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Protein

Tyrosine aminotransferase

Gene

Tat

Organism
Mus musculus (Mouse)
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 for phenylalanine.1 Publication

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphate1 Publication

Kineticsi

  1. KM=1.8 mM for tyrosine1 Publication
  2. KM=4.9 mM for glutamate1 Publication
  3. KM=11.4 mM for phenylalanine1 Publication
  4. KM=1.8 mM for 2-oxoglutarate1 Publication
  5. KM=0.7 mM for p-hydroxyphenylpyruvate1 Publication

    pH dependencei

    Optimum pH is 7.1 Publication

    Temperature dependencei

    Optimum temperature is 55-70 degrees Celsius.1 Publication

    Pathwayi: L-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. Homogentisate 1,2-dioxygenase (Hgd)
    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: UniProtKB
    • biosynthetic process Source: InterPro
    • glutamate metabolic process Source: UniProtKB
    • L-phenylalanine catabolic process Source: UniProtKB-UniPathway
    • response to glucocorticoid Source: Ensembl
    • response to mercury ion Source: Ensembl
    • response to oxidative stress Source: Ensembl
    • 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

    ReactomeiR-MMU-71182. Phenylalanine and tyrosine catabolism.
    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 8

    Organism-specific databases

    MGIiMGI:98487. Tat.

    Subcellular locationi

    GO - Cellular componenti

    • mitochondrion Source: MGI
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 454454Tyrosine aminotransferasePRO_0000123888Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiQ8QZR1.
    MaxQBiQ8QZR1.
    PaxDbiQ8QZR1.
    PRIDEiQ8QZR1.

    PTM databases

    iPTMnetiQ8QZR1.
    PhosphoSiteiQ8QZR1.

    Expressioni

    Gene expression databases

    BgeeiQ8QZR1.
    CleanExiMM_TAT.
    ExpressionAtlasiQ8QZR1. baseline and differential.
    GenevisibleiQ8QZR1. MM.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000001720.

    Structurei

    Secondary structure

    1
    454
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi83 – 875Combined sources
    Helixi91 – 10212Combined sources
    Beta strandi106 – 1083Combined sources
    Helixi116 – 12510Combined sources
    Beta strandi129 – 1313Combined sources
    Helixi135 – 1373Combined sources
    Beta strandi138 – 1436Combined sources
    Helixi144 – 15310Combined sources
    Beta strandi161 – 1644Combined sources
    Helixi170 – 17910Combined sources
    Beta strandi182 – 1854Combined sources
    Turni190 – 1945Combined sources
    Helixi198 – 2025Combined sources
    Beta strandi207 – 21711Combined sources
    Turni219 – 2213Combined sources
    Helixi227 – 23711Combined sources
    Turni238 – 2414Combined sources
    Beta strandi244 – 2474Combined sources
    Turni249 – 2524Combined sources
    Beta strandi256 – 2583Combined sources
    Helixi263 – 2664Combined sources
    Beta strandi272 – 2743Combined sources
    Helixi278 – 2814Combined sources
    Helixi285 – 2873Combined sources
    Beta strandi290 – 2956Combined sources
    Beta strandi297 – 3015Combined sources
    Helixi302 – 31312Combined sources
    Turni314 – 3163Combined sources
    Helixi321 – 33313Combined sources
    Helixi336 – 35924Combined sources
    Beta strandi373 – 3786Combined sources
    Helixi389 – 40012Combined sources
    Helixi407 – 4104Combined sources
    Beta strandi414 – 4207Combined sources
    Helixi424 – 43815Combined sources
    Turni439 – 4413Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3PDXX-ray2.91A41-442[»]
    ProteinModelPortaliQ8QZR1.
    SMRiQ8QZR1. Positions 64-442.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8QZR1.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG0259. Eukaryota.
    COG0436. LUCA.
    GeneTreeiENSGT00650000093238.
    HOGENOMiHOG000239005.
    HOVERGENiHBG004318.
    InParanoidiQ8QZR1.
    KOiK00815.
    OMAiYMRLVIT.
    OrthoDBiEOG7PVWP7.
    PhylomeDBiQ8QZR1.
    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.

