Reviewed, UniProtKB/Swiss-Prot Q5REB0 (AATM_PONAB)

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

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	430 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	Facilitates 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 By similarity. 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
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro 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
	Transit peptide	1 – 29	29	Mitochondrion By similarity
	Chain	30 – 430	401	Aspartate aminotransferase, mitochondrial		PRO_0000278665
Amino acid modifications
	Modified residue	73	1	N6-acetyllysine By similarity
	Modified residue	90	1	N6-acetyllysine By similarity
	Modified residue	94	1	N6-acetyllysine By similarity
	Modified residue	96	1	Phosphotyrosine By similarity
	Modified residue	150	1	N6-acetyllysine By similarity
	Modified residue	159	1	N6-acetyllysine By similarity
	Modified residue	185	1	N6-acetyllysine By similarity
	Modified residue	234	1	N6-acetyllysine By similarity
	Modified residue	279	1	N6-(pyridoxal phosphate)lysine By similarity
	Modified residue	296	1	N6-acetyllysine By similarity
	Modified residue	345	1	N6-acetyllysine By similarity
	Modified residue	363	1	N6-acetyllysine By similarity
	Modified residue	396	1	N6-acetyllysine By similarity
	Modified residue	401	1	Phosphotyrosine By similarity
	Modified residue	404	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	339	1	Q → T in CAH92240. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q5REB0-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 4A3B7B89A5FEB9C5	FASTA	430	47,433
	10 20 30 40 50 60 MALLHSGRAL PGIAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM 70 80 90 100 110 120 NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENSEV 130 140 150 160 170 180 LKSGRFVTVQ TISGTGALRI GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR 190 200 210 220 230 240 YYDPKTCGFD FTGAVEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA TVVKKRNLFA 250 260 270 280 290 300 FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTMVCKDADE 310 320 330 340 350 360 AKRVESQLKI LIRPMYSNPP LNGARIAAAI LNTPDLRKQW LQEVKGMADR IIGMRTQLVS 370 380 390 400 410 420 NLKKEGSTHN WQHITDQIGM FCFTGLKPEQ VERLIKEFSI YMTKDGRISV AGVTSSNVGY 430 LAHAIHQVTK

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex and Kidney.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR857622 mRNA. Translation: CAH89897.1. CR860094 mRNA. Translation: CAH92240.1.
RefSeq	NP_001124888.1.
UniGene	Pab.145
3D structure databases
SMR	Q5REB0. Positions 30-430.
ModBase	Search...
Genome annotation databases
GeneID	100171753.
Organism-specific databases
CTD	100171753.
Phylogenomic databases
HOVERGEN	Q5REB0.
OMA	IASSYSK.
Enzyme and pathway databases
BRENDA	2.6.1.1. 269192.
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_PONAB

Accession

Primary (citable) accession number: Q5REB0
Secondary accession number(s): Q5R7M0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 20, 2007
Last sequence update:	December 21, 2004
Last modified:	November 3, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)