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P12345 (AATM_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Aspartate aminotransferase, mitochondrial

Short name=mAspAT
EC=2.6.1.1
EC=2.6.1.7
Alternative name(s):
Fatty acid-binding protein
Short name=FABP-1
Glutamate oxaloacetate transaminase 2
Kynurenine aminotransferase 4
Kynurenine aminotransferase IV
Kynurenine--oxoglutarate transaminase 4
Kynurenine--oxoglutarate transaminase IV
Plasma membrane-associated fatty acid-binding protein
Short name=FABPpm
Transaminase A
Gene names
Name:GOT2
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length30 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids By similarity.

Catalytic activity

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.

L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + 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 processLipid transport
Transport
   Cellular componentCell membrane
Membrane
Mitochondrion
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

aspartate biosynthetic process

Inferred from electronic annotation. Source: Compara

aspartate catabolic process

Inferred from electronic annotation. Source: Compara

aspartate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid transport

Inferred from electronic annotation. Source: Compara

glutamate catabolic process to 2-oxoglutarate

Inferred from electronic annotation. Source: Compara

glutamate catabolic process to aspartate

Inferred from electronic annotation. Source: Compara

glutamate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

oxaloacetate metabolic process

Inferred from electronic annotation. Source: Compara

protein folding

Traceable author statement PubMed 9683573. Source: HGNC

response to ethanol

Inferred from electronic annotation. Source: Compara

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: Compara

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-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

kynurenine-oxoglutarate transaminase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›30›30Aspartate aminotransferase, mitochondrial
PRO_0000123886

Experimental info

Non-terminal residue301

Sequences

Sequence LengthMass (Da)Tools
P12345 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 410321530B95B673

FASTA303,401
        10         20         30 
SSWWAHVEMG PPDPILGVTE AYKRDTNSKK 

« Hide

References

[1]"Aspartate aminotransferase isozymes from rabbit liver. Purification and properties."
Kuramitsu S., Inoue K., Kondo K., Aki K., Kagamiyama H.
J. Biochem. 97:1337-1345(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Liver.

Cross-references

Sequence databases

PIRB27103.

3D structure databases

ProteinModelPortalP12345.
SMRP12345. Positions 1-30.
ModBaseSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000003357.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1448.
HOGENOMHOG000185898.
OrthoDBEOG4RXZ07.

Family and domain databases

PROSITEPS00105. AA_TRANSFER_CLASS_1. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAATM_RABIT
AccessionPrimary (citable) accession number: P12345
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: April 3, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families