ATTY_TRYCR
ID ATTY_TRYCR Reviewed; 416 AA.
AC P33447;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Tyrosine aminotransferase;
DE Short=TAT;
DE EC=2.6.1.5;
DE AltName: Full=L-tyrosine:2-oxoglutarate aminotransferase;
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8101971; DOI=10.1016/0166-6851(93)90223-k;
RA Bontempi E.J., Bua J., Aaslund L., Porcel B., Henriksson J., Pettersson U.,
RA Segura E.L., Oern A., Ruiz A.M.;
RT "Isolation and characterization of a gene from Trypanosoma cruzi encoding a
RT 46-kilodalton protein with homology to human and rat tyrosine
RT aminotransferase.";
RL Mol. Biochem. Parasitol. 59:253-262(1993).
RN [2]
RP PROTEIN SEQUENCE OF 120-148; 153-167 AND 324-338, AND CHARACTERIZATION.
RC STRAIN=Tulahuen 0;
RX PubMed=8100416; DOI=10.1042/bj2920901;
RA Montemartini M., Santome J.A., Cazzulo J.J., Nowicki C.;
RT "Purification and partial structural and kinetic characterization of
RT tyrosine aminotransferase from epimastigotes of Trypanosoma cruzi.";
RL Biochem. J. 292:901-906(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP SUBUNIT, AND COFACTOR.
RX PubMed=10595543; DOI=10.1110/ps.8.11.2406;
RA Blankenfeldt W., Nowicki C., Montemartini-Kalisz M., Kalisz H.M.,
RA Hecht H.-J.;
RT "Crystal structure of Trypanosoma cruzi tyrosine aminotransferase:
RT substrate specificity is influenced by cofactor binding mode.";
RL Protein Sci. 8:2406-2417(1999).
CC -!- FUNCTION: Transaminase involved in tyrosine breakdown. Converts
CC tyrosine to p-hydroxyphenylpyruvate (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-
CC glutamate; Xref=Rhea:RHEA:15093, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; EC=2.6.1.5;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:10595543};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 2/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10595543}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. Note=Mainly
CC cytoplasmic. Present to a small extent in the mitochondrial fraction.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to have three internal disulfide bonds.
CC {ECO:0000305|PubMed:8100416}.
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DR EMBL; L00673; AAA02975.1; -; Unassigned_DNA.
DR PDB; 1BW0; X-ray; 2.50 A; A/B=1-416.
DR PDBsum; 1BW0; -.
DR AlphaFoldDB; P33447; -.
DR SMR; P33447; -.
DR DrugBank; DB04083; N(6)-(pyridoxal phosphate)-L-lysine.
DR VEuPathDB; TriTrypDB:BCY84_12535; -.
DR VEuPathDB; TriTrypDB:BCY84_22838; -.
DR VEuPathDB; TriTrypDB:BCY84_22841; -.
DR VEuPathDB; TriTrypDB:BCY84_22844; -.
DR VEuPathDB; TriTrypDB:BCY84_22847; -.
DR VEuPathDB; TriTrypDB:BCY84_22850; -.
DR VEuPathDB; TriTrypDB:BCY84_22853; -.
DR VEuPathDB; TriTrypDB:BCY84_22856; -.
DR VEuPathDB; TriTrypDB:BCY84_22862; -.
DR VEuPathDB; TriTrypDB:C3747_114g58; -.
DR VEuPathDB; TriTrypDB:C4B63_101g1; -.
DR VEuPathDB; TriTrypDB:C4B63_101g2; -.
DR VEuPathDB; TriTrypDB:C4B63_26g354; -.
DR VEuPathDB; TriTrypDB:C4B63_54g138; -.
DR VEuPathDB; TriTrypDB:C4B63_81g64; -.
DR VEuPathDB; TriTrypDB:C4B63_81g65; -.
DR VEuPathDB; TriTrypDB:C4B63_81g66; -.
DR VEuPathDB; TriTrypDB:C4B63_81g67; -.
DR VEuPathDB; TriTrypDB:C4B63_81g68; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_1849; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0018030; -.
DR VEuPathDB; TriTrypDB:TcCL_ESM10819; -.
DR VEuPathDB; TriTrypDB:TcCLB.508535.50; -.
DR VEuPathDB; TriTrypDB:TcCLB.510187.40; -.
DR VEuPathDB; TriTrypDB:TcCLB.510565.11; -.
DR VEuPathDB; TriTrypDB:TCDM_06595; -.
DR VEuPathDB; TriTrypDB:TcG_12830; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_005122; -.
DR VEuPathDB; TriTrypDB:TcYC6_0085550; -.
DR BRENDA; 2.6.1.5; 6524.
DR SABIO-RK; P33447; -.
DR UniPathway; UPA00139; UER00338.
DR EvolutionaryTrace; P33447; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR005958; TyrNic_aminoTrfase.
DR InterPro; IPR005957; Tyrosine_aminoTrfase.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PIRSF; PIRSF000517; Tyr_transaminase; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01264; tyr_amTase_E; 1.
DR TIGRFAMs; TIGR01265; tyr_nico_aTase; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Cytoplasm; Direct protein sequencing;
KW Mitochondrion; Phenylalanine catabolism; Pyridoxal phosphate; Transferase;
KW Tyrosine catabolism.
FT CHAIN 1..416
FT /note="Tyrosine aminotransferase"
FT /id="PRO_0000123890"
FT MOD_RES 253
FT /note="N6-(pyridoxal phosphate)lysine"
FT CONFLICT 153
FT /note="H -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:1BW0"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:1BW0"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 78..92
FT /evidence="ECO:0007829|PDB:1BW0"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1BW0"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:1BW0"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:1BW0"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:1BW0"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:1BW0"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:1BW0"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:1BW0"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:1BW0"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:1BW0"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 275..288
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 293..304
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 308..329
FT /evidence="ECO:0007829|PDB:1BW0"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1BW0"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:1BW0"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 361..372
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 379..382
FT /evidence="ECO:0007829|PDB:1BW0"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:1BW0"
FT HELIX 396..413
FT /evidence="ECO:0007829|PDB:1BW0"
SQ SEQUENCE 416 AA; 46167 MW; 1D31564359C463C4 CRC64;
MSSWDVSMSN HAGLVFNPIR TVSDNAKPSP SPKPIIKLSV GDPTLDKNLL TSAAQIKKLK
EAIDSQECNG YFPTVGSPEA REAVATWWRN SFVHKEELKS TIVKDNVVLC SGGSHGILMA
ITAICDAGDY ALVPQPGFPH YETVCKAYGI GMHFYNCRPE NDWEADLDEI RRLKDDKTKL
LIVTNPSNPC GSNFSRKHVE DIVRLAEELR LPLFSDEIYA GMVFKGKDPN ATFTSVADFE
TTVPRVILGG TAKNLVVPGW RLGWLLYVDP HGNGPSFLEG LKRVGMLVCG PCTVVQAALG
EALLNTPQEH LDQIVAKIEE SAMYLYNHIG ECIGLAPTMP RGAMYLMSRI DLEKYRDIKT
DVEFFEKLLE EENVQVLPGT IFHAPGFTRL TTTRPVEVYR EAVERIKAFC QRHAAV