    Q8QZR1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDSYVIQTNV NDSLPSVLDV RVNIGGRSSV QGRAKGRKAR WNVRPSDMSN
    60 70 80 90 100
    KTFNPIRAIV DNMKVKPNPN KTVISLSIGD PTVFGNLPTD PEVTQAMKDA
    110 120 130 140 150
    LDSGKYNGYA PSIGYLSSRE EVASYYHCPE 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 EPMATLSTNV PILSCGGLAK RWLVPGWRLG WILIHDRRDI
    310 320 330 340 350
    FGNEIRDGLV KLSQRILGPC TIVQGALKSI LQRTPQEFYQ DTLSFLKSNA
    360 370 380 390 400
    DLCYGALSAI PGLQPVRPSG AMYLMVGIEM EHFPEFENDV EFTERLIAEQ
    410 420 430 440 450
    SVHCLPATCF EYPNFFRVVI TVPEVMMLEA CSRIQEFCEQ HYHCAEGSQE

    ECDK
    Length:454
    Mass (Da):50,565
    Last modified:June 1, 2002 - v1
    Checksum:iCDB6E1E6CDB5DC7D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti234 – 2341L → W in BAC41146 (PubMed:16141072).Curated
    Sequence conflicti362 – 3621G → V in BAC41146 (PubMed:16141072).Curated
    Sequence conflicti378 – 3781I → M in BAC41146 (PubMed:16141072).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK090244 mRNA. Translation: BAC41146.1.
    AK149383 mRNA. Translation: BAE28844.1.
    BC023949 mRNA. Translation: AAH23949.1.
    BC024120 mRNA. Translation: AAH24120.1.
    BC024264 mRNA. Translation: AAH24264.1.
    BC025934 mRNA. Translation: AAH25934.1.
    BC028821 mRNA. Translation: AAH28821.1.
    BC030728 mRNA. Translation: AAH30728.1.
    BC030729 mRNA. Translation: AAH30729.1.
    BC037526 mRNA. Translation: AAH37526.1.
    CCDSiCCDS22658.1.
    RefSeqiNP_666326.1. NM_146214.3.
    UniGeneiMm.28110.

    Genome annotation databases

    EnsembliENSMUST00000001720; ENSMUSP00000001720; ENSMUSG00000001670.
    GeneIDi234724.
    KEGGimmu:234724.
    UCSCiuc009njs.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK090244 mRNA. Translation: BAC41146.1.
    AK149383 mRNA. Translation: BAE28844.1.
    BC023949 mRNA. Translation: AAH23949.1.
    BC024120 mRNA. Translation: AAH24120.1.
    BC024264 mRNA. Translation: AAH24264.1.
    BC025934 mRNA. Translation: AAH25934.1.
    BC028821 mRNA. Translation: AAH28821.1.
    BC030728 mRNA. Translation: AAH30728.1.
    BC030729 mRNA. Translation: AAH30729.1.
    BC037526 mRNA. Translation: AAH37526.1.
    CCDSiCCDS22658.1.
    RefSeqiNP_666326.1. NM_146214.3.
    UniGeneiMm.28110.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3PDXX-ray2.91A41-442[»]
    ProteinModelPortaliQ8QZR1.
    SMRiQ8QZR1. Positions 64-442.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000001720.

    PTM databases

    iPTMnetiQ8QZR1.
    PhosphoSiteiQ8QZR1.

    Proteomic databases

    EPDiQ8QZR1.
    MaxQBiQ8QZR1.
    PaxDbiQ8QZR1.
    PRIDEiQ8QZR1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000001720; ENSMUSP00000001720; ENSMUSG00000001670.
    GeneIDi234724.
    KEGGimmu:234724.
    UCSCiuc009njs.2. mouse.

    Organism-specific databases

    CTDi6898.
    MGIiMGI:98487. Tat.

    Phylogenomic databases

    eggNOGiKOG0259. Eukaryota.
    COG0436. LUCA.
    GeneTreeiENSGT00650000093238.
    HOGENOMiHOG000239005.
    HOVERGENiHBG004318.
    InParanoidiQ8QZR1.
    KOiK00815.
    OMAiYMRLVIT.
    OrthoDBiEOG7PVWP7.
    PhylomeDBiQ8QZR1.
    TreeFamiTF105999.

    Enzyme and pathway databases

    UniPathwayiUPA00139; UER00338.
    ReactomeiR-MMU-71182. Phenylalanine and tyrosine catabolism.

    Miscellaneous databases

    ChiTaRSiTat. mouse.
    EvolutionaryTraceiQ8QZR1.
    PROiQ8QZR1.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ8QZR1.
    CleanExiMM_TAT.
    ExpressionAtlasiQ8QZR1. baseline and differential.
    GenevisibleiQ8QZR1. MM.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Liver.
    2. "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].
      Strain: FVB/N.
      Tissue: Liver.
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    4. "Tyrosine aminotransferase: biochemical and structural properties and molecular dynamics simulations."
      Mehere P., Han Q., Lemkul J.A., Vavricka C.J., Robinson H., Bevan D.R., Li J.
      Protein Cell 1:1023-1032(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 41-442, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiATTY_MOUSE
    AccessioniPrimary (citable) accession number: Q8QZR1
    Secondary accession number(s): Q3UER7, Q8BTI1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: June 1, 2002
    Last modified: June 8, 2016
    This is version 111 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    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 one 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.