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P12345 (AATM_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 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 processLipid transport
Transport
   Cellular componentCell membrane
Membrane
Mitochondrion
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   PTMAcetylation
Nitration
   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: Ensembl

aspartate catabolic process

Inferred from electronic annotation. Source: Ensembl

aspartate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid transport

Inferred from electronic annotation. Source: Ensembl

glutamate catabolic process to 2-oxoglutarate

Inferred from electronic annotation. Source: Ensembl

glutamate catabolic process to aspartate

Inferred from electronic annotation. Source: Ensembl

glutamate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

oxaloacetate metabolic process

Inferred from electronic annotation. Source: Ensembl

protein folding

Traceable author statement PubMed 9683573. Source: HGNC

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from direct assay PubMed 3099306. Source: AgBase

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

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: UniProtKB-EC

kynurenine-oxoglutarate transaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion Ref.2
Chain30 – 430401Aspartate aminotransferase, mitochondrial
PRO_0000123886

Sites

Binding site651Substrate; via amide nitrogen By similarity
Binding site1621Substrate By similarity
Binding site2151Substrate By similarity
Binding site4071Substrate By similarity

Amino acid modifications

Modified residue591N6-acetyllysine By similarity
Modified residue731N6-acetyllysine; alternate By similarity
Modified residue731N6-succinyllysine; alternate By similarity
Modified residue821N6-acetyllysine By similarity
Modified residue901N6-acetyllysine; alternate By similarity
Modified residue901N6-succinyllysine; alternate By similarity
Modified residue961Nitrated tyrosine By similarity
Modified residue1221N6-acetyllysine; alternate By similarity
Modified residue1221N6-succinyllysine; alternate By similarity
Modified residue1591N6-acetyllysine; alternate By similarity
Modified residue1591N6-succinyllysine; alternate By similarity
Modified residue1851N6-acetyllysine; alternate By similarity
Modified residue1851N6-succinyllysine; alternate By similarity
Modified residue2271N6-succinyllysine By similarity
Modified residue2341N6-acetyllysine By similarity
Modified residue2791N6-(pyridoxal phosphate)lysine; alternate By similarity
Modified residue2791N6-acetyllysine; alternate By similarity
Modified residue2961N6-acetyllysine; alternate By similarity
Modified residue2961N6-succinyllysine; alternate By similarity
Modified residue3021N6-acetyllysine By similarity
Modified residue3091N6-acetyllysine; alternate By similarity
Modified residue3091N6-succinyllysine; alternate By similarity
Modified residue3381N6-acetyllysine; alternate By similarity
Modified residue3381N6-succinyllysine; alternate By similarity
Modified residue3451N6-acetyllysine By similarity
Modified residue3631N6-acetyllysine; alternate By similarity
Modified residue3631N6-succinyllysine; alternate By similarity
Modified residue3641N6-acetyllysine By similarity
Modified residue3871N6-acetyllysine By similarity
Modified residue3961N6-acetyllysine; alternate By similarity
Modified residue3961N6-succinyllysine; alternate By similarity
Modified residue4041N6-acetyllysine; alternate By similarity
Modified residue4041N6-succinyllysine; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
P12345 [UniParc].

Last modified September 18, 2013. Version 2.
Checksum: 12F54284974D27A5

FASTA43047,409
        10         20         30         40         50         60 
MALLHSARVL SGVASAFHPG LAAAASARAS SWWAHVEMGP PDPILGVTEA YKRDTNSKKM 

        70         80         90        100        110        120 
NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK GLDKEYLPIG GLAEFCRASA ELALGENSEV 

       130        140        150        160        170        180 
VKSGRFVTVQ TISGTGALRI GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQSYR 

       190        200        210        220        230        240 
YYDPKTCGFD FTGALEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA TVVKKRNLFA 

       250        260        270        280        290        300 
FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVICKDADE 

       310        320        330        340        350        360 
AKRVESQLKI LIRPMYSNPP IHGARIASTI LTSPDLRKQW LQEVKGMADR IIGMRTQLVS 

       370        380        390        400        410        420 
NLKKEGSTHS WQHITDQIGM FCFTGLKPEQ VERLTKEFSI YMTKDGRISV AGVTSGNVGY 

       430 
LAHAIHQVTK 

« Hide

References

« Hide 'large scale' references
[1]"Genome Sequence of Oryctolagus cuniculus (European rabbit)."
The Genome Sequencing Platform
Di Palma F., Heiman D., Young S., Gnerre S., Johnson J., Lander E.S., Lindblad-Toh K.
Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Thorbecke.
[2]"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 OF 30-59.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAGW02052878 Genomic DNA. No translation available.
PIRB27103.
RefSeqXP_002711597.1. XM_002711551.1.
UniGeneOcu.5296.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000003357.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSOCUT00000003872; ENSOCUP00000003357; ENSOCUG00000003871.
GeneID100348732.

Phylogenomic databases

eggNOGCOG1448.
GeneTreeENSGT00390000014081.
HOGENOMHOG000185898.
OMARVGAFTM.
OrthoDBEOG74J980.
TreeFamTF300641.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11879. PTHR11879. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00799. TRANSAMINASE.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAATM_RABIT
AccessionPrimary (citable) accession number: P12345
Secondary accession number(s): G1SKL2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: September 18, 2013
Last modified: July 9, 2014
This is version 91 of the entry and version 2 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