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Protein

Tyrosine aminotransferase

Gene

Tat

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate.1 Publication

Cofactori

pyridoxal 5'-phosphate2 Publications

Kineticsi

  1. KM=2.2 mM for tyrosine1 Publication

    Pathway:iL-phenylalanine degradation

    This protein is involved in step 2 of the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine.
    Proteins known to be involved in the 6 steps of the subpathway in this organism are:
    1. Phenylalanine-4-hydroxylase (Pah)
    2. Tyrosine aminotransferase (Tat)
    3. 4-hydroxyphenylpyruvate dioxygenase (Hpd)
    4. no protein annotated in this organism
    5. Maleylacetoacetate isomerase (Gstz1)
    6. Fumarylacetoacetase (Fah)
    This subpathway is part of the pathway L-phenylalanine degradation, which is itself part of Amino-acid degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine, the pathway L-phenylalanine degradation and in Amino-acid degradation.

    GO - Molecular functioni

    GO - Biological processi

    • 2-oxoglutarate metabolic process Source: Ensembl
    • cellular amino acid metabolic process Source: RGD
    • gluconeogenesis Source: RGD
    • glutamate metabolic process Source: UniProtKB
    • L-phenylalanine catabolic process Source: UniProtKB-UniPathway
    • response to glucocorticoid Source: RGD
    • response to mercury ion Source: RGD
    • response to organic cyclic compound Source: RGD
    • response to oxidative stress Source: RGD
    • tyrosine catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Biological processi

    Phenylalanine catabolism, Tyrosine catabolism

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15101.
    BRENDAi2.6.1.5. 5301.
    ReactomeiREACT_306066. Phenylalanine and tyrosine catabolism.
    SABIO-RKP04694.
    UniPathwayiUPA00139; UER00338.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine aminotransferase (EC:2.6.1.5)
    Short name:
    TAT
    Alternative name(s):
    L-tyrosine:2-oxoglutarate aminotransferase
    Gene namesi
    Name:Tat
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494 Componenti: Chromosome 19

    Organism-specific databases

    RGDi3820. Tat.

    Subcellular locationi

    GO - Cellular componenti

    • mitochondrion Source: RGD
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 454454Tyrosine aminotransferasePRO_0000123889Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei280 – 2801N6-(pyridoxal phosphate)lysine1 Publication
    Modified residuei448 – 4481PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiP04694.

    PTM databases

    PhosphoSiteiP04694.

    Expressioni

    Tissue specificityi

    Liver.

    Gene expression databases

    GenevisibleiP04694. RN.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000022721.

    Structurei

    3D structure databases

    ProteinModelPortaliP04694.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0436.
    GeneTreeiENSGT00650000093238.
    HOGENOMiHOG000239005.
    HOVERGENiHBG004318.
    InParanoidiP04694.
    KOiK00815.
    OMAiNADLCYA.
    OrthoDBiEOG7PVWP7.
    PhylomeDBiP04694.
    TreeFamiTF105999.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004839. 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.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    PF07706. TAT_ubiq. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000517. Tyr_transaminase. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR01264. tyr_amTase_E. 1 hit.
    TIGR01265. tyr_nico_aTase. 1 hit.
    PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P04694-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDSYVIQTDV DDSLSSVLDV HVNIGGRNSV QGRKKGRKAR WDVRPSDMSN
    60 70 80 90 100
    KTFNPIRAIV DNMKVQPNPN KTVISLSIGD PTVFGNLPTD PEVTQAMKDA
    110 120 130 140 150
    LDSGKYNGYA PSIGYLSSRE EVASYYHCHE APLEAKDVIL TSGCSQAIEL
    160 170 180 190 200
    CLAVLANPGQ NILIPRPGFS LYRTLAESMG IEVKLYNLLP EKSWEIDLKQ
    210 220 230 240 250
    LESLIDEKTA CLVVNNPSNP CGSVFSKRHL QKILAVAERQ CVPILADEIY
    260 270 280 290 300
    GDMVFSDCKY EPLANLSTNV PILSCGGLAK RWLVPGWRLG WILIHDRRDI
    310 320 330 340 350
    FGNEIRDGLV KLSQRILGPC TIVQGALKSI LQRTPQEFYH DTLSFLKSNA
    360 370 380 390 400
    DLCYGALAAI PGLQPVRPSG AMYLMVGIEM EHFPEFENDV EFTERLIAEQ
    410 420 430 440 450
    AVHCLPATCF EYPNFFRVVI TVPEVMMLEA CSRIQEFCEQ HYHCAEGSQE

