Reviewed, UniProtKB/Swiss-Prot Q28F67 (AATM_XENTR)

Names and origin

Protein names

Recommended name:
    Aspartate aminotransferase, mitochondrial
      Short name=mAspAT
    EC=2.6.1.1
Alternative name(s):
    Transaminase A
    Glutamate oxaloacetate transaminase 2

Gene names

Name:	got2
ORF Names:	TGas123d19.1

Organism

Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)

Taxonomic identifier

8364 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Silurana

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. May facilitate cellular uptake of long-chain free fatty acids By similarity.
Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
Cofactor	Pyridoxal phosphate By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion matrix. Cell membrane By similarity.
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	Cell membrane Membrane 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 plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-aspartate:2-oxoglutarate aminotransferase activity Inferred from sequence or structural similarity. Source: UniProtKB 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 – 26	26	Mitochondrion By similarity
	Chain	27 – 427	401	Aspartate aminotransferase, mitochondrial		PRO_0000327598
Sites
	Binding site	62	1	Aspartate; via amide nitrogen By similarity
	Binding site	159	1	Aspartate By similarity
	Binding site	212	1	Aspartate By similarity
	Binding site	404	1	Aspartate By similarity
Amino acid modifications
	Modified residue	276	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q28F67-1 [UniParc]. Last modified April 4, 2006. Version 1. Checksum: 240F95773AC1A12C	FASTA	427	47,575
	10 20 30 40 50 60 MALLKSRLLV GVARCQPCLA AVQGRASSWW SHVEMGPPDP ILGVTEAFKR DTNSKKMNLG 70 80 90 100 110 120 VGAYRDDNGK PYVLSSVRKA EAQLASKNLD KEYLPIGGLA EFARASAQLA LGENCDAIQS 130 140 150 160 170 180 GRFITVQTIS GTGSLRVGAN FLQRFYKYSR DVYLPKPSWG NHTPIFRDAG LEVKGYRYYD 190 200 210 220 230 240 PKTCGFDFTG ALDDISKIPE QSIILFHACA HNPTGVDPKQ EQWKELAALI KSRRLFPFFD 250 260 270 280 290 300 MAYQGFASGD TNRDAWAVRH FIQEGINVVL SQSYAKNMGL YGERVGAFTV VCSDAEEAKR 310 320 330 340 350 360 VESQLKILIR PMYSNPPLNG ARIAAAILTQ PDLRKEWLQE VKGMANRIIS MREQLVSNLK 370 380 390 400 410 420 KEGSIHNWQH ISDQIGMFCF TGLRPEQVER LIKEFSIYMT KDGRISVAGV TSANNGYLAH AIHQVTK

References

[1]	Sanger Xenopus tropicalis EST/cDNA project Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Tissue: Gastrula.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR762138 mRNA. Translation: CAJ83961.1.
RefSeq	NP_001016933.1.
UniGene	Str.1247
3D structure databases
SMR	Q28F67. Positions 27-427.
ModBase	Search...
Protein-protein interaction databases
STRING	Q28F67.
Genome annotation databases
GeneID	549687.
KEGG	xtr:549687.
Organism-specific databases
CTD	549687.
Xenbase	XB-FEAT-998299. got2.
Phylogenomic databases
eggNOG	veNOG12918.
HOVERGEN	Q28F67.
Enzyme and pathway databases
BRENDA	2.6.1.1. 279072.
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

AATM_XENTR

Accession

Primary (citable) accession number: Q28F67

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	April 4, 2006
Last modified:	February 9, 2010
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Xenopus annotation project