ARAT2_THELN
ID ARAT2_THELN Reviewed; 389 AA.
AC H3ZPU1; Q9UWK8;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Aromatic-amino-acid aminotransferase 2;
DE Short=ARAT-II;
DE Short=AROAT;
DE EC=2.6.1.57;
GN ORFNames=OCC_04737;
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 2-31, 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=1.55 mM for phenylalanine {ECO:0000269|PubMed:8125113};
CC KM=2.37 mM for tyrosine {ECO:0000269|PubMed:8125113};
CC KM=4.62 mM for tryptophan {ECO:0000269|PubMed:8125113};
CC KM=0.49 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; EHR77995.1; -; Genomic_DNA.
DR PIR; S42364; S42364.
DR RefSeq; WP_004069212.1; NC_022084.1.
DR AlphaFoldDB; H3ZPU1; -.
DR SMR; H3ZPU1; -.
DR STRING; 523849.OCC_04737; -.
DR EnsemblBacteria; EHR77995; EHR77995; OCC_04737.
DR GeneID; 16550508; -.
DR KEGG; tlt:OCC_04737; -.
DR HOGENOM; CLU_017584_4_3_2; -.
DR OMA; IHMEVGQ; -.
DR OrthoDB; 32104at2157; -.
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; 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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Direct protein sequencing; Pyridoxal phosphate;
KW Transferase.
FT CHAIN 1..389
FT /note="Aromatic-amino-acid aminotransferase 2"
FT /id="PRO_0000429270"
FT MOD_RES 233
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="A -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="R -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 14..16
FT /note="EIR -> WIA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 44105 MW; B99F0D922CB62699 CRC64;
MALSDRLEMV NPSEIRKLFD LAQGIEGIIS LGIGEPDFDT PEHIKEYAKE ALDKGLTHYS
PNIGILELRE AVAEKFKKHN GIDADPKTQI MITVGTNQQI LMGLATFLKD NEEVLIPSPM
FVSYAPAVIL AGGKPVEVPT YEENEFRLSV DELEKYVTPK TRALIINTPN NPTGAVLTKK
DLEEIADFAV EHDLMILSDE VYEYFVYDGV KNYSIASLDG MFERTITMNG FSKTFAMTGW
RLGFLAAPEW VVEKMVRFQM YNATCPVTFI QYAAAKALRD ERSWQAVEEM RREYERRRNL
VWKRLNEMGL PTVKPKGAFY IFPRIKDTGL SSKEFSELMI KEAKVVVVPG SAFGQAGEGY
VRISYATAYE KLEEAMDRME KVLKEKKLV
