Reviewed, UniProtKB/Swiss-Prot P08907 (AATM_HORSE)

Names and origin

Protein names

Recommended name:
    Aspartate aminotransferase, mitochondrial
    EC=2.6.1.1
Alternative name(s):
    mAspAT
    Transaminase A
    Glutamate oxaloacetate transaminase 2
    Fatty acid-binding protein
    FABP-1
    FABPpm

Gene names

Name:

GOT2

Organism

Equus caballus (Horse)

Taxonomic identifier

9796 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus

Protein attributes

Sequence length	401 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Facilitates cellular uptake of long-chain free fatty acids By similarity.
Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
Cofactor	Pyridoxal phosphate.
Subunit structure	Homodimer.
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
Biological process	Lipid transport Transport
Cellular component	Cell membrane Membrane Mitochondrion
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid transport Inferred from electronic annotation. Source: UniProtKB-KW
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 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
	Chain	1 – 401	401	Aspartate aminotransferase, mitochondrial		PRO_0000123885
Amino acid modifications
	Modified residue	44	1	N6-acetyllysine By similarity
	Modified residue	61	1	N6-acetyllysine By similarity
	Modified residue	65	1	N6-acetyllysine By similarity
	Modified residue	67	1	Phosphotyrosine By similarity
	Modified residue	121	1	N6-acetyllysine By similarity
	Modified residue	130	1	N6-acetyllysine By similarity
	Modified residue	156	1	N6-acetyllysine By similarity
	Modified residue	205	1	N6-acetyllysine By similarity
	Modified residue	250	1	N6-(pyridoxal phosphate)lysine
	Modified residue	267	1	N6-acetyllysine By similarity
	Modified residue	316	1	N6-acetyllysine By similarity
	Modified residue	334	1	N6-acetyllysine By similarity
	Modified residue	367	1	N6-acetyllysine By similarity
	Modified residue	372	1	Phosphotyrosine By similarity
	Modified residue	375	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P08907-1 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 8562D82170A40487	FASTA	401	44,567
	10 20 30 40 50 60 SSWWAHVEMG PPDPILGVTE AYKRDTNSKK MNLGVGAYRD DNGKPYVLPS VRKAEAQIAA 70 80 90 100 110 120 KNLDKEYLPI GGLAEFCKAS AELALGENSE ALKSGRYVTV QSISGTGALR IGANFLQRFF 130 140 150 160 170 180 KFSRDVFLPK PSWGNHTPIF RDAGLQLHAY RYYDPKTCGF DVTGALEDIS KIPQQSIILL 190 200 210 220 230 240 HACAHNPTGV DPRPEQWKEI ATLVKKNNLF AFFDMAYQGF ASGDGNKDAW AVRYFIEQGI 250 260 270 280 290 300 NVCLCQSYAK NMGLYGERVG AFTMVCKDAD EAKRVESQLK ILIRPLYSNP PLNGARIAST 310 320 330 340 350 360 ILTSPDLRKQ WLQEVKGMAD RIISMRTQLV SNLKKEGSSH SWQHIADQIG MFCFTGLKPE 370 380 390 400 QVERLTKEFS IYMTKDGRIS VAGVTSGNVG YLAHAIHQVT K

References

[1]	"The complete amino acid sequences of cytosolic and mitochondrial aspartate aminotransferases from horse heart, and inferences on evolution of the isoenzymes." Doonan S., Martini F., Angelaccio S., Pascarella S., Barra D., Bossa F. J. Mol. Evol. 23:328-335(1986) [PubMed: 3104605] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Primary structure of aspartate aminotransferase from horse heart and comparison with that of other homotopic and heterotopic isoenzymes." Martini F., Angelaccio S., Barra D., Doonan S., Bossa F. Comp. Biochem. Physiol. 76B:483-487(1983) [PubMed: 6641173] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases
PIR	B26341.
3D structure databases
HSSP	HSSP built from PDB template 7AAT based on UniProtKB P00508.
SMR	P08907. Positions 1-401.
ModBase	Search...
Genome annotation databases
Ensembl	ENSECAT00000017874; ENSECAP00000014550; ENSECAG00000016504; Equus caballus. [Genome view]
Phylogenomic databases
HOVERGEN	P08907.
Enzyme and pathway databases
BRENDA	2.6.1.1. 1464.
Family and domain databases
InterPro	IPR004839. Aminotransferase_I/II. IPR000796. Asp_trans. IPR004838. NHTrfase_class1_PyrdxlP-BS. 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_HORSE

Accession

Primary (citable) accession number: P08907

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	October 13, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)