Tyrosine aminotransferase - Rattus norvegicus (Rat)

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P04694 (ATTY_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Tyrosine aminotransferase
Short name=TAT
EC=2.6.1.5

Alternative name(s):
L-tyrosine:2-oxoglutarate aminotransferase

Gene names

Name:

Tat

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	454 AA.
Sequence status	Complete.
Protein existence	Evidence 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: K_M=2.2 mM for tyrosine Ref.5

Ontologies

Keywords
Biological process	Phenylalanine catabolism Tyrosine catabolism
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	2-oxoglutarate metabolic process Inferred from electronic annotation. Source: Compara L-phenylalanine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway gluconeogenesis Traceable author statement Ref.1. Source: RGD glutamate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB response to glucocorticoid stimulus Inferred from direct assay PubMed 16307467. Source: RGD response to mercury ion Inferred from direct assay PubMed 16307467. 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_component	mitochondrion Inferred from direct assay PubMed 4390541. Source: RGD
Molecular_function	L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 454

454

Tyrosine aminotransferase

PRO_0000123889

Amino acid modifications

Modified residue

N-acetylmethionine Ref.1

Modified residue

280

N6-(pyridoxal phosphate)lysine Ref.2

Experimental info

Sequence conflict

59 – 60

IV → KT in AAA42203. Ref.2

Sequence conflict

209 – 210

TA → LE in AAA42203. Ref.2

Sequence conflict

285

P → L in CAA33725. Ref.4

Sequence conflict

304

Missing in CAA33725. Ref.4

Sequence conflict

359 – 360

AI → DL in AAA42203. Ref.2

Sequence conflict

445

A → D in AAA42203. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P04694 [UniParc].

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

454

50,635

        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' referencesShow '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, MASS SPECTROMETRY, COFACTOR.
[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.
IPI	IPI00197893.
PIR	XNRTY. A23310.
RefSeq	NP_036800.1. NM_012668.2.
UniGene	Rn.9947.
3D structure databases
ProteinModelPortal	P04694.
ModBase	Search...
PTM databases
PhosphoSite	P04694.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000022721; ENSRNOP00000022721; ENSRNOG00000016348.
GeneID	24813.
KEGG	rno:24813.
UCSC	RGD:3820. rat.
Organism-specific databases
CTD	6898.
RGD	3820. Tat.
Phylogenomic databases
eggNOG	COG0436.
GeneTree	ENSGT00650000093238.
HOGENOM	HOG000239005.
HOVERGEN	HBG004318.
InParanoid	P04694.
KO	K00815.
OMA	FIRVVIT.
OrthoDB	EOG4SQWWR.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-15101.
BRENDA	2.6.1.5. 5301.
SABIO-RK	P04694.
UniPathway	UPA00139; UER00338.
Gene expression databases
Genevestigator	P04694.
GermOnline	ENSRNOG00000016348. Rattus norvegicus.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	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]
Pfam	PF00155. Aminotran_1_2. 1 hit. PF07706. TAT_ubiq. 1 hit. [Graphical view]
PIRSF	PIRSF000517. Tyr_transaminase. 1 hit.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01264. tyr_amTase_E. 1 hit. TIGR01265. tyr_nico_aTase. 1 hit.
PROSITE	PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P04694.
ChEMBL	CHEMBL5947.
NextBio	604502.

Entry information

Entry name

ATTY_RAT

Accession

Primary (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 3, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents