Tyrosine aminotransferase - Homo sapiens (Human)

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

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	454 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate.
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 2/6.
Subunit structure	Homodimer By similarity.
Involvement in disease	Defects in TAT are the cause of tyrosinemia type 2 (TYRO2) [MIM:276600]; also known as Richner-Hanhart syndrome. TYRO2 is an inborn error of metabolism characterized by elevations of tyrosine in the blood and urine, and oculocutaneous manifestations. Typical features include palmoplantar keratosis, painful corneal ulcers, and mental retardation. Ref.7
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

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Ontologies

Keywords
Biological process	Phenylalanine catabolism Tyrosine catabolism
Coding sequence diversity	Polymorphism
Disease	Disease mutation Mental retardation Palmoplantar keratoderma
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	L-phenylalanine catabolic process Non-traceable author statement. Source: UniProtKB biosynthetic process Inferred from electronic annotation. Source: InterPro tyrosine catabolic process Non-traceable author statement. Source: UniProtKB
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Inferred from electronic annotation. Source: InterPro L-tyrosine:2-oxoglutarate aminotransferase activity Ref.1 Non-traceable author statement. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 454

454

Tyrosine aminotransferase

PRO_0000123887

Amino acid modifications

Modified residue

280

1

N6-(pyridoxal phosphate)lysine

Natural variations

Natural variant

70

1

N → D: dbSNP rs16973344.

VAR_048226

Natural variant

362

1

G → V in TYRO2. dbSNP rs28934277.

VAR_000560

Secondary structure

1

.

454

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P17735-1 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 82B5B24F3B2CE489
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FASTA

454

50,399

        10         20         30         40         50         60 
MDPYMIQMSS KGNLPSILDV HVNVGGRSSV PGKMKGRKAR WSVRPSDMAK KTFNPIRAIV 

        70         80         90        100        110        120 
DNMKVKPNPN KTMISLSIGD PTVFGNLPTD PEVTQAMKDA LDSGKYNGYA PSIGFLSSRE 

       130        140        150        160        170        180 
EIASYYHCPE APLEAKDVIL TSGCSQAIDL CLAVLANPGQ NILVPRPGFS LYKTLAESMG 

       190        200        210        220        230        240 
IEVKLYNLLP EKSWEIDLKQ LEYLIDEKTA CLIVNNPSNP CGSVFSKRHL QKILAVAARQ 

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

       310        320        330        340        350        360 
FGNEIRDGLV KLSQRILGPC TIVQGALKSI LCRTPGEFYH NTLSFLKSNA DLCYGALAAI 

       370        380        390        400        410        420 
PGLRPVRPSG AMYLMVGIEM EHFPEFENDV EFTERLVAEQ SVHCLPATCF EYPNFIRVVI 

       430        440        450 
TVPEVMMLEA CSRIQEFCEQ HYHCAEGSQE ECDK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the human tyrosine aminotransferase gene." Rettenmeier R., Natt E., Zentgraf H., Scherer G. Nucleic Acids Res. 18:3853-3861(1990) [PubMed: 1973834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Nucleotide sequence of the human tyrosine aminotransferase gene." Zelenin S.M., Mertvetsov N.P. Bioorg. Khim. 20:196-204(1994) [PubMed: 7908801] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Cloning and expression of human tyrosine aminotransferase cDNA." Seralini G.E., Luu-The V., Labrie F. Biochim. Biophys. Acta 1260:97-101(1995) [PubMed: 7999802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Human tyrosine aminotransferase." Structural genomics consortium (SGC) Submitted (AUG-2008) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 38-444 IN COMPLEX WITH PYRIDOXAL PHOSPHATE.
[7]	"Point mutations in the tyrosine aminotransferase gene in tyrosinemia type II." Natt E., Kida K., Odievre M., di Rocco M., Scherer G. Proc. Natl. Acad. Sci. U.S.A. 89:9297-9301(1992) [PubMed: 1357662] [Abstract] Cited for: VARIANT TYRO2 VAL-362.
+	Additional computationally mapped references.

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Web resources

GeneReviews

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Cross-references

Sequence databases

X52520 mRNA. Translation: CAA36750.1.
X52509

X52519 Genomic DNA. Translation: CAA36749.1.
X55675 mRNA. Translation: CAA39210.1.
AK313380 mRNA. Translation: BAG36178.1.
CH471166 Genomic DNA. Translation: EAW59230.1.

IPI

IPI00016764.

PIR

S10887.

RefSeq

NP_000344.1.

UniGene

Hs.161640

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DYD	X-ray	2.30	A/B	41-444	[»]

ModBase

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Protein-protein interaction databases

STRING

P17735.

Proteomic databases

PRIDE

P17735.

Genome annotation databases

Ensembl

ENST00000355962; ENSP00000348234; ENSG00000198650; Homo sapiens. [Genome view]

GeneID

6898.

KEGG

hsa:6898.

UCSC

uc002fap.2. human.

Organism-specific databases

CTD

6898.

GeneCards

GC16M070158.

H-InvDB

HIX0038602.

HGNC

HGNC:11573. TAT.

MIM

276600. gene+phenotype.

Orphanet

28378. Tyrosinemia, type 2.

PharmGKB

PA36338.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P17735.

HOVERGEN

P17735.

OMA

CVPILAD

OrthoDB

EOG9MSGJ9

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-12018.

BRENDA

2.6.1.5. 247.

Pathway_Interaction_DB

hnf3bpathway. FOXA2 and FOXA3 transcription factor networks.

Reactome

REACT_13. Metabolism of amino acids.

Gene expression databases

ArrayExpress

P17735.

Bgee

P17735.

CleanEx

HS_TAT.

Genevestigator

P17735.

GermOnline

ENSG00000198650. Homo sapiens.

Family and domain databases

InterPro

IPR001176. ACC_synthase.
IPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase_major.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR011715. Tyr_aa_trans_ubi.
IPR005958. TyrNic_aminoTrfase.
IPR005957. Tyrosine_aminoTrfase.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.

Pfam

PF00155. Aminotran_1_2. 1 hit.
PF07706. TAT_ubiq. 1 hit.
[Graphical view]

PRINTS

PR00753. ACCSYNTHASE.

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 Resources

DrugBank

DB00142. L-Glutamic Acid.
DB00120. L-Phenylalanine.
DB00135. L-Tyrosine.
DB00114. Pyridoxal Phosphate.

NextBio

26963.

SOURCE

Search...

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Entry information

Entry name

ATTY_HUMAN

Accession

Primary (citable) accession number: P17735
Secondary accession number(s): B2R8I1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	November 24, 2009
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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