    ECDK
    Length:454
    Mass (Da):50,635
    Last modified:August 13, 1987 - v1
    Checksum:i835EBE0D2476AF71
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti59 – 602IV → KT in AAA42203 (PubMed:2562840).Curated
    Sequence conflicti209 – 2102TA → LE in AAA42203 (PubMed:2562840).Curated
    Sequence conflicti285 – 2851P → L in CAA33725 (PubMed:1983704).Curated
    Sequence conflicti304 – 3041Missing in CAA33725 (PubMed:1983704).Curated
    Sequence conflicti359 – 3602AI → DL in AAA42203 (PubMed:2562840).Curated
    Sequence conflicti445 – 4451A → D in AAA42203 (PubMed:2562840).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X02741 mRNA. Translation: CAA26519.1.
    M18340 mRNA. Translation: AAA42203.1.
    BC089813 mRNA. Translation: AAH89813.1.
    X15690 Genomic DNA. Translation: CAA33725.1.
    PIRiA23310. XNRTY.
    RefSeqiNP_036800.1. NM_012668.2.
    UniGeneiRn.9947.

    Genome annotation databases

    EnsembliENSRNOT00000022721; ENSRNOP00000022721; ENSRNOG00000016348.
    GeneIDi24813.
    KEGGirno:24813.
    UCSCiRGD:3820. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X02741 mRNA. Translation: CAA26519.1.
    M18340 mRNA. Translation: AAA42203.1.
    BC089813 mRNA. Translation: AAH89813.1.
    X15690 Genomic DNA. Translation: CAA33725.1.
    PIRiA23310. XNRTY.
    RefSeqiNP_036800.1. NM_012668.2.
    UniGeneiRn.9947.

    3D structure databases

    ProteinModelPortaliP04694.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000022721.

    Chemistry

    BindingDBiP04694.
    ChEMBLiCHEMBL5947.

    PTM databases

    PhosphoSiteiP04694.

    Proteomic databases

    PRIDEiP04694.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000022721; ENSRNOP00000022721; ENSRNOG00000016348.
    GeneIDi24813.
    KEGGirno:24813.
    UCSCiRGD:3820. rat.

    Organism-specific databases

    CTDi6898.
    RGDi3820. Tat.

    Phylogenomic databases

    eggNOGiCOG0436.
    GeneTreeiENSGT00650000093238.
    HOGENOMiHOG000239005.
    HOVERGENiHBG004318.
    InParanoidiP04694.
    KOiK00815.
    OMAiNADLCYA.
    OrthoDBiEOG7PVWP7.
    PhylomeDBiP04694.
    TreeFamiTF105999.

    Enzyme and pathway databases

    UniPathwayiUPA00139; UER00338.
    BioCyciMetaCyc:MONOMER-15101.
    BRENDAi2.6.1.5. 5301.
    ReactomeiREACT_306066. Phenylalanine and tyrosine catabolism.
    SABIO-RKP04694.

    Miscellaneous databases

    NextBioi604502.
    PROiP04694.

    Gene expression databases

    GenevisibleiP04694. RN.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004839. 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.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    PF07706. TAT_ubiq. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000517. Tyr_transaminase. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR01264. tyr_amTase_E. 1 hit.
    TIGR01265. tyr_nico_aTase. 1 hit.
    PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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], ACETYLATION AT MET-1.
    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.

    Entry informationi

    Entry nameiATTY_RAT
    AccessioniPrimary (citable) accession number: P04694
    Secondary accession number(s): Q5EBB6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: July 22, 2015
    This is version 134 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.