ID   ARAT1_THELN             Reviewed;         417 AA.
AC   H3ZPL1; Q9UWK9;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Aromatic-amino-acid aminotransferase 1;
DE            Short=ARAT-I;
DE            Short=AROAT;
DE            EC=2.6.1.57;
GN   ORFNames=OCC_04335;
OS   Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX   PubMed=22493191; DOI=10.1128/jb.00123-12;
RA   Gardner A.F., Kumar S., Perler F.B.;
RT   "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT   litoralis NS-C.";
RL   J. Bacteriol. 194:2375-2376(2012).
RN   [2]
RP   PROTEIN SEQUENCE OF 8-34, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX   PubMed=8125113; DOI=10.1111/j.1432-1033.1994.tb18654.x;
RA   Andreotti G., Cubellis M.V., Nitti G., Sannia G., Mai X., Marino G.,
RA   Adams M.W.;
RT   "Characterization of aromatic aminotransferases from the hyperthermophilic
RT   archaeon Thermococcus litoralis.";
RL   Eur. J. Biochem. 220:543-549(1994).
CC   -!- FUNCTION: Catalyzes the transamination of phenylalanine, tyrosine and
CC       tryptophan. Shows virtually no activity towards aspartic acid, alanine,
CC       valine or isoleucine. {ECO:0000269|PubMed:8125113}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic
CC         oxo-acid + L-glutamate; Xref=Rhea:RHEA:17533, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:73309, ChEBI:CHEBI:84824; EC=2.6.1.57;
CC         Evidence={ECO:0000269|PubMed:8125113};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000305|PubMed:8125113};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.55 mM for phenylalanine {ECO:0000269|PubMed:8125113};
CC         KM=2.39 mM for tyrosine {ECO:0000269|PubMed:8125113};
CC         KM=1.47 mM for tryptophan {ECO:0000269|PubMed:8125113};
CC         KM=0.44 mM for 2-oxoglutarate {ECO:0000269|PubMed:8125113};
CC       Temperature dependence:
CC         Optimum temperature is 95-100 degrees Celsius.
CC         {ECO:0000269|PubMed:8125113};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8125113}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; CP006670; EHR78055.1; -; Genomic_DNA.
DR   PIR; S42354; S42354.
DR   RefSeq; WP_004069050.1; NC_022084.1.
DR   AlphaFoldDB; H3ZPL1; -.
DR   SMR; H3ZPL1; -.
DR   STRING; 523849.OCC_04335; -.
DR   EnsemblBacteria; EHR78055; EHR78055; OCC_04335.
DR   GeneID; 16548664; -.
DR   KEGG; tlt:OCC_04335; -.
DR   HOGENOM; CLU_017584_0_6_2; -.
DR   OMA; MRLNFTY; -.
DR   OrthoDB; 51060at2157; -.
DR   Proteomes; UP000015502; Chromosome.
DR   GO; GO:0080130; F:L-phenylalanine: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   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Direct protein sequencing; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..417
FT                   /note="Aromatic-amino-acid aminotransferase 1"
FT                   /id="PRO_0000429269"
FT   MOD_RES         258
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        19
FT                   /note="E -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        30
FT                   /note="K -> R (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   417 AA;  47610 MW;  EED16AD708D2346E CRC64;
     MELEKRLKEK LEAPTLDYEK YFSEKALGMK ASEIRELLKL VETSDVISLA GGLPAPETFP
     VEIIGEITKE VLEKHAAQAL QYGTTKGFTP LRLALAEWMR ERYDIPISKV DIMTTSGSQQ
     ALDLIGRVFI NPGDIIVVEA PTYLAALQAF KYYEPEFVQI PLDDEGMNVD LLEEKLQELE
     KEGKKVKIVY TIPTFQNPAG VTMNEKRRKR LLELASQYDF IIVEDNPYGE LRYSGEPVKP
     IKAWDEEGRV IYLGTFSKIL APGFRIGWIA AEPHFIRKLE IAKQSVDLCT NTFSQVIAWK
     YVEGGYLDKH IPKIIEFYKP RRDAMLKALE EFMPDGVKWT KPEGGMFVWA TLPEGIDTKL
     MLEKAVAKGV AYVPGEAFFA HRDVKNTMRL NFTYVPEEKI REGIKRLAET IKEEMKK