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P04694

- ATTY_RAT

UniProt

P04694 - ATTY_RAT

Protein

Tyrosine aminotransferase

Gene

Tat

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    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 phosphate.2 Publications

    Kineticsi

    1. KM=2.2 mM for tyrosine1 Publication

    Pathwayi

    GO - Molecular functioni

    1. amino acid binding Source: RGD
    2. L-phenylalanine:2-oxoglutarate aminotransferase activity Source: UniProtKB-EC
    3. L-tyrosine:2-oxoglutarate aminotransferase activity Source: UniProtKB
    4. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: Ensembl
    2. cellular amino acid metabolic process Source: RGD
    3. gluconeogenesis Source: RGD
    4. glutamate metabolic process Source: UniProtKB
    5. L-phenylalanine catabolic process Source: UniProtKB-UniPathway
    6. response to glucocorticoid Source: RGD
    7. response to mercury ion Source: RGD
    8. response to organic cyclic compound Source: RGD
    9. response to oxidative stress Source: RGD
    10. tyrosine catabolic process Source: UniProtKB

    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_204731. 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: Chromosome 19

    Organism-specific databases

    RGDi3820. Tat.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: RGD

    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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP04694.

    PTM databases

    PhosphoSiteiP04694.

    Expressioni

    Tissue specificityi

    Liver.

    Gene expression databases

    GenevestigatoriP04694.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP04694.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0436.
    GeneTreeiENSGT00650000093238.
    HOGENOMiHOG000239005.
    HOVERGENiHBG004318.
    InParanoidiP04694.
    KOiK00815.
    OMAiHCAEGSQ.
    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.
    IPR021178. Tyrosine_transaminase.
    [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

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    MDSYVIQTDV DDSLSSVLDV HVNIGGRNSV QGRKKGRKAR WDVRPSDMSN    50
    KTFNPIRAIV DNMKVQPNPN KTVISLSIGD PTVFGNLPTD PEVTQAMKDA 100
    LDSGKYNGYA PSIGYLSSRE EVASYYHCHE APLEAKDVIL TSGCSQAIEL 150
    CLAVLANPGQ NILIPRPGFS LYRTLAESMG IEVKLYNLLP EKSWEIDLKQ 200
    LESLIDEKTA CLVVNNPSNP CGSVFSKRHL QKILAVAERQ CVPILADEIY 250
    GDMVFSDCKY EPLANLSTNV PILSCGGLAK RWLVPGWRLG WILIHDRRDI 300
    FGNEIRDGLV KLSQRILGPC TIVQGALKSI LQRTPQEFYH DTLSFLKSNA 350
    DLCYGALAAI PGLQPVRPSG AMYLMVGIEM EHFPEFENDV EFTERLIAEQ 400
    AVHCLPATCF EYPNFFRVVI TVPEVMMLEA CSRIQEFCEQ HYHCAEGSQE 450
    ECDK 454
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02741 mRNA. Translation: CAA26519.1 .
    M18340 mRNA. Translation: AAA42203.1 .
    BC089813 mRNA. Translation: AAH89813.1 .
    X15690 Genomic DNA. Translation: CAA33725.1 .
    PIRi A23310. XNRTY.
    RefSeqi NP_036800.1. NM_012668.2.
    UniGenei Rn.9947.

    3D structure databases

    ProteinModelPortali P04694.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P04694.
    ChEMBLi CHEMBL5947.

    PTM databases

    PhosphoSitei P04694.

    Proteomic databases

    PRIDEi P04694.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000022721 ; ENSRNOP00000022721 ; ENSRNOG00000016348 .
    GeneIDi 24813.
    KEGGi rno:24813.
    UCSCi RGD:3820. rat.

    Organism-specific databases

    CTDi 6898.
    RGDi 3820. Tat.

    Phylogenomic databases

    eggNOGi COG0436.
    GeneTreei ENSGT00650000093238.
    HOGENOMi HOG000239005.
    HOVERGENi HBG004318.
    InParanoidi P04694.
    KOi K00815.
    OMAi HCAEGSQ.
    OrthoDBi EOG7PVWP7.
    PhylomeDBi P04694.
    TreeFami TF105999.

    Enzyme and pathway databases

    UniPathwayi UPA00139 ; UER00338 .
    BioCyci MetaCyc:MONOMER-15101.
    BRENDAi 2.6.1.5. 5301.
    Reactomei REACT_204731. Phenylalanine and tyrosine catabolism.
    SABIO-RK P04694.

    Miscellaneous databases

    NextBioi 604502.
    PROi P04694.

    Gene expression databases

    Genevestigatori P04694.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR004839. 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 ]
    Pfami PF00155. Aminotran_1_2. 1 hit.
    PF07706. TAT_ubiq. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000517. Tyr_transaminase. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR01264. tyr_amTase_E. 1 hit.
    TIGR01265. tyr_nico_aTase. 1 hit.
    PROSITEi PS00105. AA_TRANSFER_CLASS_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 128 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