A5A6K8 (AATC_PANTR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate aminotransferase, cytoplasmic
EC=2.6.1.1

Alternative name(s):
Glutamate oxaloacetate transaminase 1
Transaminase A

Gene names

Name:

GOT1

Organism

Pan troglodytes (Chimpanzee)

Taxonomic identifier

9598 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	413 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 By similarity.
Catalytic activity	L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
Cofactor	Pyridoxal phosphate By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm 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	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Phosphoprotein
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	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 413	412	Aspartate aminotransferase, cytoplasmic		PRO_0000297546
Sites
	Binding site	39	1	Aspartate; via amide nitrogen By similarity
	Binding site	141	1	Aspartate By similarity
	Binding site	195	1	Aspartate By similarity
	Binding site	387	1	Aspartate By similarity
Amino acid modifications
	Modified residue	66	1	Phosphoserine By similarity
	Modified residue	71	1	Phosphotyrosine By similarity
	Modified residue	259	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5A6K8 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: 6CFB38EA09540219	FASTA	413	46,233
	10 20 30 40 50 60 MAPPSVFAEV PQAQPVLVFK LTADFREDPD PRKVNLGVGA YRTDDCHPWV LPVVKKVEQK 70 80 90 100 110 120 IANDNSLNHE YLPILGLAEF RSCASRLALG DDSPALKEKR VGGVQSLGGT GALRIGADFL 130 140 150 160 170 180 ARWYNGTNNK NTPVYVSSPT WENHNAVFSA AGFKDIRSYR YWDAEKRGLD LQGFLNDLEN 190 200 210 220 230 240 APEFSIVVLH ACAHNPTGID PTPEQWKQIA SVMKHRFLFP FFDSAYQGFA SGNLERDAWA 250 260 270 280 290 300 IRYFVSEGFE FFCAQSFSKN FGLYNERVGN LTVVGKEPES ILQVLSQMEK IVRITWSNPP 310 320 330 340 350 360 AQGARIVAST LSNPELFEEW TGNVKTMADR ILSMRSELRA RLEALKTPGT WNHITDQIGM 370 380 390 400 410 FSFTGLNPKQ VEYLVNEKHI YLLPSGRINV SGLTTKNLDY VATSIHEAVT KIQ

References

[1]

"Mapping of chimpanzee full-length cDNAs onto the human genome unveils large potential divergence of the transcriptome." Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I., Kusuda J., Gojobori T., Hashimoto K., Hirai M. Gene 399:1-10(2007) [PubMed: 17574350] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB222136 mRNA. Translation: BAF62381.1.
RefSeq	NP_001092011.1. NM_001098541.1.
UniGene	Ptr.165.
3D structure databases
ProteinModelPortal	A5A6K8.
SMR	A5A6K8. Positions 2-413.
ModBase	Search...
Protein-protein interaction databases
STRING	A5A6K8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	450664.
KEGG	ptr:450664.
Organism-specific databases
CTD	2805.
Phylogenomic databases
eggNOG	prNOG05649.
GeneTree	ENSGT00390000014081.
HOVERGEN	HBG000951.
InParanoid	A5A6K8.
OrthoDB	EOG47D9G5.
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.
KO	K14454.
PANTHER	PTHR11879. Asp_trans. 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

AATC_PANTR

Accession

Primary (citable) accession number: A5A6K8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 21, 2007
Last sequence update:	June 12, 2007
Last modified:	November 16, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program