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	‹1 – 49	›49	Mitochondrion Potential
	Chain	50 – 454	405	Aspartate aminotransferase P2, mitochondrial		PRO_0000001212
Sites
	Binding site	86	1	Aspartate; via amide nitrogen By similarity
	Binding site	182	1	Aspartate By similarity
	Binding site	235	1	Aspartate By similarity
	Binding site	428	1	Aspartate By similarity
Amino acid modifications
	Modified residue	299	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P26563 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 744CC12F1D81E739	FASTA	454	49,916
	10 20 30 40 50 60 SSLLSIPSLS LQYNDKLKVG GNSLRFSKEQ SNTFSNAKSS CRISMVAAVN VSRFEGIPMA 70 80 90 100 110 120 PPDPILGVSE AFRADTSDAK LNLGVGAYRT EELQPYVLKV VNKAENLMLE RGQNKEYLAI 130 140 150 160 170 180 EGLAAFNKAT AELLLGADNP AIKQQRVATV QGLSGTGSLR LGAALIERYF PGAKVLISAP 190 200 210 220 230 240 TWGNHKNIFN DARVPWSEYR YYDPKTVGLD FEGMIEDIKA APEGTFVLLH GCAHNPTGID 250 260 270 280 290 300 PTPEQWEKIA DVIQEKNHIP FFDVAYQGFA SGSLDEDAAS VRLFVARGLE VLVAQSYSKN 310 320 330 340 350 360 LGLYAERIGA INVISSSPES AARVKSQLKR IARPMYSNPP VHGARIVADI VGNPALFDEW 370 380 390 400 410 420 KVEMEMMAGR IKNVRQQLYD SISSKDKSGK DWSFILKQIG MFSYTGLNKN QSDNMTNKWH 430 440 450 VYMTKDGRIS LAGLSLAKCE YLADAIIDSF HYVS

References

[1]

"Molecular cloning of a cDNA encoding aspartate aminotransferase-P2 from lupin root nodules." Reynolds P.H.S., Smith L.A., Jones W.T., Dickson J.M.J., Jones S.J., Rodber K., Liddane C.P. Plant Mol. Biol. 19:465-472(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Uniharvest. Tissue: Root nodule.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X59761 mRNA. Translation: CAA42430.1.
PIR	XNYLB. S22465.
3D structure databases
ProteinModelPortal	P26563.
SMR	P26563. Positions 52-448.
ModBase	Search...
Proteomic databases
ProMEX	P26563.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.40.640.10. 1 hit.
InterPro	IPR004839. Aminotransferase_I/II. IPR000796. Asp_trans. IPR004838. NHTrfase_class1_PyrdxlP-BS. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
PANTHER	PTHR11879. PTHR11879. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00799. TRANSAMINASE.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITE	PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AATM_LUPAN

Accession

Primary (citable) accession number: P26563

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	April 3, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program