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P04694 (ATTY_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Tyrosine aminotransferase

Short name=TAT
EC=2.6.1.5
Alternative name(s):
L-tyrosine:2-oxoglutarate aminotransferase
Gene names
Name:Tat
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity towards phenylalanine. Ref.5

Catalytic activity

L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate. Ref.5

Cofactor

Pyridoxal phosphate. Ref.2 Ref.5

Pathway

Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 2/6.

Subunit structure

Homodimer. Ref.5

Tissue specificity

Liver.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=2.2 mM for tyrosine Ref.5

Ontologies

Keywords
   Biological processPhenylalanine catabolism
Tyrosine catabolism
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from electronic annotation. Source: Ensembl

L-phenylalanine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

cellular amino acid metabolic process

Inferred from direct assay PubMed 12717026. Source: RGD

gluconeogenesis

Traceable author statement Ref.1. Source: RGD

glutamate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

response to glucocorticoid

Inferred from direct assay PubMed 16307467. Source: RGD

response to mercury ion

Inferred from direct assay PubMed 16307467. Source: RGD

response to organic cyclic compound

Inferred from direct assay PubMed 15755314. Source: RGD

response to oxidative stress

Inferred from direct assay PubMed 16335249. Source: RGD

tyrosine catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentmitochondrion

Inferred from direct assay PubMed 4390541. Source: RGD

   Molecular_functionL-phenylalanine:2-oxoglutarate aminotransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

L-tyrosine:2-oxoglutarate aminotransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

amino acid binding

Inferred from direct assay PubMed 12717026. Source: RGD

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454Tyrosine aminotransferase
PRO_0000123889

Amino acid modifications

Modified residue11N-acetylmethionine Ref.1
Modified residue2801N6-(pyridoxal phosphate)lysine Ref.2

Experimental info

Sequence conflict59 – 602IV → KT in AAA42203. Ref.2
Sequence conflict209 – 2102TA → LE in AAA42203. Ref.2
Sequence conflict2851P → L in CAA33725. Ref.4
Sequence conflict3041Missing in CAA33725. Ref.4
Sequence conflict359 – 3602AI → DL in AAA42203. Ref.2
Sequence conflict4451A → D in AAA42203. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P04694 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 835EBE0D2476AF71

FASTA45450,635
        10         20         30         40         50         60 
MDSYVIQTDV DDSLSSVLDV HVNIGGRNSV QGRKKGRKAR WDVRPSDMSN KTFNPIRAIV 

        70         80         90        100        110        120 
DNMKVQPNPN KTVISLSIGD PTVFGNLPTD PEVTQAMKDA LDSGKYNGYA PSIGYLSSRE 

       130        140        150        160        170        180 
EVASYYHCHE APLEAKDVIL TSGCSQAIEL CLAVLANPGQ NILIPRPGFS LYRTLAESMG 

       190        200        210        220        230        240 
IEVKLYNLLP EKSWEIDLKQ LESLIDEKTA CLVVNNPSNP CGSVFSKRHL QKILAVAERQ 

       250        260        270        280        290        300 
CVPILADEIY GDMVFSDCKY EPLANLSTNV PILSCGGLAK RWLVPGWRLG WILIHDRRDI 

       310        320        330        340        350        360 
FGNEIRDGLV KLSQRILGPC TIVQGALKSI LQRTPQEFYH DTLSFLKSNA DLCYGALAAI 

       370        380        390        400        410        420 
PGLQPVRPSG AMYLMVGIEM EHFPEFENDV EFTERLIAEQ AVHCLPATCF EYPNFFRVVI 

       430        440        450 
TVPEVMMLEA CSRIQEFCEQ HYHCAEGSQE ECDK 

« Hide

References

« Hide 'large scale' references
[1]"Complete complementary DNA of rat tyrosine aminotransferase messenger RNA. Deduction of the primary structure of the enzyme."
Grange T., Guenet C., Dietrich J.-B., Chasserot S., Fromont M., Befort N., Jami J., Beck G., Pictet R.
J. Mol. Biol. 184:347-350(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The structure of tyrosine aminotransferase. Evidence for domains involved in catalysis and enzyme turnover."
Hargrove J.L., Scoble H.A., Mathews W.R., Baumstark B.R., Biemann K.
J. Biol. Chem. 264:45-53(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[4]"Nucleotide sequence of rat liver tyrosine aminotransferase gene fragment."
Morozov I.V.
DNA Seq. 1:151-155(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 190-386.
Tissue: Liver.
[5]"Isolation and characterization of active N-terminal truncated apo- and holoenzyme of mammalian liver tyrosine aminotransferase."
Lorber B., Dietrich J.-B., Kern D.
FEBS Lett. 291:345-349(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[6]"Structural and immunochemical properties of rat liver tyrosine aminotransferase."
Dietrich J.-B., Genot G., Beck G.
Biochimie 70:673-679(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02741 mRNA. Translation: CAA26519.1.
M18340 mRNA. Translation: AAA42203.1.
BC089813 mRNA. Translation: AAH89813.1.
X15690 Genomic DNA. Translation: CAA33725.1.
PIRXNRTY. A23310.
RefSeqNP_036800.1. NM_012668.2.
UniGeneRn.9947.

3D structure databases

ProteinModelPortalP04694.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP04694.
ChEMBLCHEMBL5947.

PTM databases

PhosphoSiteP04694.

Proteomic databases

PRIDEP04694.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000022721; ENSRNOP00000022721; ENSRNOG00000016348.
GeneID24813.
KEGGrno:24813.
UCSCRGD:3820. rat.

Organism-specific databases

CTD6898.
RGD3820. Tat.

Phylogenomic databases

eggNOGCOG0436.
GeneTreeENSGT00650000093238.
HOGENOMHOG000239005.
HOVERGENHBG004318.
InParanoidP04694.
KOK00815.
OMAFRVVITV.
OrthoDBEOG7PVWP7.
PhylomeDBP04694.
TreeFamTF105999.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15101.
BRENDA2.6.1.5. 5301.
SABIO-RKP04694.
UniPathwayUPA00139; UER00338.

Gene expression databases

GenevestigatorP04694.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR011715. Tyr_aminoTrfase_ubiquitination.
IPR005958. TyrNic_aminoTrfase.
IPR005957. Tyrosine_aminoTrfase.
IPR021178. Tyrosine_transaminase.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
PF07706. TAT_ubiq. 1 hit.
[Graphical view]
PIRSFPIRSF000517. Tyr_transaminase. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01264. tyr_amTase_E. 1 hit.
TIGR01265. tyr_nico_aTase. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio604502.
PROP04694.

Entry information

Entry nameATTY_RAT
AccessionPrimary (citable) accession number: P04694
Secondary accession number(s): Q5EBB6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 124 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

PATHWAY comments

Index of metabolic and biosynthesis pathways