Reviewed, UniProtKB/Swiss-Prot P85310 (AATM_CATRO)

Names and origin

Protein names	Recommended name:     Aspartate aminotransferase, mitochondrial     EC=2.6.1.1 Alternative name(s):     Transaminase A     Glutamate oxaloacetate transaminase 2
Organism	Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Taxonomic identifier	4058 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Gentianales › Apocynaceae › Rauvolfioideae › Vinceae › Catharanthus

Protein attributes

Sequence length	28 AA.
Sequence status	Fragments.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol By similarity.
Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. UniProtKB P00508
Cofactor	Pyridoxal phosphate By similarity. UniProtKB P00508
Subunit structure	Homodimer By similarity. UniProtKB P00508
Subcellular location	Mitochondrion matrix By similarity UniProtKB P00508.
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
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Direct protein sequencing
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 glutamate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-aspartate:2-oxoglutarate aminotransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›28	›28	Aspartate aminotransferase, mitochondrial		PRO_0000312771
Experimental info
	Non-adjacent residues	13 – 14	2
	Non-terminal residue	1	1
	Non-terminal residue	28	1

Sequences

	Sequence		Length	Mass (Da)
	P85310-1 [UniParc]. Last modified December 4, 2007. Version 1. Checksum: 8D8BE476675B227A	FASTA	28	3,031
	10 20 DDNGKPYVLP SVRTCGFDFT GAVEDISK

References

[1]	Varman P.A.M., Ranjitha Kumari B.D. Submitted (OCT-2007) to UniProtKB Cited for: PROTEIN SEQUENCE.

Cross-references

3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.6.1.1. 20471.
Family and domain databases
PROSITE	PS00105. AA_TRANSFER_CLASS_1. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AATM_CATRO

Accession

Primary (citable) accession number: P85310

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	December 4, 2007
Last modified:	February 9, 2010
This is version 12 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)